|
Name |
Accession |
Description |
Interval |
E-value |
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
395-1446 |
0e+00 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 1715.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 395 PRKVLVLGSGGLSIGQAGEFDYSGSQAIKAMKEENIQTILINPNIATVQTSKGLADKVYFLPITPEYVTQVIKNERPDGV 474
Cdd:TIGR01369 6 IKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKERPDAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 475 LLTFGGQTALNCGVELKKQGVLEKYKVRVLGTPVASIEMTEDRKIFVEKMEEINEHVAPSEAAMSVEQAVAAAERLGYPV 554
Cdd:TIGR01369 86 LPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKEIGYPV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 555 LVRSAFALGGLGSGFANNRDEMITLVTQAFAHT--SQVLVDKSLKGWKEIEYEVVRDAYDNCVTVCNMENIDPLGIHTGE 632
Cdd:TIGR01369 166 IVRPAFTLGGTGGGIAYNREELKEIAERALSASpiNQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPMGVHTGD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 633 SIVVAPSQTLNDYEYNMLRNTAIKVIRHLGVVGECNIQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLS 712
Cdd:TIGR01369 246 SIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAKVAAKLA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 713 LGIPLPVLKNSVTNSTTANFEPSLDYCVVKVPRWDLSKFLRVSTKIGSSMKSVGEVMAIGRSFEEAFQKALRMVDENCVG 792
Cdd:TIGR01369 326 VGYTLDELKNPVTGTTPASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSLEIGATG 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 793 FDHTIKP-----ESEEELQTPTDKRIFVLAAALHAGYTVERLYELTKIDHWFLHKMKNIADHKKLLETYKQDEsaMPPEI 867
Cdd:TIGR01369 406 FDLPDREvepdeDLWRALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEVKLTD--LDPEL 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 868 MRKAKQLGFSDKQIAQAVQSTELAVRKLRRDWKIFPVVKQIDTVAAEWPAQTNYLYLTYHGSESDVVF-EQPHVMVIGSG 946
Cdd:TIGR01369 484 LRRAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERDDVPFtDKKKVLVLGSG 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 947 VYRIGSSVEFDWCAVGCIMELRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYEMENPEGVILSMGGQLPN 1026
Cdd:TIGR01369 564 PNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQFGGQTPL 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1027 NIAMSLHRQQCRILGTSPEFIDNAENRFKFSRMLDTIGISQPRWKELSDTESAVNFCETVGYPCLVRPSYVLSGAAMNVA 1106
Cdd:TIGR01369 644 NLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRAMEIV 723
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1107 YSDTDMEKFLSSAVAVSKEHPVVISKFIQEAKEIDVDAVACDGEVIAIAVSEHVENAGVHSGDATLVTPPQDINQKTMER 1186
Cdd:TIGR01369 724 YNEEELRRYLEEAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEEAGVHSGDSTCVLPPQTLSAEIVDR 803
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1187 IKMIVHAIGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPYVSKTLGVDLVALATRVILGEEVEAVG--LMRGNGIV 1264
Cdd:TIGR01369 804 IKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLEELGvgKEKEPKYV 883
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1265 GVKVPQFSFSRLAGADVVLGVEMTSTGEVACFGENRYEAYLKAMLSTGFKIPKKNILLSIGSYKNKSELLPTVQTLESLG 1344
Cdd:TIGR01369 884 AVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRIPKKGSVLLSVRDKDKEELLDLARKLAEKG 963
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1345 YNLYASLGTADFYTEHGVKVMAVDWPFEeesdcpnkdKQRNIMDYLEENHFDLVINLSMRNSGgrrlssFVTKGYRTRRM 1424
Cdd:TIGR01369 964 YKLYATEGTAKFLGEAGIKPELVLKVSE---------GRPNILDLIKNGEIELVINTTSKGAG------TATDGYKIRRE 1028
|
1050 1060
....*....|....*....|..
gi 822092823 1425 AIDFSVPLITDIKCTKLFVQAL 1446
Cdd:TIGR01369 1029 ALDYGVPLITTLNTAEAFAEAL 1050
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
396-1447 |
0e+00 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 1451.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 396 RKVLVLGSGGLSIGQAGEFDYSGSQAIKAMKEENIQTILINPNIATVQTSKGLADKVYFLPITPEYVTQVIKNERPDGVL 475
Cdd:PRK05294 8 KKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEKERPDAIL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 476 LTFGGQTALNCGVELKKQGVLEKYKVRVLGTPVASIEMTEDRKIFVEKMEEINEHVAPSEAAMSVEQAVAAAERLGYPVL 555
Cdd:PRK05294 88 PTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVAEEIGYPVI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 556 VRSAFALGGLGSGFANNRDEMITLVTQAFAH--TSQVLVDKSLKGWKEIEYEVVRDAYDNCVTVCNMENIDPLGIHTGES 633
Cdd:PRK05294 168 IRPSFTLGGTGGGIAYNEEELEEIVERGLDLspVTEVLIEESLLGWKEYEYEVMRDKNDNCIIVCSIENIDPMGVHTGDS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 634 IVVAPSQTLNDYEYNMLRNTAIKVIRHLGVV-GECNIQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLS 712
Cdd:PRK05294 248 ITVAPAQTLTDKEYQMLRDASIAIIREIGVEtGGCNVQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPIAKVAAKLA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 713 LGIPLPVLKNSVTNSTTANFEPSLDYCVVKVPRWDLSKFLRVSTKIGSSMKSVGEVMAIGRSFEEAFQKALRMVDENCVG 792
Cdd:PRK05294 328 VGYTLDEIKNDITGKTPASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALRSLEIGVTG 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 793 FDHTI-----KPESEEELQTPTDKRIFVLAAALHAGYTVERLYELTKIDHWFLHKMKNIADHKKLLETYKQDesaMPPEI 867
Cdd:PRK05294 408 LDEDLfeeesLEELREELKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELKENGLP---LDAEL 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 868 MRKAKQLGFSDKQIAQAVQSTELAVRKLRRDWKIFPVVKQIDTVAAEWPAQTNYLYLTY-HGSESDVVfEQPHVMVIGSG 946
Cdd:PRK05294 485 LREAKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYeEECESNPS-DRKKVLVLGSG 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 947 VYRIGSSVEFDWCAVGCIMELRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYEMENPEGVILSMGGQLPN 1026
Cdd:PRK05294 564 PNRIGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKPKGVIVQFGGQTPL 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1027 NIAMSLHRQQCRILGTSPEFIDNAENRFKFSRMLDTIGISQPRWKELSDTESAVNFCETVGYPCLVRPSYVLSGAAMNVA 1106
Cdd:PRK05294 644 KLAKALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPVLVRPSYVLGGRAMEIV 723
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1107 YSDTDMEKFLSSAVAVSKEHPVVISKFIQEAKEIDVDAVaCDGEVIAIA-VSEHVENAGVHSGDATLVTPPQDINQKTME 1185
Cdd:PRK05294 724 YDEEELERYMREAVKVSPDHPVLIDKFLEGAIEVDVDAI-CDGEDVLIGgIMEHIEEAGVHSGDSACSLPPQTLSEEIIE 802
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1186 RIKMIVHAIGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPYVSKTLGVDLVALATRVILGEEVEAVGLMRGN--GI 1263
Cdd:PRK05294 803 EIREYTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKIAARVMLGKKLAELGYTKGLipPY 882
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1264 VGVKVPQFSFSRLAGADVVLGVEMTSTGEVACFGENRYEAYLKAMLSTGFKIPKK-NILLSIgSYKNKSELLPTVQTLES 1342
Cdd:PRK05294 883 VAVKEAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKAQLAAGNRLPTSgTVFLSV-RDRDKEEVVELAKRLLE 961
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1343 LGYNLYASLGTADFYTEHGVKVMAVdwpfeeesdcpNKDKQR--NIMDYLEENHFDLVINlSMRNSGGRRlssfvtKGYR 1420
Cdd:PRK05294 962 LGFKILATSGTAKFLREAGIPVELV-----------NKVHEGrpHIVDLIKNGEIDLVIN-TPTGRQAIR------DGFS 1023
|
1050 1060
....*....|....*....|....*..
gi 822092823 1421 TRRMAIDFSVPLITDIKCTKLFVQALK 1447
Cdd:PRK05294 1024 IRRAALEYKVPYITTLAGARAAVKAIE 1050
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
396-1449 |
0e+00 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 1109.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 396 RKVLVLGSGGLSIGQAGEFDYSGSQAIKAMKEENIQTILINPNIATVQTSKGLADKVYFLPITPEYVTQVIKNERPDGVL 475
Cdd:PRK12815 8 QKILVIGSGPIVIGQAAEFDYSGTQACLALKEEGYQVVLVNPNPATIMTDPAPADTVYFEPLTVEFVKRIIAREKPDALL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 476 LTFGGQTALNCGVELKKQGVLEKYKVRVLGTPVASIEMTEDRKIFVEKMEEINEHVAPSEAAMSVEQAVAAAERLGYPVL 555
Cdd:PRK12815 88 ATLGGQTALNLAVKLHEDGILEQYGVELLGTNIEAIQKGEDRERFRALMKELGEPVPESEIVTSVEEALAFAEKIGFPII 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 556 VRSAFALGGLGSGFANNRDEMITLVTQAFA--HTSQVLVDKSLKGWKEIEYEVVRDAYDNCVTVCNMENIDPLGIHTGES 633
Cdd:PRK12815 168 VRPAYTLGGTGGGIAENLEELEQLFKQGLQasPIHQCLLEESIAGWKEIEYEVMRDRNGNCITVCNMENIDPVGIHTGDS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 634 IVVAPSQTLNDYEYNMLRNTAIKVIRHLGVVGECNIQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLSL 713
Cdd:PRK12815 248 IVVAPSQTLTDDEYQMLRSASLKIISALGVVGGCNIQFALDPKSKQYYLIEVNPRVSRSSALASKATGYPIAKIAAKLAV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 714 GIPLPVLKNSVTNSTTANFEPSLDYCVVKVPRWDLSKFLRVSTKIGSSMKSVGEVMAIGRSFEEAFQKALRMVDENCVGF 793
Cdd:PRK12815 328 GYTLNELKNPVTGLTYASFEPALDYVVVKFPRWPFDKFGYADRTLGTQMKATGEVMAIGRNFESAFQKALRSLEIKRNGL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 794 DHTIK--PESEEEL----QTPTDKRIFVLAAALHAGYTVERLYELTKIDHWFLHKMKNIadhKKLLETYKQDESAMPPEI 867
Cdd:PRK12815 408 SLPIElsGKSDEELlqdlRHPDDRRLFALLEALRRGITYEEIHELTKIDPFFLQKFEHI---VALEKKLAEDGLDLSADL 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 868 MRKAKQLGFSDKQIAQAVQSTELAVRKLRRDWKIFPVVKQIDTVAAEWPAQTNYLYLTYHG-SESDVVFEQPHVMVIGSG 946
Cdd:PRK12815 485 LRKVKEKGFSDALLAELTGVTEEEVRALRKKLGIRPSYKMVDTCAAEFEAKTPYYYSTYFGeSEAEPSSEKKKVLILGSG 564
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 947 VYRIGSSVEFDWCAVGCIMELRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYEMENPEGVILSMGGQLPN 1026
Cdd:PRK12815 565 PIRIGQGIEFDYSSVHAAFALKKEGYETIMINNNPETVSTDYDTADRLYFEPLTLEDVLNVAEAENIKGVIVQFGGQTAI 644
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1027 NIAMSLHRQQCRILGTSPEFIDNAENRFKFSRMLDTIGISQPRWKELSDTESAVNFCETVGYPCLVRPSYVLSGAAMNVA 1106
Cdd:PRK12815 645 NLAKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAVV 724
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1107 YSDTDMEKFLssAVAVSKEHPVVISKFIqEAKEIDVDAVaCDGEVIAIA-VSEHVENAGVHSGDATLVTPPQDINQKTME 1185
Cdd:PRK12815 725 YDEPALEAYL--AENASQLYPILIDQFI-DGKEYEVDAI-SDGEDVTIPgIIEHIEQAGVHSGDSIAVLPPQSLSEEQQE 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1186 RIKMIVHAIGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPYVSKTLGVDLVALATRVILG----EEVEAVGLMRGN 1261
Cdd:PRK12815 801 KIRDYAIKIAKKLGFRGIMNIQFVLANDEIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLGkslaELGYPNGLWPGS 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1262 GIVGVKVPQFSFSRLAGADVVLGVEMTSTGEVACFGENRYEAYLKAMLSTGFKIPKKNILLSIGSYKNKSELLPTVQTLE 1341
Cdd:PRK12815 881 PFIHVKMPVFSYLKYPGVDNTLGPEMKSTGEVMGIDKDLEEALYKGYEASDLHIPSYGTIFISVRDEDKPEVTKLARRFA 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1342 SLGYNLYASLGTADFYTEHGVKVMAVDWPFEEesdcpnkdkQRNIMDYLEENHFDLVINLSMRNSGGRrlssfvtKGYRT 1421
Cdd:PRK12815 961 QLGFKLLATEGTANWLAEEGITTGVVEKVQEG---------SPSLLERIKQHRIVLVVNTSLSDSASE-------DAIKI 1024
|
1050 1060
....*....|....*....|....*...
gi 822092823 1422 RRMAIDFSVPLITDIKCTKLFVQALKQI 1449
Cdd:PRK12815 1025 RDEALSTHIPVFTELETAQAFLQVLESL 1052
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
396-1453 |
0e+00 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 891.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 396 RKVLVLGSGGLSIGQAGEFDYSGSQAIKAMKEENIQTILINPNIATVQTSKGLADKVYFLPITPEYVTQVIKNERPDGVL 475
Cdd:PLN02735 24 KKIMILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATIMTDPETADRTYIAPMTPELVEQVIAKERPDALL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 476 LTFGGQTALNCGVELKKQGVLEKYKVRVLGTPVASIEMTEDRKIFVEKMEEINEHVAPSEAAMSVEQAVAAAERLG-YPV 554
Cdd:PLN02735 104 PTMGGQTALNLAVALAESGILEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPPSGIATTLDECFEIAEDIGeFPL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 555 LVRSAFALGGLGSGFANNRDEMITLVTQAFA--HTSQVLVDKSLKGWKEIEYEVVRDAYDNCVTVCNMENIDPLGIHTGE 632
Cdd:PLN02735 184 IIRPAFTLGGTGGGIAYNKEEFETICKAGLAasITSQVLVEKSLLGWKEYELEVMRDLADNVVIICSIENIDPMGVHTGD 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 633 SIVVAPSQTLNDYEYNMLRNTAIKVIRHLGVvgEC---NIQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAA 709
Cdd:PLN02735 264 SITVAPAQTLTDKEYQRLRDYSVAIIREIGV--ECggsNVQFAVNPVDGEVMIIEMNPRVSRSSALASKATGFPIAKMAA 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 710 KLSLGIPLPVLKNSVTNSTTANFEPSLDYCVVKVPRWDLSKFLRVSTKIGSSMKSVGEVMAIGRSFEEAFQKALRMVDEN 789
Cdd:PLN02735 342 KLSVGYTLDQIPNDITLKTPASFEPSIDYVVTKIPRFAFEKFPGSQPILTTQMKSVGEAMALGRTFQESFQKALRSLETG 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 790 CVGFDHTIKPESE-------EELQTPTDKRIFVLAAALHAGYTVERLYELTKIDHWFLHKMKNIADHKKLLETYKQDEsa 862
Cdd:PLN02735 422 FSGWGCAKVKELDwdweqlkYKLRVPNPDRIHAIYAAMKKGMTVDEIHELTFIDPWFLTQLKELVDVEQFLKSRSLSE-- 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 863 MPPEIMRKAKQLGFSDKQIAQAVQSTELAVRKLRRDWKIFPVVKQIDTVAAEWPAQTNYLYLTYHGSESDVVFEQPHVMV 942
Cdd:PLN02735 500 LSKDDFYEVKRRGFSDKQIAFATKSTEKEVRSKRLSLGVTPSYKRVDTCAAEFEANTPYMYSSYDGECESAPTNKKKVLI 579
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 943 IGSGVYRIGSSVEFDWCAVGCIMELRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYEMENPEGVILSMGG 1022
Cdd:PLN02735 580 LGGGPNRIGQGIEFDYCCCHASFALQDAGYETIMMNSNPETVSTDYDTSDRLYFEPLTVEDVLNVIDLERPDGIIVQFGG 659
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1023 QLPNNIAMSLHRQ-------------QCRILGTSPEFIDNAENRFKFSRMLDTIGISQPRWKELSDTESAVNFCETVGYP 1089
Cdd:PLN02735 660 QTPLKLALPIQKYldknpppsasgngNVKIWGTSPDSIDAAEDRERFNAILNELKIEQPKGGIARSEADALAIAKRIGYP 739
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1090 CLVRPSYVLSGAAMNVAYSDTDMEKFLSSAVAVSKEHPVVISKFIQEAKEIDVDAVA-CDGEVIAIAVSEHVENAGVHSG 1168
Cdd:PLN02735 740 VVVRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDPERPVLVDKYLSDATEIDVDALAdSEGNVVIGGIMEHIEQAGVHSG 819
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1169 DATLVTPPQDINQKTMERIKMIVHAIGQELQVTGPFNLQL-IAKDDQLKVIECNVRVSRSFPYVSKTLGVDLVALATRVI 1247
Cdd:PLN02735 820 DSACSLPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYaITPSGEVYIIEANPRASRTVPFVSKAIGHPLAKYASLVM 899
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1248 LGEEVEAVGLMRGNGI--VGVKVPQFSFSRLAGADVVLGVEMTSTGEVACFGENRYEAYLKAMLSTGFKIPKK-NILLSI 1324
Cdd:PLN02735 900 SGKSLKDLGFTEEVIPahVSVKEAVLPFDKFQGCDVLLGPEMRSTGEVMGIDYEFSKAFAKAQIAAGQRLPLSgTVFISL 979
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1325 GSyKNKSELLPTVQTLESLGYNLYASLGTADFYTEHGVKVMAVDWPFEeesdcpnkdKQRNIMDYLEENHfdlvINLSMR 1404
Cdd:PLN02735 980 ND-LTKPHLVPIARGFLELGFRIVSTSGTAHFLELAGIPVERVLKLHE---------GRPHAGDMLANGQ----IQLMVI 1045
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....*....
gi 822092823 1405 NSGGRRLSSfvTKGYRTRRMAIDFSVPLITDIKCTKLFVQALKQIGQAP 1453
Cdd:PLN02735 1046 TSSGDALDQ--KDGRQLRRMALAYKVPIITTVAGALATAQAVKSLKECP 1092
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
401-945 |
0e+00 |
|
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440226 [Multi-domain] Cd Length: 536 Bit Score: 661.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 401 LGSGGLSIGQAGEFDYSGSQAIKAMKEENIQTILINPNIATVQTSKGLADKVYFLPITPEYVTQVIKNERPDGVLLTFGG 480
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 481 QTALNCGVELKKQGVLEKykVRVLGTPVASIEMTEDRKIFVEKMEEINEHVAPSEAAMSVEQAVAAAERLGYPVLVRSAF 560
Cdd:COG0458 81 QTALNLAVELEEAGILEG--VKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 561 ALGGLGSGFANNRDEMITLVTQAFAH--TSQVLVDKSLKGWKEIEYEVVRDAYDNCVTVCNMENIDPLGIHTGESIVVAP 638
Cdd:COG0458 159 VLGGRGMGIVYNEEELEEYLERALKVspDHPVLIDESLLGAKEIEVDVVRDGEDNVIIVGIMEHIEPAGVHSGDSICVAP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 639 SQTLNDYEYNMLRNTAIKVIRHLGVVGECNIQYALNpeSEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLSLGIPLP 718
Cdd:COG0458 239 PQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVD--DGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 719 VLKNsvtnstTANFEPSLDYCVVKVPRWDLSKFLRVSTKIGSSMKSVGEVMAIGRSFEEAFQKALRMVDENCVG--FDHT 796
Cdd:COG0458 317 ELGN------DTGFEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGtvLLSL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 797 IKPESEEE--LQTPTDKRIFVLAAALHAGYTVERLYELTKIDHWFLHKMKNIadhkkLLETYKQDESAMPPEIMRKAKQL 874
Cdd:COG0458 391 VADDDKEEalLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPI-----IVDEIELEEIILVINTLLGAKSL 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 822092823 875 GFSDKQIAQAVQSTELAVRKLRRDWKIFPVVKQIDTVAAEWPAQTNYLYLTYHGSESDVVFEQPHVMVIGS 945
Cdd:COG0458 466 GDSDGIIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYYYSTYEYENESEETEEPKVVVIGS 536
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
1466-1812 |
0e+00 |
|
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate synthetase-aspartate transcarbamoylase-dihydroorotase, which catalyzes the first three steps of de novo pyrimidine nucleotide biosynthesis. Dihydroorotase (DHOase) catalyzes the third step, the reversible interconversion of carbamoyl aspartate to dihydroorotate.
Pssm-ID: 238641 [Multi-domain] Cd Length: 344 Bit Score: 579.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1466 KLIRLPGLIDVHVHLREPGATHKEDFSSGTAAALAGGITMVCAMPNTNPAIIDPNSFTMAQKLAKAGCRCDYALFVGASS 1545
Cdd:cd01316 1 RTIRLPGLIDVHVHLREPGATHKEDFASGTKAALAGGFTMVRAMPNTNPSIVDVASLKLVQSLAQAKARCDYAFSIGATS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1546 DNAALLPSIASSTAGLKMYLNDTYSTLKMDNVSLWMEHFEKWPKHLPIVAHAEKQTVAAILLVAQLYQRPVHICHVAKKE 1625
Cdd:cd01316 81 TNAATVGELASEAVGLKFYLNETFSTLILDKITAWASHFNAWPSTKPIVTHAKSQTLAAVLLLASLHNRSIHICHVSSKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1626 EILIIRAAKQKGIQVTCEVAPHHLFLCEDNVPvigKDKAQVRPMLGTREDMEALWENLDIIDCFATDHAPHSAEEKISEK 1705
Cdd:cd01316 161 EINLIRLAKARGLKVTCEVSPHHLFLSQDDLP---RGQYEVRPFLPTREDQEALWENLDYIDCFATDHAPHTLAEKTGNK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1706 PPPGYPGLETMLPLLFTAVSEGRLTVDDIIKRLYENPRKIFSLPAQEDTYVEVDLEQEWIIPKHMQFTKSKWTPFEGMKV 1785
Cdd:cd01316 238 PPPGFPGVETSLPLLLTAVHEGRLTIEDIVDRLHTNPKRIFNLPPQSDTYVEVDLDEEWTIPKNPLQSKKGWTPFEGKKV 317
|
330 340
....*....|....*....|....*..
gi 822092823 1786 KGKVMRVVLRGEVAYIDGQVLVPPGYG 1812
Cdd:cd01316 318 KGKVQRVVLRGETAFIDGEIVAPPGFG 344
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
943-1436 |
5.54e-172 |
|
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440226 [Multi-domain] Cd Length: 536 Bit Score: 537.92 E-value: 5.54e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 943 IGSGVYRIGSSVEFDWCAVGCIMELRKMGYKTIMVNYNPETVSTDYDMCDRLYFDEISFEVVMDIYEMENPEGVILSMGG 1022
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1023 QLPNNIAMSLHRQQ----CRILGTSPEFIDNAENRFKFSRMLDTIGISQPRWKELSDTESAVNFCETVGYPCLVRPSYVL 1098
Cdd:COG0458 81 QTALNLAVELEEAGilegVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSYVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1099 SGAAMNVAYSDTDMEKFLSSAVAVSKEHPVVISKFIQEAKEIDVDAVaCDGE--VIAIAVSEHVENAGVHSGDATLVTPP 1176
Cdd:COG0458 161 GGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVV-RDGEdnVIIVGIMEHIEPAGVHSGDSICVAPP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1177 QDINQKTMERIKMIVHAIGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPYVSKTLGVDLVALATRVILGEEVEAVG 1256
Cdd:COG0458 240 QTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLDELG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1257 LmrGNGI------VGVKVPQFSFSRLAGADVVLGVEMTSTGEVACFGENRYEAYLKAMLSTGFKIPKKnILLSIGSYKNK 1330
Cdd:COG0458 320 N--DTGFeptldyVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGT-VLLSLVADDDK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1331 SELLPTVQTLESLGYNLYASLGTADFYTEHGVKVMAVDWPFEeesdcpnkdKQRNIMDYLEENHFDLVINLSMRNSGGRR 1410
Cdd:COG0458 397 EEALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSE---------GRPIIVDEIELEEIILVINTLLGAKSLGD 467
|
490 500
....*....|....*....|....*.
gi 822092823 1411 lssfvtkGYRTRRMAIDFSVPLITDI 1436
Cdd:COG0458 468 -------SDGIIRRALAAKVPYVTTL 486
|
|
| PRK12564 |
PRK12564 |
carbamoyl-phosphate synthase small subunit; |
4-359 |
1.30e-166 |
|
carbamoyl-phosphate synthase small subunit;
Pssm-ID: 237139 [Multi-domain] Cd Length: 360 Bit Score: 515.39 E-value: 1.30e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 4 KMASLVLEDGTTFKGRLFGAVSSVSGEVVFQTGMVGYPEALTDPSYKSQILTLTYPMIGNYGIPKDedgefglskWFESS 83
Cdd:PRK12564 3 MKAYLVLEDGTVFEGKAFGAEGETVGEVVFNTSMTGYQEILTDPSYAGQIVTFTYPLIGNYGVNRE---------DFESD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 84 QIHAAALIVGEVSENPSHWSAAKSLDEWLREQGIPGLQGVDTRCLTKKIREKGTMLGKLVVEGTPADNIP-----FDNPD 158
Cdd:PRK12564 74 RPHAKGLIVRELSDIPSNWRSEMSLDEYLKENGIPGISGIDTRALTRKLREKGAMKGVIATEDFDAEELLekaraFPGLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 159 ARNLVKEVSMKAPKVF---NPEGTVRITAIDCGIKYNQIRCLCQRGARVTVVPWDQPLD---SNDFDGLFISNGPGNPEY 232
Cdd:PRK12564 154 GLDLVKEVSTKEPYPWpgpGGELKYKVVAIDFGVKRNILRELAERGCRVTVVPATTTAEeilALNPDGVFLSNGPGDPAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 233 CKETVENIRKVacVENPKPIFGICLGHQLLSLVIGAKTYKMKYGNRGHNQPCIHKGTSRCYITSQNHGFAVDPETLPKDW 312
Cdd:PRK12564 234 LDYAIEMIREL--LEKKIPIFGICLGHQLLALALGAKTYKMKFGHRGANHPVKDLETGKVEITSQNHGFAVDEDSLPANL 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 822092823 313 DVLFTNANDQTSEGIVHNHKPLFSVQFHPEHMAGPTDLVGLFDVFLD 359
Cdd:PRK12564 312 EVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDEFVE 358
|
|
| CarA |
COG0505 |
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
4-362 |
1.15e-164 |
|
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase small subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440271 [Multi-domain] Cd Length: 361 Bit Score: 509.95 E-value: 1.15e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 4 KMASLVLEDGTTFKGRLFGAVSSVSGEVVFQTGMVGYPEALTDPSYKSQILTLTYPMIGNYGIPkDEDgefglskwFESS 83
Cdd:COG0505 3 MKALLVLEDGTVFEGKSFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVTFTYPHIGNYGVN-DED--------FESD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 84 QIHAAALIVGEVSENPSHWSAAKSLDEWLREQGIPGLQGVDTRCLTKKIREKGTMLGKLVVEGTPADNIP-----FDNPD 158
Cdd:COG0505 74 RPWVAGLVVRELSRRPSNWRSEESLDEYLKEHGIPGISGIDTRALTRHLREKGAMKGVISTGDLDIEELLekaraAPGME 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 159 ARNLVKEVSMKAPKVF--NPEGTVRITAIDCGIKYNQIRCLCQRGARVTVVPWDQPLD---SNDFDGLFISNGPGNPEYC 233
Cdd:COG0505 154 GLDLVKEVSTKEPYEWteAPGAGFHVVALDFGVKRNILRELAERGCRVTVVPATTSAEeilALNPDGVFLSNGPGDPAAL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 234 KETVENIRKVacVENPKPIFGICLGHQLLSLVIGAKTYKMKYGNRGHNQPCIHKGTSRCYITSQNHGFAVDPETLPK-DW 312
Cdd:COG0505 234 DYAIETIREL--LGKGIPIFGICLGHQLLALALGAKTYKLKFGHRGANHPVKDLETGRVEITSQNHGFAVDEDSLPAtDL 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 822092823 313 DVLFTNANDQTSEGIVHNHKPLFSVQFHPEHMAGPTDLVGLFDVFLDTVR 362
Cdd:COG0505 312 EVTHVNLNDGTVEGLRHKDLPAFSVQYHPEASPGPHDSAYLFDRFIELME 361
|
|
| CPSaseIIsmall |
TIGR01368 |
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small ... |
6-363 |
1.27e-163 |
|
carbamoyl-phosphate synthase, small subunit; This model represents the whole of the small chain of the glutamine-dependent form (EC 6.3.5.5) of carbamoyl phosphate synthase, CPSase II. The C-terminal domain has glutamine amidotransferase activity. Note that the sequence from the mammalian urea cycle form has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I (EC 6.3.4.16). CPSases of pyrimidine biosynthesis, arginine biosynthesis, and the urea cycle may be encoded by one or by several genes, depending on the species. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273580 [Multi-domain] Cd Length: 357 Bit Score: 507.16 E-value: 1.27e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 6 ASLVLEDGTTFKGRLFGAVSSVSGEVVFQTGMVGYPEALTDPSYKSQILTLTYPMIGNYGIPKDedgefglskWFESSQI 85
Cdd:TIGR01368 1 AYLVLEDGTVFRGYSFGAEGTVAGEVVFNTGMTGYQEILTDPSYKGQIVVFTYPLIGNYGVNDE---------DAESKGI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 86 HAAALIVGEVSENPSHWSAAKSLDEWLREQGIPGLQGVDTRCLTKKIREKGTMLGKLVVEGTPADN----IPFD-NPDAR 160
Cdd:TIGR01368 72 HVSGLVVRELSDRYSNWRATESLDQFLKRHGIPGIYGVDTRALVKKIREKGTMKGVISTEDSNDEElvekARVSpDITGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 161 NLVKEVSMKAPKVFNPEGT--VRITAIDCGIKYNQIRCLCQRGARVTVVPWDQPLD---SNDFDGLFISNGPGNPEYCKE 235
Cdd:TIGR01368 152 NLVAEVSTKEPYTWGQRGGkgKRVVVIDFGVKRNILRRLVKRGCEVTVVPYDTDAEeikKYNPDGIFLSNGPGDPAAVEP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 236 TVENIRKVAcveNPKPIFGICLGHQLLSLVIGAKTYKMKYGNRGHNQPCIHKGTSRCYITSQNHGFAVDPETLPK-DWDV 314
Cdd:TIGR01368 232 AIETIRKLL---EKIPIFGICLGHQLLALAFGAKTYKMKFGHRGGNHPVKDLITGRVEITSQNHGYAVDPDSLPAgDLEV 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 822092823 315 LFTNANDQTSEGIVHNHKPLFSVQFHPEHMAGPTDLVGLFDVFLDTVRD 363
Cdd:TIGR01368 309 THVNLNDGTVEGIRHKDLPVFSVQYHPEASPGPHDTEYLFDEFIDLMKK 357
|
|
| PyrB |
COG0540 |
Aspartate carbamoyltransferase, catalytic subunit [Nucleotide transport and metabolism]; ... |
1925-2230 |
4.47e-138 |
|
Aspartate carbamoyltransferase, catalytic subunit [Nucleotide transport and metabolism]; Aspartate carbamoyltransferase, catalytic subunit is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 440306 [Multi-domain] Cd Length: 306 Bit Score: 433.33 E-value: 4.47e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1925 HPLVGQHILSVRQFSKEQMSHLFNVAHTLRLMVQKERPLDILKGKVMASMFYEVSTRTSSSFAAAMHRLGGSVVHFCEST 2004
Cdd:COG0540 1 MSFKMRHLLSIEDLSREEIEELLDTAEEFKEVLRPIKKVPLLRGKTVANLFFEPSTRTRLSFELAAKRLGADVINFSAST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 2005 SSTQKGESLVDSVNTMSCY-ADVIVLRHPIPGAVESAARHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITM 2083
Cdd:COG0540 81 SSVSKGESLADTIRTLEAYgADAIVIRHPQEGAARLLAEHVDVPVINAGDGAHEHPTQALLDLYTIREEFGRLDGLKVAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 2084 VGDLKHGRTVHSLARLLTQYRITLRYVAPKNLsMPAEIidfvASKGIkqEEFNSIEEALPDTDVLYMTRIQKERFS---- 2159
Cdd:COG0540 161 VGDLKHSRVARSNIKALSKLGAEVTLVAPPTL-LPEEI----EELGV--EVTTDLDEALPDADVVYMLRIQKERFTdglf 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 822092823 2160 -SEKEYnacFGQFILTPHIMTGAKRKMVVMHPLP--RVNEISVEVDTDPRAAYFRQAENGMYIRMALLATVLGR 2230
Cdd:COG0540 234 pSYREY---KRSYGLTAERLALAKPDAIVMHPGPrnRGVEIDSDVDDTPRSVIFEQVTNGVAVRMALLYLLLGG 304
|
|
| PRK12838 |
PRK12838 |
carbamoyl phosphate synthase small subunit; Reviewed |
6-361 |
1.05e-133 |
|
carbamoyl phosphate synthase small subunit; Reviewed
Pssm-ID: 183784 [Multi-domain] Cd Length: 354 Bit Score: 422.76 E-value: 1.05e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 6 ASLVLEDGTTFKGRLFGAVSSVSGEVVFQTGMVGYPEALTDPSYKSQILTLTYPMIGNYGIPkDEDgefglskwFESSQI 85
Cdd:PRK12838 3 AYLILEDGTVFEGELIGAPIDVTGEIVFNTGMTGYQEVLTDPSYKGQIVVFTYPLIGNYGIN-ADD--------YESKQP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 86 HAAALIVGEVSENPSHWSAAKSLDEWLREQGIPGLQGVDTRCLTKKIREKGTMLGKLVvegTPADNIPFDNPDA----RN 161
Cdd:PRK12838 74 QVKGVIVYELSREGSHYRAKQSLDDFLKEWNIPGISGVDTRALVKHIREKGTMKASIT---TTDDAHAFDQIKAlvlpKN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 162 LVKEVSMKAPKVFnPEGTVRITAIDCGIKYNQIRCLCQRGARVTVVPWDQPL---DSNDFDGLFISNGPGNPEYCKETVE 238
Cdd:PRK12838 151 VVAQVSTKEPYTY-GNGGKHVALIDFGYKKSILRSLSKRGCKVTVLPYDTSLeeiKNLNPDGIVLSNGPGDPKELQPYLP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 239 NIRKVAcveNPKPIFGICLGHQLLSLVIGAKTYKMKYGNRGHNQPCIHKGTSRCYITSQNHGFAVDPETL-PKDWDVLFT 317
Cdd:PRK12838 230 EIKKLI---SSYPILGICLGHQLIALALGADTEKLPFGHRGANHPVIDLTTGRVWMTSQNHGYVVDEDSLdGTPLSVRFF 306
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 822092823 318 NANDQTSEGIVHNHKPLFSVQFHPEHMAGPTDLVGLFDVFLDTV 361
Cdd:PRK12838 307 NVNDGSIEGLRHKKKPVLSVQFHPEAHPGPHDAEYIFDEFLEMM 350
|
|
| pyrB |
PRK00856 |
aspartate carbamoyltransferase catalytic subunit; |
1926-2230 |
2.53e-124 |
|
aspartate carbamoyltransferase catalytic subunit;
Pssm-ID: 234849 [Multi-domain] Cd Length: 305 Bit Score: 394.05 E-value: 2.53e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1926 PLVGQHILSVRQFSKEQMSHLFNVAHTLR-LMVQKERPLDILKGKVMASMFYEVSTRTSSSFAAAMHRLGGSVVHFCEST 2004
Cdd:PRK00856 2 PLKMKHLLSIEDLSREEIELLLDTAEEFKeVLRREVKKVPLLRGKTVANLFFEPSTRTRLSFELAAKRLGADVINFSAST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 2005 SSTQKGESLVDSVNTMSCY-ADVIVLRHPIPGAVESAARHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITM 2083
Cdd:PRK00856 82 SSVSKGETLADTIRTLSAMgADAIVIRHPQSGAARLLAESSDVPVINAGDGSHQHPTQALLDLLTIREEFGRLEGLKVAI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 2084 VGDLKHGRTVHSLARLLTQYRITLRYVAPKNLsMPAEIIDFvaskgikqEEFNSIEEALPDTDVLYMTRIQKERF----- 2158
Cdd:PRK00856 162 VGDIKHSRVARSNIQALTRLGAEVRLIAPPTL-LPEGMPEY--------GVHTDLDEVIEDADVVMMLRVQKERMdggll 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 822092823 2159 SSEKEYnacFGQFILTPHIMTGAKRKMVVMHPLP--RVNEISVEVDTDPRAAYFRQAENGMYIRMALLATVLGR 2230
Cdd:PRK00856 233 PSYEEY---KRSYGLTAERLALAKPDAIVMHPGPvnRGVEIASDVADGPQSVIFEQVTNGVAVRMAVLELLLGG 303
|
|
| PLN02527 |
PLN02527 |
aspartate carbamoyltransferase |
1930-2229 |
5.37e-124 |
|
aspartate carbamoyltransferase
Pssm-ID: 178142 [Multi-domain] Cd Length: 306 Bit Score: 393.34 E-value: 5.37e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1930 QHILSVRQFSKEQMSHLFNVAHTLRLMVQKERPLDILKGKVMASMFYEVSTRTSSSFAAAMHRLGGSVVHfCES---TSS 2006
Cdd:PLN02527 1 SDVIEAQQFDREMLELLFEVAREMEKVERGSPGSQMLKGYLMATLFYEPSTRTRLSFESAMKRLGGEVLT-TENageFSS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 2007 TQKGESLVDSVNTMSCYADVIVLRHPIPGAVESAARHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITMVGD 2086
Cdd:PLN02527 80 AAKGETLEDTIRTVEGYSDIIVLRHFESGAARRAAATAEIPVINAGDGPGQHPTQALLDVYTIQREIGRLDGIKVGLVGD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 2087 LKHGRTVHSLARLLTQYR-ITLRYVAPKNLSMPAEIIDFVASKGIKQEEFNSIEEALPDTDVLYMTRIQKERFS-SEKEY 2164
Cdd:PLN02527 160 LANGRTVRSLAYLLAKYEdVKIYFVAPDVVKMKDDIKDYLTSKGVEWEESSDLMEVASKCDVLYQTRIQRERFGeRIDLY 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 822092823 2165 NACFGQFILTPHIMTGAKRKMVVMHPLPRVNEISVEVDTDPRAAYFRQAENGMYIRMALLATVLG 2229
Cdd:PLN02527 240 EAARGKYIVDKKVMDVLPKHAVVMHPLPRLDEITTDVDSDPRAAYFRQAKNGLFIRMALLKLLLG 304
|
|
| asp_carb_tr |
TIGR00670 |
aspartate carbamoyltransferase; Aspartate transcarbamylase (ATCase) is an alternate name.PyrB ... |
1931-2229 |
3.56e-110 |
|
aspartate carbamoyltransferase; Aspartate transcarbamylase (ATCase) is an alternate name.PyrB encodes the catalytic chain of aspartate carbamoyltransferase, an enzyme of pyrimidine biosynthesis, which organizes into trimers. In some species, including E. coli and the Archaea but excluding Bacillus subtilis, a regulatory subunit PyrI is also present in an allosterically regulated hexameric holoenzyme. Several molecular weight classes of ATCase are described in MEDLINE:96303527 and often vary within taxa. PyrB and PyrI are fused in Thermotoga maritima.Ornithine carbamoyltransferases are in the same superfamily and form an outgroup. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273209 [Multi-domain] Cd Length: 301 Bit Score: 353.20 E-value: 3.56e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1931 HILSVRQFSKEQMSHLFNVAHTLRLMVQKERPLDILKGKVMASMFYEVSTRTSSSFAAAMHRLGGSVVHFCES-TSSTQK 2009
Cdd:TIGR00670 2 HLISISDLSREEIELLLETARELEQVLNGKEPLKLLKGKILANLFFEPSTRTRLSFETAMKRLGGSVVNFSDSeTSSVAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 2010 GESLVDSVNTMSCYADVIVLRHPIPGAVESAARHCRRPVINAGDGVGEHPTQALLDIFTIREELGTVNGMTITMVGDLKH 2089
Cdd:TIGR00670 82 GETLADTIKTLSGYVDAIVIRHPLEGAARLAAEVSEVPVINAGDGSNQHPTQTLLDLYTIYEEFGRLDGLKIALVGDLKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 2090 GRTVHSLARLLTQYRITLRYVAPKNLSMPAEIIDFVASKGIKQEEFNSIEEALPDTDVLYMTRIQKERFSSEKEYNACFG 2169
Cdd:TIGR00670 162 GRTVHSLAEALTRFGVEVYLISPEELRMPKEILEELKAKGIKVRETESLEEVIDEADVLYVTRIQKERFPDPEEYEKVKG 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 2170 QFILTPHIMTGAKRKMVVMHPLPRVNEISVEVDTDPRAAYFRQAENGMYIRMALLATVLG 2229
Cdd:TIGR00670 242 SYGITLERLEAAKKGVIIMHPLPRVDEIDPSVDDTPHAKYFKQAFNGVPVRMALLALLLG 301
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
1467-1792 |
2.58e-104 |
|
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and dihydroorotase, are involved in the metabolism of pyrimidines and purines, sharing the property of hydrolyzing the cyclic amide bond of each substrate to the corresponding N-carbamyl amino acids. Allantoinases catalyze the degradation of purines, while dihydropyrimidinases and hydantoinases, a microbial counterpart of dihydropyrimidinase, are involved in pyrimidine degradation. Dihydroorotase participates in the de novo synthesis of pyrimidines.
Pssm-ID: 238627 [Multi-domain] Cd Length: 337 Bit Score: 338.21 E-value: 2.58e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1467 LIRLPGLIDVHVHLREPGAT-HKEDFSSGTAAALAGGITMVCAMPNTNPAIIDPNSFTMAQKLAKAGCRCDYALFVGASS 1545
Cdd:cd01302 1 LLVLPGFIDIHVHLRDPGGTtYKEDFESGSRAAAAGGVTTVIDMPNTGPPPIDLPAIELKIKLAEESSYVDFSFHAGIGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1546 -DNAALLP-SIASSTAGLKMYLNDTYSTLKMDNVSLWMEHFEKWP-KHLPIVAHAEKqtvaaILLVAQLYQRPVHICHVA 1622
Cdd:cd01302 81 gDVTDELKkLFDAGINSLKVFMNYYFGELFDVDDGTLMRTFLEIAsRGGPVMVHAER-----AAQLAEEAGANVHIAHVS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1623 KKEEILIIRAAKQKGIQVTCEVAPHHLFLCEDNVPVIGKdKAQVRPMLGTREDMEALWENL--DIIDCFATDHAPHSAEE 1700
Cdd:cd01302 156 SGEALELIKFAKNKGVKVTCEVCPHHLFLDESMLRLNGA-WGKVNPPLRSKEDREALWEGVknGKIDTIASDHAPHSKEE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1701 KIS----EKPPPGYPGLETMLPLLFTAVSEGRLTVDDIIKRLYENPRKIFSLPAQED---------TYVEVDLEQEWIIP 1767
Cdd:cd01302 235 KESgkdiWKAPPGFPGLETRLPILLTEGVKRGLSLETLVEILSENPARIFGLYPKGTiavgydadlVIVDPKKEWKVTAE 314
|
330 340
....*....|....*....|....*
gi 822092823 1768 KHMqfTKSKWTPFEGMKVKGKVMRV 1792
Cdd:cd01302 315 EIE--SKADWTPFEGMEVTGKPVST 337
|
|
| GATase1_CPSase |
cd01744 |
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
182-358 |
6.27e-103 |
|
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This group of sequences represents the small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II. CPSase II catalyzes the production of carbomyl phosphate (CP) from bicarbonate, glutamine and two molecules of MgATP. The reaction is believed to proceed by a series of four biochemical reactions involving a minimum of three discrete highly reactive intermediates. The synthesis of CP is critical for the initiation of two separate biosynthetic pathways. In one CP is coupled to aspartate, its carbon and nitrogen nuclei ultimately incorporated into the aromatic moieties of pyrimidine nucleotides. In the second pathway CP is condensed with ornithine at the start of the urea cycle and is utilized for the detoxification of ammonia and biosynthesis of arginine. CPSases may be encoded by one or by several genes, depending on the species. The E.coli enzyme is a heterodimer consisting of two polypeptide chains referred to as the small and large subunit. Ammonia an intermediate during the biosynthesis of carbomyl phosphate produced by the hydrolysis of glutamine in the small subunit of the enzyme is delivered via a molecular tunnel between the remotely located carboxyphosphate active site in the large subunit. CPSase IIs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. This group also contains the sequence from the mammalian urea cycle form which has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I.
Pssm-ID: 153215 [Multi-domain] Cd Length: 178 Bit Score: 327.15 E-value: 6.27e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 182 ITAIDCGIKYNQIRCLCQRGARVTVVPWDQPLD---SNDFDGLFISNGPGNPEYCKETVENIRKVAcvENPKPIFGICLG 258
Cdd:cd01744 1 VVVIDFGVKHNILRELLKRGCEVTVVPYNTDAEeilKLDPDGIFLSNGPGDPALLDEAIKTVRKLL--GKKIPIFGICLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 259 HQLLSLVIGAKTYKMKYGNRGHNQPCIHKGTSRCYITSQNHGFAVDPETLPKDWDVLFTNANDQTSEGIVHNHKPLFSVQ 338
Cdd:cd01744 79 HQLLALALGAKTYKMKFGHRGSNHPVKDLITGRVYITSQNHGYAVDPDSLPGGLEVTHVNLNDGTVEGIRHKDLPVFSVQ 158
|
170 180
....*....|....*....|
gi 822092823 339 FHPEHMAGPTDLVGLFDVFL 358
Cdd:cd01744 159 FHPEASPGPHDTEYLFDEFL 178
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
516-718 |
1.81e-100 |
|
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.
Pssm-ID: 397079 [Multi-domain] Cd Length: 209 Bit Score: 321.56 E-value: 1.81e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 516 DRKIFVEKMEEINEHVAPSEAAM--SVEQAVAAAERLGYPVLVRSAFALGGLGSGFANNRDEMITLVTQAFAHT------ 587
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPveTEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEApaafgn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 588 SQVLVDKSLKGWKEIEYEVVRDAYDNCVTVCNMENIDPLgiHTGESIVVAPSQTLNDYEYNMLRNTAIKVIRHLGVVGEC 667
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 822092823 668 NIQYALNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLSLGIPLP 718
Cdd:pfam02786 159 TVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
1470-1816 |
2.16e-100 |
|
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; Dihydroorotase or related cyclic amidohydrolase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 439814 [Multi-domain] Cd Length: 439 Bit Score: 330.90 E-value: 2.16e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1470 LPGLIDVHVHLREPGATHKEDFSSGTAAALAGGITMVCAMPNTNPAIIDPNSFTMAQKLAKAGCRCDYALFVGASSD--- 1546
Cdd:COG0044 49 LPGLIDLHVHLREPGLEHKEDIETGTRAAAAGGVTTVVDMPNTNPVTDTPEALEFKLARAEEKALVDVGPHGALTKGlge 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1547 NAALLPSIASSTA-GLKMYLndTYSTLK-MDNVSLWMEHFEKWPKH-LPIVAHAEKQT---------------------- 1601
Cdd:COG0044 129 NLAELGALAEAGAvAFKVFM--GSDDGNpVLDDGLLRRALEYAAEFgALVAVHAEDPDlirggvmnegktsprlglkgrp 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1602 -------VAAILLVAQLYQRPVHICHVAKKEEILIIRAAKQKGIQVTCEVAPHHLFLCEDNVPviGKD-KAQVRPMLGTR 1673
Cdd:COG0044 207 aeaeeeaVARDIALAEETGARLHIVHVSTAEAVELIREAKARGLPVTAEVCPHHLTLTDEDLE--RYGtNFKVNPPLRTE 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1674 EDMEALWENL--DIIDCFATDHAPHSAEEKisEKP----PPGYPGLETMLPLLFT-AVSEGRLTVDDIIKRLYENPRKIF 1746
Cdd:COG0044 285 EDREALWEGLadGTIDVIATDHAPHTLEEK--ELPfaeaPNGIPGLETALPLLLTeLVHKGRLSLERLVELLSTNPARIF 362
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 822092823 1747 SLPA----QEDTY---VEVDLEQEWIIPKHMQFTKSKWTPFEGMKVKGKVMRVVLRGEVAYIDGQVLVPPgYGQDVK 1816
Cdd:COG0044 363 GLPRkgriAVGADadlVLFDPDAEWTVTAEDLHSKSKNTPFEGRELTGRVVATIVRGRVVYEDGEVVGEP-RGRFLR 438
|
|
| PRK08192 |
PRK08192 |
aspartate carbamoyltransferase; Provisional |
1929-2229 |
2.31e-93 |
|
aspartate carbamoyltransferase; Provisional
Pssm-ID: 169269 [Multi-domain] Cd Length: 338 Bit Score: 306.65 E-value: 2.31e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1929 GQHILSVRQFSKEQMSHLFNVAHTLRLMVQKERPLDILKGKVMASMFYEVSTRTSSSFAAAMHRLGGSV---VHFceSTS 2005
Cdd:PRK08192 5 GSHILSVNQLDRDAIQRIFNVADRMEPYALREKRTRVLEGAILGNLFFEPSTRTRVSFGCAFNLLGGHVretTGM--ASS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 2006 STQKGESLVDSVNTMSCYADVIVLRHPIPGAVESAARHCRRPVINAGDGVGEHPTQALLDIFTIREEL----GTVNGMTI 2081
Cdd:PRK08192 83 SLSKGESLYDTARVLSTYSDVIAMRHPDAGSVKEFAEGSRVPVINGGDGSNEHPTQALLDLFTIQKELahagRGIDGMHI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 2082 TMVGDLKHGRTVHSLARLLTQY-RITLRYVAPKNLSMPAEIIDFVASKGIKQEEFNSIEEALPDTDVLYMTRIQKERFSS 2160
Cdd:PRK08192 163 AMVGDLKFGRTVHSLSRLLCMYkNVSFTLVSPKELAMPDYVISDIENAGHKITITDQLEGNLDKADILYLTRIQEERFPS 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 822092823 2161 EKEYNACFGQFILTPHIMTG-AKRKMVVMHPLPR-----VNEISVEVDTDPRAAYFRQAENGMYIRMALLATVLG 2229
Cdd:PRK08192 243 QEEANKYRGKFRLNQSIYTQhCKSNTVIMHPLPRdsraqANELDNDLNSHPNLAIFRQADNGLLIRMALFALTLG 317
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
380-784 |
3.55e-91 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 322.33 E-value: 3.55e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 380 HLTFPGSPDPNAFVRPRKVLVLGSGGLSIGQAGEFDYSGSQAIKAMKEENIQTILINPNIATVQTSKGLADKVYFLPITP 459
Cdd:TIGR01369 539 YSTYEGERDDVPFTDKKKVLVLGSGPNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTF 618
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 460 EYVTQVIKNERPDGVLLTFGGQTALNCGVELKKQGvlekykVRVLGTPVASIEMTEDRKIFVEKMEEINEHVAPSEAAMS 539
Cdd:TIGR01369 619 EDVMNIIELEKPEGVIVQFGGQTPLNLAKALEEAG------VPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATS 692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 540 VEQAVAAAERLGYPVLVRSAFALGGLGSGFANNRDEMITLVTQAFAHTSQ--VLVDKSLKGWKEIEYEVVrdAYDNCVTV 617
Cdd:TIGR01369 693 VEEAVEFASEIGYPVLVRPSYVLGGRAMEIVYNEEELRRYLEEAVAVSPEhpVLIDKYLEDAVEVDVDAV--SDGEEVLI 770
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 618 CN-MENIDPLGIHTGESIVVAPSQTLNDYEYNMLRNTAIKVIRHLGVVGECNIQYALnpESEQYYIIEVNARLSRSSALA 696
Cdd:TIGR01369 771 PGiMEHIEEAGVHSGDSTCVLPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAV--KDGEVYVIEVNPRASRTVPFV 848
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 697 SKATGYPLAYVAAKLSLG---IPLPVLKnsvtnsttanfEPSLDYCVVKVPRWDLSKFLRVSTKIGSSMKSVGEVMAIGR 773
Cdd:TIGR01369 849 SKATGVPLAKLAVRVMLGkklEELGVGK-----------EKEPKYVAVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGR 917
|
410
....*....|.
gi 822092823 774 SFEEAFQKALR 784
Cdd:TIGR01369 918 DLAEAFLKAQL 928
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
1467-1802 |
3.40e-89 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 297.88 E-value: 3.40e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1467 LIRLPGLIDVHVHLREPGATHKEDFSSGTAAALAGGITMVCAMPNTNPAIIDPNSFTMAQKLAKAGCRCDY----ALFVG 1542
Cdd:PRK09357 49 LVVAPGLVDLHVHLREPGQEDKETIETGSRAAAAGGFTTVVAMPNTKPVIDTPEVVEYVLDRAKEAGLVDVlpvgAITKG 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1543 ASSDNAALLPSIASstAGLKMYLNDTystLKMDNVSLWMEHFEKWPKH-LPIVAHAE-----------KQTVAAIL---- 1606
Cdd:PRK09357 129 LAGEELTEFGALKE--AGVVAFSDDG---IPVQDARLMRRALEYAKALdLLIAQHCEdpslteggvmnEGEVSARLglpg 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1607 --------------LVAQLYQRPVHICHVAKKEEILIIRAAKQKGIQVTCEVAPHHLFLCEDNVPviGKD-KAQVRPMLG 1671
Cdd:PRK09357 204 ipavaeevmiardvLLAEATGARVHICHVSTAGSVELIRWAKALGIKVTAEVTPHHLLLTDEDLL--TYDpNYKVNPPLR 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1672 TREDMEALWENL--DIIDCFATDHAPHSAEEKISE--KPPPGYPGLETMLPLLFTA-VSEGRLTVDDIIKRLYENPRKIF 1746
Cdd:PRK09357 282 TEEDREALIEGLkdGTIDAIATDHAPHAREEKECEfeAAPFGITGLETALSLLYTTlVKTGLLDLEQLLEKMTINPARIL 361
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 822092823 1747 SLPA------QEDTYVEVDLEQEWII-PKHMqFTKSKWTPFEGMKVKGKVMRVVLRGEVAYID 1802
Cdd:PRK09357 362 GLPAgplaegEPADLVIFDPEAEWTVdGEDF-ASKGKNTPFIGMKLKGKVVYTIVDGKIVYQD 423
|
|
| PRK11891 |
PRK11891 |
aspartate carbamoyltransferase; Provisional |
1930-2229 |
4.55e-89 |
|
aspartate carbamoyltransferase; Provisional
Pssm-ID: 183362 [Multi-domain] Cd Length: 429 Bit Score: 297.93 E-value: 4.55e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1930 QHILSVRQFSKEQMSHLFNVAHTLRLMVQKERPLDILKGKVMASMFYEVSTRTSSSFAAAMHRLGGSVvhfCEST----S 2005
Cdd:PRK11891 88 PQLLSVDQFSRDSVEALFRVADVMQPIARRQKISRVLEGAVLGNLFFEASTRTRVSFGAAFCRLGGSV---CDTTgftfS 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 2006 STQKGESLVDSVNTMSCYADVIVLRHPIPGAVESAARHCRRPVINAGDGVGEHPTQALLDIFTIREE---LG-TVNGMTI 2081
Cdd:PRK11891 165 SMAKGESIYDTSRVMSGYVDALVIRHPEQGSVAEFARATNLPVINGGDGPGEHPSQALLDLYTIQREfsrLGkIVDGAHI 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 2082 TMVGDLKHGRTVHSLARLLTQYR-ITLRYVAPKNLSMPAEIIDFVASKGIKQEEFNSIEEALPDTDVLYMTRIQKERFSS 2160
Cdd:PRK11891 245 ALVGDLKYGRTVHSLVKLLALYRgLKFTLVSPPTLEMPAYIVEQISRNGHVIEQTDDLAAGLRGADVVYATRIQKERFAD 324
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 822092823 2161 EkEYNACFGQFILTPHIMTGA-KRKMVVMHPLPR-----VNEISVEVDTDPRAAYFRQAENGMYIRMALLATVLG 2229
Cdd:PRK11891 325 E-SFEGYTPDFQINQALVDAVcKPDTLIMHPLPRdsrpgANDLSTDLNRDPRLAIFRQTDNGIPVRMAIFAVLLG 398
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
1470-1796 |
8.21e-89 |
|
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This group contains the archeal members of the DHOase family.
Pssm-ID: 238643 [Multi-domain] Cd Length: 361 Bit Score: 294.63 E-value: 8.21e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1470 LPGLIDVHVHLREPGATHKEDFSSGTAAALAGGITMVCAMPNTNPAIIDPNSFTMAQKLAKAGCRCDYALFVGAS-SDNA 1548
Cdd:cd01318 5 LPGVIDIHVHFREPGLTYKEDFVSGSRAAAAGGVTTVMDMPNTKPPTTTAEALYEKLRLAAAKSVVDYGLYFGVTgSEDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1549 ALLPsiASSTAGLKMYLNDtySTlkmDNVSLWMEHFEKWPKH--LPIVAHAEKQT------------------------- 1601
Cdd:cd01318 85 EELD--KAPPAGYKIFMGD--ST---GDLLDDEETLERIFAEgsVLVTFHAEDEDrlrenrkelkgesahprirdaeaaa 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1602 --VAAILLVAQLYQRPVHICHVAKKEEILIIRAAKQKgiqVTCEVAPHHLFLCEDNVPVIGKdKAQVRPMLGTREDMEAL 1679
Cdd:cd01318 158 vaTARALKLARRHGARLHICHVSTPEELKLIKKAKPG---VTVEVTPHHLFLDVEDYDRLGT-LGKVNPPLRSREDRKAL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1680 WENL--DIIDCFATDHAPHSAEEKIS--EKPPPGYPGLETMLPLLFTAVSEGRLTVDDIIKRLYENPRKIFSLP---AQE 1752
Cdd:cd01318 234 LQALadGRIDVIASDHAPHTLEEKRKgyPAAPSGIPGVETALPLMLTLVNKGILSLSRVVRLTSHNPARIFGIKnkgRIA 313
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 822092823 1753 DTY----VEVDLEQEWIIPKHMQFTKSKWTPFEGMKVKGKVMRVVLRG 1796
Cdd:cd01318 314 EGYdadlTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPVMTIVRG 361
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
1467-1802 |
2.74e-88 |
|
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of dihydroorotase found in E. coli, this class tends to appear in a large, multifunctional complex with aspartate transcarbamoylase. Homologous domains appear in multifunctional proteins of higher eukaryotes. In some species, including Pseudomonas putida and P. aeruginosa, this protein is inactive but is required as a non-catalytic subunit of aspartate transcarbamoylase (ATCase). In these species, a second, active dihydroorotase is also present. The seed for this model does not include any example of the dihydroorotase domain of eukaryotic multidomain pyrimidine synthesis proteins. All proteins described by this model should represent active and inactive dihydroorotase per se and functionally equivalent domains of multifunctional proteins from higher eukaryotes, but exclude related proteins such as allantoinase. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273302 [Multi-domain] Cd Length: 411 Bit Score: 294.74 E-value: 2.74e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1467 LIRLPGLIDVHVHLREPGATHKEDFSSGTAAALAGGITMVCAMPNTNPAIIDPNSFTMAQKLAKAGCRCDYALFVGASSD 1546
Cdd:TIGR00857 35 LLVLPGFIDLHVHLRDPGEEYKEDIESGSKAAAHGGFTTVADMPNTKPPIDTPETLEWKLQRLKKVSLVDVHLYGGVTQG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1547 N--AALLPSIASSTAGL--KMYLNDTYSTLKMDNVSLWME-----------HFE---------------KWPKHLPIVA- 1595
Cdd:TIGR00857 115 NqgKELTEAYELKEAGAvgRMFTDDGSEVQDILSMRRALEyaaiagvpialHAEdpdliyggvmhegpsAAQLGLPARPp 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1596 HAEKQTVAAILLVAQLYQRPVHICHVAKKEEILIIRAAKQKGIQVTCEVAPHHLFLCEDNVPVIGKDkAQVRPMLGTRED 1675
Cdd:TIGR00857 195 EAEEVAVARLLELAKHAGCPVHICHISTKESLELIVKAKSQGIKITAEVTPHHLLLSEEDVARLDGN-GKVNPPLREKED 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1676 MEALWENL--DIIDCFATDHAPHSAEEKIS--EKPPPGYPGLETMLPLLFTAVSEGRLTVDDIIKRLYENPRKIFSLP-- 1749
Cdd:TIGR00857 274 RLALIEGLkdGIIDIIATDHAPHTLEEKTKefAAAPPGIPGLETALPLLLQLLVKGLISLKDLIRMLSINPARIFGLPdk 353
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 822092823 1750 -----AQEDTYVEVDLEQEWIIPKHMQFTKSKWTPFEGMKVKGKVMRVVLRGEVAYID 1802
Cdd:TIGR00857 354 gtleeGNPADITVFDLKKEWTINAETFYSKAKNTPFEGMSLKGKPIATILRGKVVYED 411
|
|
| carA |
CHL00197 |
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional |
1-368 |
2.06e-87 |
|
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
Pssm-ID: 214392 [Multi-domain] Cd Length: 382 Bit Score: 291.32 E-value: 2.06e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1 MSLKMASLVLEDGTTFKGRLFGAVSSVSGEVVFQTGMVGYPEALTDPSYKSQILTLTYPMIGNYGIPKDEdgefglskwF 80
Cdd:CHL00197 2 KKMIPAILVLEDGTYYRGWSFSNPITTIGEVVFNTGMTGYQEIITDPSYFEQIVTFTYPEIGNTGINLED---------I 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 81 ESSQIHAAALIVGEVSENPSHWSAAKSLDEWLREQGIPGLQGVDTRCLTKKIREKGTMLG-------------------- 140
Cdd:CHL00197 73 ESVKIQVKGIIAKNICKSSSNWRQQESLVSYLQRHKIPFIFGIDTRALTQHLRRFGTMNGcisnqnlnlsylrakikesp 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 141 -----KLVVEGTPADNIPFDNPDARNLVKEVSMKAPKVFNpegtVRITAIDCGIKYNQIRCLCQRGARVTVVPWDQPL-D 214
Cdd:CHL00197 153 hmpssDLIPRVTTSSYYEWDEKSHPSFYLADNKRPHSSYQ----LKIIVIDFGVKYNILRRLKSFGCSITVVPATSPYqD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 215 SNDF--DGLFISNGPGNPE---YCKETVENIRKVACvenpkPIFGICLGHQLLSLVIGAKTYKMKYGNRGHNQPC-IHKg 288
Cdd:CHL00197 229 ILSYqpDGILLSNGPGDPSaihYGIKTVKKLLKYNI-----PIFGICMGHQILSLALEAKTFKLKFGHRGLNHPSgLNQ- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 289 tsRCYITSQNHGFAVDPETLPKD-WDVLFTNANDQTSEGIVHNHKPLFSVQFHPEHMAGPTDLVGLFDVFLDTVRDVKEN 367
Cdd:CHL00197 303 --QVEITSQNHGFAVNLESLAKNkFYITHFNLNDGTVAGISHSPKPYFSVQYHPEASPGPHDADYLFEYFIEIIKHSKSS 380
|
.
gi 822092823 368 K 368
Cdd:CHL00197 381 K 381
|
|
| CPSase_sm_chain |
pfam00988 |
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ... |
8-142 |
3.90e-76 |
|
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase domain is in the amino terminus of protein. Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00289. The small chain has a GATase domain in the carboxyl terminus. See pfam00117.
Pssm-ID: 460017 [Multi-domain] Cd Length: 126 Bit Score: 248.39 E-value: 3.90e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 8 LVLEDGTTFKGRLFGAVSSVSGEVVFQTGMVGYPEALTDPSYKSQILTLTYPMIGNYGIPKDEdgefglskwFESSQIHA 87
Cdd:pfam00988 1 LVLEDGTVFEGKSFGAAGSTVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNPED---------FESDKIHV 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 822092823 88 AALIVGEVSENPSHWSAAKSLDEWLREQGIPGLQGVDTRCLTKKIREKGTMLGKL 142
Cdd:pfam00988 72 AGLVVREYSDEPSNWRAEESLDEWLKEQGIPGISGVDTRALTRKIREKGAMKGVI 126
|
|
| PLN02771 |
PLN02771 |
carbamoyl-phosphate synthase (glutamine-hydrolyzing) |
6-349 |
1.92e-74 |
|
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
Pssm-ID: 178370 [Multi-domain] Cd Length: 415 Bit Score: 255.29 E-value: 1.92e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 6 ASLVLEDGTTFKGRLFGAVSSVSGEVVFQTGMVGYPEALTDPSYKSQILTLTYPMIGNYGIPKDEDgefglskwfESSQI 85
Cdd:PLN02771 57 ARLVLEDGSVWKAKSFGARGTQVGEVVFNTSLTGYQEILTDPSYAGQFVLMTNPHIGNTGVNFDDE---------ESRQC 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 86 HAAALIVGEVSENPSHWSAAKSLDEWLREQGIPGLQGVDTRCLTKKIREKGTMLGKLVVEGTPADNIPFD-----NPDAR 160
Cdd:PLN02771 128 FLAGLVIRSLSISTSNWRCTKTLGDYLAERNIMGIYDVDTRAITRRLREDGSLIGVLSTEDSKTDEELLKmsrswDIVGI 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 161 NLVKEVSMKAPKV----------FNPEG----TVRITAIDCGIKYNQIRCLCQRGARVTVVPWDQP----LDSNDfDGLF 222
Cdd:PLN02771 208 DLISGVSCKSPYEwvdktnpewdFNTNSrdgeSYHVIAYDFGIKHNILRRLASYGCKITVVPSTWPaseaLKMKP-DGVL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 223 ISNGPGNPE---YCKETV-ENIRKVacvenpkPIFGICLGHQLLSLVIGAKTYKMKYGNRGHNQPCIHKGTSRCYITSQN 298
Cdd:PLN02771 287 FSNGPGDPSavpYAVETVkELLGKV-------PVFGICMGHQLLGQALGGKTFKMKFGHHGGNHPVRNNRTGRVEISAQN 359
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 822092823 299 HGFAVDPETLPKDWDVLFTNANDQTSEGIVHNHKPLFSVQFHPEHMAGPTD 349
Cdd:PLN02771 360 HNYAVDPASLPEGVEVTHVNLNDGSCAGLAFPALNVMSLQYHPEASPGPHD 410
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
1464-1809 |
2.21e-73 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 251.23 E-value: 2.21e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1464 SQKLIrLPGLIDVHVHLREPGATHKEDFSSGTAAALAGGITMVCAMPNTNPAIIDPNSFTMAQKLAKAGCRCDYAL-FVG 1542
Cdd:PRK04250 41 KGGII-LPGLIDVHVHLRDFEESYKETIESGTKAALHGGITLVFDMPNTKPPIMDEKTYEKRMRIAEKKSYADYALnFLI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1543 ASsdNAALLPSI---------ASSTAGLkmYLND---TYSTLkMDNVSLWMEHFE---KWPKHLPIvahAEKQTVAAILL 1607
Cdd:PRK04250 120 AG--NCEKAEEIkadfykifmGASTGGI--FSENfevDYACA-PGIVSVHAEDPElirEFPERPPE---AEVVAIERALE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1608 VAQLYQRPVHICHVAKKEEILIIraaKQKGIQ-VTCEVAPHHLFLCEDNVPVIGKDKaqVRPMLGTREDMEALWENLDII 1686
Cdd:PRK04250 192 AGKKLKKPLHICHISTKDGLKLI---LKSNLPwVSFEVTPHHLFLTRKDYERNPLLK--VYPPLRSEEDRKALWENFSKI 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1687 DCFATDHAPHSAEEKisEKPPPGYPGLETMLPLLFTAVSEGRLTVDDIIKRLYENPRKIFSLP------AQEDTYVEVDL 1760
Cdd:PRK04250 267 PIIASDHAPHTLEDK--EAGAAGIPGLETEVPLLLDAANKGMISLFDIVEKMHDNPARIFGIKnygieeGNYANFAVFDM 344
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 822092823 1761 EQEWIIPKHMQFTKSKWTPFEGMKVKGKVMRVVLRGEVAYIDGQVLVPP 1809
Cdd:PRK04250 345 KKEWTIKAEELYTKAGWTPYEGFKLKGKVIMTILRGEVVMEDDEIIGKP 393
|
|
| CPSase_sm_chain |
smart01097 |
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase ... |
6-142 |
1.86e-72 |
|
Carbamoyl-phosphate synthase small chain, CPSase domain; The carbamoyl-phosphate synthase domain is in the amino terminus of protein. Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesise carbamoyl phosphate. The small chain has a GATase domain in the carboxyl terminus.
Pssm-ID: 198165 [Multi-domain] Cd Length: 130 Bit Score: 238.04 E-value: 1.86e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 6 ASLVLEDGTTFKGRLFGAVSSVSGEVVFQTGMVGYPEALTDPSYKSQILTLTYPMIGNYGIPKDedgefglskWFESSQI 85
Cdd:smart01097 3 AYLVLEDGTVFEGESFGAEGETVGEVVFNTGMTGYQEILTDPSYAGQIVVFTYPLIGNYGVNDE---------DFESDKI 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 822092823 86 HAAALIVGEVSENPSHWSAAKSLDEWLREQGIPGLQGVDTRCLTKKIREKGTMLGKL 142
Cdd:smart01097 74 QVKGLVVRELSDEPSNWRSEQSLDEFLKENGIPGISGIDTRALTRKLREKGAMKGVI 130
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
1448-1805 |
2.15e-71 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 246.90 E-value: 2.15e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1448 QIGQAPRVKTHVDSMTSQKLIRLPGLIDVHVHLREPGATHKEDFSSGTAAALAGGITMVCAMPNTNPAIIDPNsfTMAQK 1527
Cdd:PRK07575 33 AIAPEISATAVDTVIDAEGLTLLPGVIDPQVHFREPGLEHKEDLFTASRACAKGGVTSFLEMPNTKPLTTTQA--ALDDK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1528 LAKAGCRC--DYALFVGASSDNAALLPSiASSTAGLKMYLNDTYSTLKMDNVSLWMEHFEKwpKHLPIVAHAEKQT---- 1601
Cdd:PRK07575 111 LARAAEKCvvNYGFFIGATPDNLPELLT-ANPTCGIKIFMGSSHGPLLVDEEAALERIFAE--GTRLIAVHAEDQArira 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1602 ----------VA---------AILLVAQL-------YQRPVHICHVAKKEEILIIRAAKqkGIQVTCEVAPHHLFLCEDN 1655
Cdd:PRK07575 188 rraefagisdPAdhsqiqdeeAALLATRLalklskkYQRRLHILHLSTAIEAELLRQDK--PSWVTAEVTPQHLLLNTDA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1656 VPVIGKdKAQVRPMLGTREDMEALWENL--DIIDCFATDHAPHSAEEKISEKP--PPGYPGLETMLPLLFTAVSEGRLTV 1731
Cdd:PRK07575 266 YERIGT-LAQMNPPLRSPEDNEALWQALrdGVIDFIATDHAPHTLEEKAQPYPnsPSGMPGVETSLPLMLTAAMRGKCTV 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1732 DDIIKRLYENPRKIFSLPAQ---EDTY----VEVDLEQEWIIPKHMQFTKSKWTPFEGMKVKGKVMRVVLRGEVAYIDGQ 1804
Cdd:PRK07575 345 AQVVRWMSTAVARAYGIPNKgriAPGYdadlVLVDLNTYRPVRREELLTKCGWSPFEGWNLTGWPVTTIVGGQIVFDRGQ 424
|
.
gi 822092823 1805 V 1805
Cdd:PRK07575 425 V 425
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
1465-1792 |
4.79e-69 |
|
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This subgroup also contains proteins that lack the active site, like unc-33, a C.elegans protein involved in axon growth.
Pssm-ID: 238642 [Multi-domain] Cd Length: 374 Bit Score: 237.91 E-value: 4.79e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1465 QKLIRLPGLIDVHVHLREPGATHKEDFSSGTAAALAGGITMVCAMPNTNPAIIDPN---------------------SFT 1523
Cdd:cd01317 8 EGKILAPGLVDLHVHLREPGFEYKETLESGAKAAAAGGFTTVVCMPNTNPVIDNPAvvellknrakdvgivrvlpigALT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1524 MAQK---------LAKAGCrcdyalfVGASSD-----NAALLPSIASSTAGLKMYL---------------NDTYSTLKM 1574
Cdd:cd01317 88 KGLKgeelteigeLLEAGA-------VGFSDDgkpiqDAELLRRALEYAAMLDLPIivhpedpslagggvmNEGKVASRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1575 DnvslwmehfekwpkhLP-IVAHAEKQTVAAILLVAQLYQRPVHICHVAKKEEILIIRAAKQKGIQVTCEVAPHHLFLCE 1653
Cdd:cd01317 161 G---------------LPgIPPEAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKGLPVTAEVTPHHLLLDD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1654 DNVPviGKD-KAQVRPMLGTREDMEALWENL--DIIDCFATDHAPHSAEEKisEKP----PPGYPGLETMLPLLFT-AVS 1725
Cdd:cd01317 226 EALE--SYDtNAKVNPPLRSEEDREALIEALkdGTIDAIASDHAPHTDEEK--DLPfaeaPPGIIGLETALPLLWTlLVK 301
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 822092823 1726 EGRLTVDDIIKRLYENPRKIFSLPAQEDTYVE------VDLEQEWII-PKHMQfTKSKWTPFEGMKVKGKVMRV 1792
Cdd:cd01317 302 GGLLTLPDLIRALSTNPAKILGLPPGRLEVGApadlvlFDPDAEWIVdEETFR-SKSKNTPFDGQKLKGRVLAT 374
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
1470-1822 |
2.43e-64 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 226.73 E-value: 2.43e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1470 LPGLIDVHVHLREPGATHKEDFSSGTAAALAGGITMVCAMPNTNPAIIDPNsfTMAQKLAKAGCR--CDYALFVGASSDN 1547
Cdd:PRK09060 55 LPGVIDSQVHFREPGLEHKEDLETGSRAAVLGGVTAVFEMPNTNPLTTTAE--ALADKLARARHRmhCDFAFYVGGTRDN 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1548 AALLPSI--ASSTAGLKMYL-NDTYSTLKMDNVSLwmE------------HFEKWP-----KHLPIVAHAEKQTV----- 1602
Cdd:PRK09060 133 ADELAELerLPGCAGIKVFMgSSTGDLLVEDDEGL--RrilrngrrraafHSEDEYrlrerKGLRVEGDPSSHPVwrdee 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1603 AAIL----LV--AQLYQRPVHICHVAKKEEILIIRAAKQKgiqVTCEVAPHHLFL-CEDNVPVIGKdKAQVRPMLGTRED 1675
Cdd:PRK09060 211 AALLatrrLVrlARETGRRIHVLHVSTAEEIDFLADHKDV---ATVEVTPHHLTLaAPECYERLGT-LAQMNPPIRDARH 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1676 MEALWENLD--IIDCFATDHAPHSAEEKisEKP----PPGYPGLETMLPLLFTAVSEGRLTVDDIIKRLYENPRKIFSLP 1749
Cdd:PRK09060 287 RDGLWRGVRqgVVDVLGSDHAPHTLEEK--AKPypasPSGMTGVQTLVPIMLDHVNAGRLSLERFVDLTSAGPARIFGIA 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1750 AQ--------EDTYVeVDLEQEWIIPKHMQFTKSKWTPFEGMKVKGKVMRVVLRGEVAYIDGQVLVPPGyGQDVKSWSAT 1821
Cdd:PRK09060 365 GKgriavgydADFTI-VDLKRRETITNEWIASRCGWTPYDGKEVTGWPVGTIVRGQRVMWDGELVGPPT-GEPVRFLETL 442
|
.
gi 822092823 1822 P 1822
Cdd:PRK09060 443 P 443
|
|
| GATase |
pfam00117 |
Glutamine amidotransferase class-I; |
185-359 |
5.92e-64 |
|
Glutamine amidotransferase class-I;
Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 215.95 E-value: 5.92e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 185 IDCG--IKYNQIRCLCQRGARVTVVPWDQP---LDSNDFDGLFISNGPGNPEYCKETVENIRKVacVENPKPIFGICLGH 259
Cdd:pfam00117 3 IDNGdsFTYNLARALRELGVEVTVVPNDTPaeeILEENPDGIILSGGPGSPGAAGGAIEAIREA--RELKIPILGICLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 260 QLLSLVIGAKTYKMK-YGNRGHNQPCIH------KGTSRCYITSQNHGFAVDPETLPKDWDVLFTNANDQTSEGIVHNHK 332
Cdd:pfam00117 81 QLLALAFGGKVVKAKkFGHHGKNSPVGDdgcglfYGLPNVFIVRRYHSYAVDPDTLPDGLEVTATSENDGTIMGIRHKKL 160
|
170 180
....*....|....*....|....*..
gi 822092823 333 PLFSVQFHPEHMAGPTDLVGLFDVFLD 359
Cdd:pfam00117 161 PIFGVQFHPESILTPHGPEILFNFFIK 187
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
1470-1816 |
1.53e-63 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 224.53 E-value: 1.53e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1470 LPGLIDVHVHLREPGATHKEDFSSGTAAALAGGITMVCAMPNTNPAIIDPNSFTMAQKLAKAGCRCDYALfVGASSDNAA 1549
Cdd:PRK02382 53 LPGGIDVHVHFREPGYTHKETWYTGSRSAAAGGVTTVVDQPNTDPPTVDGESFDEKAELAARKSIVDFGI-NGGVTGNWD 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1550 LLPSI-------------ASSTAGLKM--------------------------YLNDTYSTLKMDNVSlwmehFEKWPKH 1590
Cdd:PRK02382 132 PLESLwergvfalgeifmADSTGGMGIdeelfeealaeaarlgvlatvhaedeDLFDELAKLLKGDAD-----ADAWSAY 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1591 LPivAHAEKQTVAAILLVAQLYQRPVHICHVAKKEEILIIRAAKqkgiqVTCEVAPHHLFLCEDNVPVIGKdKAQVRPML 1670
Cdd:PRK02382 207 RP--AAAEAAAVERALEVASETGARIHIAHISTPEGVDAARREG-----ITCEVTPHHLFLSRRDWERLGT-FGKMNPPL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1671 GTREDMEALWENLD--IIDCFATDHAPHSAEEK---ISEKPPpGYPGLETMLPLLFTAVSEGRLTVDDIIKRLYENPRKI 1745
Cdd:PRK02382 279 RSEKRREALWERLNdgTIDVVASDHAPHTREEKdadIWDAPS-GVPGVETMLPLLLAAVRKNRLPLERVRDVTAANPARI 357
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 822092823 1746 FSLPAQ---EDTY----VEVDLEQEWIIPKHMQFTKSKWTPFEGMKVKGKVMrVVLRGEVAYIDGQVLVPPGYGQDVK 1816
Cdd:PRK02382 358 FGLDGKgriAEGYdadlVLVDPDAAREIRGDDLHSKAGWTPFEGMEGVFPEL-TMVRGTVVWDGDDINAKRGRGEFLR 434
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
1443-1809 |
1.48e-62 |
|
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the dihydropyrimidinase family, which catalyzes the reversible hydrolytic ring opening of dihydropyrimidines and hydantoins (five-membered cyclic diamides used in biotechnology). But L-HYDs differ by having an L-enantio specificity and by lacking activity on possible natural substrates such as dihydropyrimidines. Allantoinase catalyzes the hydrolytic cleavage of the five-member ring of allantoin (5-ureidohydantoin) to form allantoic acid.
Pssm-ID: 238640 [Multi-domain] Cd Length: 447 Bit Score: 221.78 E-value: 1.48e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1443 VQALKQIGQAPRVKTHVDSmtSQKLIrLPGLIDVHVHLREPGATHKEDFSSGTAAALAGGITMVCAMP-NTNPAIIDPNS 1521
Cdd:cd01315 27 IAAIGPDIANTEAEEVIDA--GGLVV-MPGLIDTHVHINEPGRTEWEGFETGTKAAAAGGITTIIDMPlNSIPPTTTVEN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1522 FTMAQKLAKAGCRCDYALFVGASSDNA-ALLPSIASSTAGLKMYLNDTySTLKMDNVSLW--MEHFEKWPKH-LPIVAHA 1597
Cdd:cd01315 104 LEAKLEAAQGKLHVDVGFWGGLVPGNLdQLRPLDEAGVVGFKCFLCPS-GVDEFPAVDDEqlEEAMKELAKTgSVLAVHA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1598 E----------------KQTVAA----------------ILLVAQLYQRPVHICHVAKKEEILIIRAAKQKGIQVTCEVA 1645
Cdd:cd01315 183 EnpeitealqeqakakgKRDYRDylasrpvfteveaiqrILLLAKETGCRLHIVHLSSAEAVPLIREARAEGVDVTVETC 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1646 PHHLFLCEDNVPVIGKdKAQVRPMLGTREDMEALWENL--DIIDCFATDHAPHSAEEKISEKPP-----PGYPGLETMLP 1718
Cdd:cd01315 263 PHYLTFTAEDVPDGGT-EFKCAPPIRDAANQEQLWEALenGDIDMVVSDHSPCTPELKLLGKGDffkawGGISGLQLGLP 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1719 LLFT-AVSEGRLTVDDIIKRLYENPRKIFSLPAQEDT--------YVEVDLEQEWIIPKHMQFTKSKWTPFEGMKVKGKV 1789
Cdd:cd01315 342 VMLTeAVNKRGLSLEDIARLMCENPAKLFGLSHQKGRiavgydadFVVWDPEEEFTVDAEDLYYKNKISPYVGRTLKGRV 421
|
410 420
....*....|....*....|
gi 822092823 1790 MRVVLRGEVAYIDGQVLVPP 1809
Cdd:cd01315 422 HATILRGTVVYQDGEVVGEP 441
|
|
| CPSase_L_D3 |
smart01096 |
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ... |
802-926 |
8.69e-58 |
|
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain.
Pssm-ID: 198164 [Multi-domain] Cd Length: 124 Bit Score: 195.75 E-value: 8.69e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 802 EEELQTPTDKRIFVLAAALHAGYTVERLYELTKIDHWFLHKMKNIADHKKLLETYKQDEsaMPPEIMRKAKQLGFSDKQI 881
Cdd:smart01096 2 LEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKGGLDE--LDADLLRKAKRLGFSDRQI 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 822092823 882 AQAVQSTELAVRKLRRDWKIFPVVKQIDTVAAEWPAQTNYLYLTY 926
Cdd:smart01096 80 AKLLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
|
|
| ArgF |
COG0078 |
Ornithine carbamoyltransferase [Amino acid transport and metabolism]; Ornithine ... |
1927-2230 |
1.31e-56 |
|
Ornithine carbamoyltransferase [Amino acid transport and metabolism]; Ornithine carbamoyltransferase is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 439848 [Multi-domain] Cd Length: 310 Bit Score: 199.51 E-value: 1.31e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1927 LVGQHILSVRQFSKEQMSHLFNVAHTLRLMVQKERPLDILKGKVMASMFYEVSTRTSSSFAAAMHRLGGSVVHFceSTSS 2006
Cdd:COG0078 3 LKGRHFLSLLDLTPEELRALLDLAAELKAKRKAGIPHRPLKGKTLAMIFEKPSTRTRVSFEVGMAQLGGHAIYL--DPGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 2007 TQ--KGESLVDSVNTMSCYADVIVLR---HPIpgaVESAARHCRRPVINA-GDgvGEHPTQALLDIFTIREELGTVNGMT 2080
Cdd:COG0078 81 SQlgRGESIKDTARVLSRYVDGIMIRtfgHET---LEELAKYAGVPVINGlTD--LFHPCQALADLLTIREHFGKLKGLK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 2081 ITMVGDlkhGRTV-HSLARLLTQYRITLRYVAPKNLSMPAEIID----FVASKGIKQEEFNSIEEALPDTDVLY------ 2149
Cdd:COG0078 156 VAYVGD---GNNVaNSLLLAAAKLGMDVRIATPEGYEPDPEIVAkakeIAAESGGSITITHDPAEAVKGADVVYtdvwvs 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 2150 MTriQKErfsSEKEYNACFGQFILTPHIMTGAKRKMVVMHPLP--RVNEISVEVDTDPRAAYFRQAENGMYIRMALLATV 2227
Cdd:COG0078 233 MG--QEE---EAEERIKAFKPYQVNEELMALAKPDAIFMHCLPahRGEEVTDEVIDGPQSVVFDEAENRLHAQKALLAWL 307
|
...
gi 822092823 2228 LGR 2230
Cdd:COG0078 308 LGG 310
|
|
| OTCace_N |
pfam02729 |
Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding domain; |
1931-2071 |
1.57e-54 |
|
Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding domain;
Pssm-ID: 460665 [Multi-domain] Cd Length: 140 Bit Score: 186.86 E-value: 1.57e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1931 HILSVRQFSKEQMSHLFNVAHTLRLMVQKERPLDILKGKVMASMFYEVSTRTSSSFAAAMHRLGGSVVHFCESTSSTQKG 2010
Cdd:pfam02729 1 HFLSLEDLSREEIEALLDLAAELKEARKRGKKLPLLKGKTVALLFEEPSTRTRVSFEVAAKRLGGHVIYLSSSDIQLSSG 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 822092823 2011 ESLVDSVNTMSCYADVIVLRHPIPGAVESAARHCRRPVINAGdGVGEHPTQALLDIFTIRE 2071
Cdd:pfam02729 81 ESLADTARVLSRYVDAIVIRHFGHEDLEELAEYASVPVINAG-GDHEHPTQALADLLTIRE 140
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
1454-1805 |
1.58e-50 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 186.61 E-value: 1.58e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1454 RVKTHVDSMTSQKLIR------LPGLIDVHVHLREPGATHKEDFSSGTAAALAGGITMVCAMPNTNPAIIDPNsfTMAQK 1527
Cdd:PRK09236 31 KIASSISAKSADTVIDaagrylLPGMIDDQVHFREPGLTHKGDIASESRAAVAGGITSFMEMPNTNPPTTTLE--ALEAK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1528 LAKAGCRC--DYALFVGASSDNAALLPSI-ASSTAGLKMYLNDtySTLKM--DNVSLWMEHFEKWPkhLPIVAHAEKQTV 1602
Cdd:PRK09236 109 YQIAAQRSlaNYSFYFGATNDNLDEIKRLdPKRVCGVKVFMGA--STGNMlvDNPETLERIFRDAP--TLIATHCEDTPT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1603 A-----------------------------------AILLvAQLYQRPVHICHVAKKEEILIIRAAKQKGIQVTCEVAPH 1647
Cdd:PRK09236 185 IkanlakykekygddipaemhplirsaeacykssslAVSL-AKKHGTRLHVLHISTAKELSLFENGPLAEKRITAEVCVH 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1648 HLFLCEDNVPVIGkdkAQVR--PMLGTREDMEALWENL--DIIDCFATDHAPHSAEEKisEKP----PPGYPGLETMLPL 1719
Cdd:PRK09236 264 HLWFDDSDYARLG---NLIKcnPAIKTASDREALRQALadDRIDVIATDHAPHTWEEK--QGPyfqaPSGLPLVQHALPA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1720 LFTAVSEGRLTVDDIIKRLYENPRKIFSLpaQEDTY---------VEVDLEQEWIIPKHMQFTKSKWTPFEGMKVKGKVM 1790
Cdd:PRK09236 339 LLELVHEGKLSLEKVVEKTSHAPAILFDI--KERGFiregywadlVLVDLNSPWTVTKENILYKCGWSPFEGRTFRSRVA 416
|
410
....*....|....*
gi 822092823 1791 RVVLRGEVAYIDGQV 1805
Cdd:PRK09236 417 TTFVNGQLVYHNGQL 431
|
|
| allantoinase |
TIGR03178 |
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ... |
1467-1809 |
1.40e-48 |
|
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ring-opening hydrolysis. The seed members of this model are all in the vicinity of other genes involved in the processes of xanthine/urate/allantoin catabolism. Although not included in the seed, many eukaryotic homologs of this family are included above the trusted cutoff. Below the noise cutoff are related hydantoinases.
Pssm-ID: 163175 [Multi-domain] Cd Length: 443 Bit Score: 180.66 E-value: 1.40e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1467 LIRLPGLIDVHVHLREPGATHKEDFSSGTAAALAGGITMVCAMP-NTNPAIIDPNSFTMAQKLAKAGCRCDYALFVGASS 1545
Cdd:TIGR03178 47 LVVFPGVVDTHVHINEPGRTEWEGFETGTRAAAAGGITTYIDMPlNSIPATTTRASLEAKFEAAKGKLAVDVGFWGGLVP 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1546 DNAALLPSIASSTA-GLKMYLN----DTYSTLKMDNVSLWMEHFEKwpKHLPIVAHAEK--------------------- 1599
Cdd:TIGR03178 127 YNLDDLRELDEAGVvGFKAFLSpsgdDEFPHVDDWQLYKGMRELAR--LGQLLLVHAENpaitsalgeeappqggvgada 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1600 -----------QTVAAILLVAQLYQRPVHICHVAKKEEILIIRAAKQKGIQVTCEVAPHHLFLCEDNVPVIGKdKAQVRP 1668
Cdd:TIGR03178 205 ylasrpvfaevEAIRRTLALAKVTGCRVHVVHLSSAEAVELITEAKQEGLDVTVETCPHYLTLTAEEVPDGGT-LAKCAP 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1669 MLGTREDMEALWENL--DIIDCFATDHAPHSAEEKISE---KPPPGYPGLETMLPLLFTAVSEGR-LTVDDIIKRLYENP 1742
Cdd:TIGR03178 284 PIRDLANQEGLWEALlnGLIDCVVSDHSPCTPDLKRAGdffKAWGGIAGLQSTLDVMFDEAVQKRgLPLEDIARLMATNP 363
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 822092823 1743 RKIFSL-------PAQEDTYVEVDLEQEWIIPKHMQFTKSKWTPFEGMKVKGKVMRVVLRGEVAYIDGQVLVPP 1809
Cdd:TIGR03178 364 AKRFGLaqkgriaPGKDADFVFVDPDESYTLTPDDLYYRHKVSPYVGRTIGGRVRATYLRGQCIYDDEQFIGAP 437
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
1447-1812 |
7.30e-46 |
|
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases are a family of enzymes that catalyze the reversible hydrolytic ring opening of the amide bond in five- or six-membered cyclic diamides, like dihydropyrimidine or hydantoin. The hydrolysis of dihydropyrimidines is the second step of reductive catabolism of pyrimidines in human. The hydrolysis of 5-substituted hydantoins in microorganisms leads to enantiomerically pure N-carbamyl amino acids, which are used for the production of antibiotics, peptide hormones, pyrethroids, and pesticides. HYDs are classified depending on their stereoselectivity. This family also includes collapsin response regulators (CRMPs), cytosolic proteins involved in neuronal differentiation and axonal guidance which have strong homology to DHPases, but lack most of the active site residues.
Pssm-ID: 238639 [Multi-domain] Cd Length: 447 Bit Score: 172.79 E-value: 7.30e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1447 KQIGQ----APRVKThVDSmtSQKLIrLPGLIDVHVHLREP--GATHKEDFSSGTAAALAGGITMVCAMPNTNPAIIDPN 1520
Cdd:cd01314 27 VAIGPnleaPGGVEV-IDA--TGKYV-LPGGIDPHTHLELPfmGTVTADDFESGTRAAAAGGTTTIIDFAIPNKGQSLLE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1521 SFTMAQKLAKAGCRCDYALFVGASSDNAAL---LPSIA----SStagLKMYLndTYSTLKMDNVSLWMEHFEKwPKHLPI 1593
Cdd:cd01314 103 AVEKWRGKADGKSVIDYGFHMIITDWTDSVieeLPELVkkgiSS---FKVFM--AYKGLLMVDDEELLDVLKR-AKELGA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1594 VA--HAEKQTVA---------------------------------AILLvAQLYQRPVHICHVAKKEEILIIRAAKQKGI 1638
Cdd:cd01314 177 LVmvHAENGDVIaelqkkllaqgktgpeyhalsrppeveaeatarAIRL-AELAGAPLYIVHVSSKEAADEIARARKKGL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1639 QVTCEVAPHHLFLCEDNVPVIGKD--KAQVRPMLGTREDMEALWENL--DIIDCFATDHAPHSAEEKISEKP-----PPG 1709
Cdd:cd01314 256 PVYGETCPQYLLLDDSDYWKDWFEgaKYVCSPPLRPKEDQEALWDGLssGTLQTVGSDHCPFNFAQKARGKDdftkiPNG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1710 YPGLETMLPLLFTA-VSEGRLTVDDIIKRLYENPRKIFSLPAQEDTYVE--------VDLEQEWIIPKHMQFTKSKWTPF 1780
Cdd:cd01314 336 VPGVETRMPLLWSEgVAKGRITLEKFVELTSTNPAKIFGLYPRKGTIAVgsdadlviWDPNAEKTISADTHHHNVDYNIF 415
|
410 420 430
....*....|....*....|....*....|..
gi 822092823 1781 EGMKVKGKVMRVVLRGEVAYIDGQVLVPPGYG 1812
Cdd:cd01314 416 EGMKVKGWPVVTISRGKVVVEDGELVGEKGSG 447
|
|
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
1470-1816 |
9.04e-46 |
|
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily converts 5,6-dihydrouracil to 3-ureidopropanoate but also acts on dihydrothymine and hydantoin. The enzyme is a metalloenzyme.
Pssm-ID: 273937 [Multi-domain] Cd Length: 454 Bit Score: 172.96 E-value: 9.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1470 LPGLIDVHVHLREP--GATHKEDFSSGTAAALAGGITMVCAMPNTNPAIIDPNSFTMAQKLAKAGCRCDYALFVGASSDN 1547
Cdd:TIGR02033 50 LPGGIDVHTHLEMPfgGTTTADDFFTGTKAAAAGGTTTIIDFVVPEKGSSLTEALETWHEKAEGKSVIDYGFHMDITHWN 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1548 AALLPS-----IASSTAGLKMYLndTYSTLKMDNVSLWMEHFEKWPKHLPIV-AHAEK---------------------- 1599
Cdd:TIGR02033 130 DSVLEEhipevKEEGINSFKVFM--AYKNLLMVDDEELFEILKRLKELGALLqVHAENgdiiaelqarmlaqgitgpeyh 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1600 ----------QTVAAILLVAQLYQRPVHICHVAKKEEILIIRAAKQKGIQVTCEVAPHHLFLCEDNVPVIGKD--KAQVR 1667
Cdd:TIGR02033 208 alsrppeleaEAVARAITLAALADAPLYVVHVSTKDAADEIAQARKKGQPVFGETCPQYLVLDDTHYDKPGFEgaKYVCS 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1668 PMLGTREDMEALWE--NLDIIDCFATDHAPHSAEEKIS------EKPPPGYPGLETMLPLLFTA-VSEGRLTVDDIIKRL 1738
Cdd:TIGR02033 288 PPLREPEDQDALWSalSSGALQTVGSDHCTFNFAQKKAigkddfTKIPNGGPGVEERMSLLFDEgVAKGRITLEKFVEVT 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1739 YENPRKIFSLPAQEDTYVE--------VDLEQEWIIPKHMQFTKSKWTPFEGMKVKGKVMRVVLRGEVAYIDGQVLVPPG 1810
Cdd:TIGR02033 368 STNPAKIFNLYPRKGTIAVgsdadiviWDPNRTTVISAETHHSNADYNPFEGFKVRGAPVSVLSRGRVVVEDGQLVGTAG 447
|
....*.
gi 822092823 1811 YGQDVK 1816
Cdd:TIGR02033 448 AGRFVK 453
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
1470-1816 |
3.30e-45 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 171.04 E-value: 3.30e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1470 LPGLIDVHVHLREPGATHKEDFSSGTAAALAGGITMVCAMP-NTNPAIIDPNSFTMAQKLAKAGCRCDYALFVGASSDNA 1548
Cdd:PRK06189 53 FPGMIDVHVHFNEPGRTHWEGFATGSAALAAGGCTTYFDMPlNSIPPTVTREALDAKAELARQKSAVDFALWGGLVPGNL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1549 ALLPSIASSTA-GLKMYLND--TYSTLKMDNVSLWmEHFEKWPKHLPIVA-HAEK-------QTVAA------------- 1604
Cdd:PRK06189 133 EHLRELAEAGViGFKAFMSNsgTDEFRSSDDLTLY-EGMKEIAALGKILAlHAESdaltrhlTTQARqqgktdvrdyles 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1605 ------------ILLVAQLYQRPVHICHVAKKEEILIIRAAKQKGIQVTCEVAPHHLFLCEDNVPVIGKdKAQVRPMLGT 1672
Cdd:PRK06189 212 rpvvaeleavqrALLYAQETGCPLHFVHISSGKAVALIAEAKKRGVDVSVETCPHYLLFTEEDFERIGA-VAKCAPPLRS 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1673 REDMEALWENL--DIIDCFATDHAPHSAEEKISE---KPPPGYPGLETMLPLLFT-AVSEGRLTVDDIIKRLYENPRKIF 1746
Cdd:PRK06189 291 RSQKEELWRGLlaGEIDMISSDHSPCPPELKEGDdffLVWGGISGGQSTLLVMLTeGYIERGIPLETIARLLATNPAKRF 370
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 822092823 1747 SLP-------AQEDTYVEVDLEQEWIIPKHMQFTKSKWTPFEGMKVKGKVMRVVLRGEVAYIDGQVlVPPGYGQDVK 1816
Cdd:PRK06189 371 GLPqkgrlevGADADFVLVDLDETYTLTKEDLFYRHKQSPYEGRTFPGRVVATYLRGQCVYQDGEV-FPPPRGQLLR 446
|
|
| PRK00779 |
PRK00779 |
ornithine carbamoyltransferase; Provisional |
1926-2228 |
9.44e-45 |
|
ornithine carbamoyltransferase; Provisional
Pssm-ID: 234835 [Multi-domain] Cd Length: 304 Bit Score: 165.27 E-value: 9.44e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1926 PLVGQHILSVRQFSKEQMSHLFNVAHTLRLMVQKERPLDILKGKVMASMFYEVSTRTSSSFAAAMHRLGGSVVHFceSTS 2005
Cdd:PRK00779 1 MLMGRHFLSLDDLSPEELEELLDLAAELKKKRKAGEPHPPLKGKTLAMIFEKPSTRTRVSFEVGMAQLGGHAIFL--SPR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 2006 STQ--KGESLVDSVNTMSCYADVIVLR---HPIpgaVESAARHCRRPVINA-GDgvGEHPTQALLDIFTIREELGTVNGM 2079
Cdd:PRK00779 79 DTQlgRGEPIEDTARVLSRYVDAIMIRtfeHET---LEELAEYSTVPVINGlTD--LSHPCQILADLLTIYEHRGSLKGL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 2080 TITMVGDlkhGRTV-HSLARLLTQYRITLRYVAPKNLSMPAEIIDFVA-SKGIKQEEFNSIEEALPDTDVLY------MT 2151
Cdd:PRK00779 154 KVAWVGD---GNNVaNSLLLAAALLGFDLRVATPKGYEPDPEIVEKIAkETGASIEVTHDPKEAVKGADVVYtdvwvsMG 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 822092823 2152 RiQKERfssEKEYNAcFGQFILTPHIMTGAKRKMVVMHPLP--RVNEISVEVDTDPRAAYFRQAENGMYIRMALLATVL 2228
Cdd:PRK00779 231 Q-EAEA---EERLKA-FAPYQVNEELMALAKPDAIFMHCLPahRGEEVTDEVIDGPQSVVWDEAENRLHAQKALLAWLL 304
|
|
| pyrC |
PRK00369 |
dihydroorotase; Provisional |
1470-1810 |
3.46e-44 |
|
dihydroorotase; Provisional
Pssm-ID: 234738 [Multi-domain] Cd Length: 392 Bit Score: 166.48 E-value: 3.46e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1470 LPGLIDVHVHLREPGATHKEDFSSGTAAALAGGITMVCAMPNTNPAIIDPNsfTMAQKLA--KAGCRCDYALFVGASSD- 1546
Cdd:PRK00369 46 LPGAIDLHVHLRGLKLSYKEDVASGTSEAAYGGVTLVADMPNTIPPLNTPE--AITEKLAelEYYSRVDYFVYSGVTKDp 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1547 -NAALLPsiassTAGLKMYLND--TYSTLKMDNVS--LWMEHFE-----KWPKHLPIVAHAEkqtVAAILLVaQLYQRpV 1616
Cdd:PRK00369 124 eKVDKLP-----IAGYKIFPEDleREETFRVLLKSrkLKILHPEvplalKSNRKLRRNCWYE---IAALYYV-KDYQN-V 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1617 HICHVAKKEeilIIRAAKQKGIqvTCEVAPHHLFL-----CEDNV-PVIgKDKAQVRPMLgtredmEALWEnldiIDCFA 1690
Cdd:PRK00369 194 HITHASNPR---TVRLAKELGF--TVDITPHHLLVngekdCLTKVnPPI-RDINERLWLL------QALSE----VDAIA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1691 TDHAPHSAEEKISEKP--PPGYPGLETMLPLLFTAVSEGRLTVDDIIKRLYENPRKIFSLPAQE------DTYVEVDLEq 1762
Cdd:PRK00369 258 SDHAPHSSFEKLQPYEvcPPGIAALSFTPPFIYTLVSKGILSIDRAVELISTNPARILGIPYGEikegyrANFTVIQFE- 336
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 822092823 1763 EWiiPKHMQFTKSKWTPFEGMKVKGKVMRVVLRGEVAYIDGQVLVPPG 1810
Cdd:PRK00369 337 DW--RYSTKYSKVIETPLDGFELKASVYATIVQGKLAYLEGEVFPVKG 382
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
1470-1798 |
4.75e-44 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 166.57 E-value: 4.75e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1470 LPGLIDVHVHLREPGATHKEDFSSGTAAALAGGITMVCAMPNTNPAIIDPNSFTMAQKLAKAGCRCDYALFVGASSDNAA 1549
Cdd:PRK01211 45 LPAATDIHVHFRTPGETEKEDFSTGTLSAIFGGTTFIMDMPNNNIPIKDYNAFSDKLGRVAPKAYVDFSLYSMETGNNAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1550 LLPSIassTAGLKMYLNDTYSTLKMDNVSLWMEHFEKwpKHLPIVAHAEKQ------------------------TVAAI 1605
Cdd:PRK01211 125 ILDER---SIGLKVYMGGTTNTNGTDIEGGEIKKINE--ANIPVFFHAELSeclrkhqfesknlrdhdlarpiecEIKAV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1606 LLVAQLYQRPVHICHVAKKEEILiiraakqkgiQVTCEVAPHHLFLcEDNVPV--IGKdkaqVRPMLGTREDMEALWENL 1683
Cdd:PRK01211 200 KYVKNLDLKTKIIAHVSSIDVIG----------RFLREVTPHHLLL-NDDMPLgsYGK----VNPPLRDRWTQERLLEEY 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1684 --DIIDCFATDHAPHSAEEKIS-EKPPPGYPGLETMLPLLFTAVSEGRLTVDDIIKRLYENPRKIFSLPAQ--EDTY--- 1755
Cdd:PRK01211 265 isGRFDILSSDHAPHTEEDKQEfEYAKSGIIGVETRVPLFLALVKKKILPLDVLYKTAIERPASLFGIKKGkiEEGYdad 344
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 822092823 1756 -VEVDLEQEWIIPKHMQFTKSKWTPFEGMKVKGKvMRVVLRGEV 1798
Cdd:PRK01211 345 fMAFDFTNIKKINDKRLHSKCPVSPFNGFDAIFP-SHVIMRGEV 387
|
|
| MGS_CPS_I_III |
cd01423 |
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases ... |
1318-1444 |
1.10e-43 |
|
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases (CPS), including ammonia-dependent CPS Type I, and glutamine-dependent CPS Type III. These are multidomain proteins, in which MGS is the C-terminal domain.
Pssm-ID: 238711 [Multi-domain] Cd Length: 116 Bit Score: 155.15 E-value: 1.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1318 KNILLSIGSYkNKSELLPTVQTLESLGYNLYASLGTADFYTEHGVKVMAVDWPFEEESdcPNKDKQRNImdyLEENHFDL 1397
Cdd:cd01423 1 KGILISIGSY-SKPELLPTAQKLSKLGYKLYATEGTADFLLENGIPVTPVAWPSEEPQ--NDKPSLREL---LAEGKIDL 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 822092823 1398 VINLSMRNSGGRRLSsfvtkGYRTRRMAIDFSVPLITDIKCTKLFVQ 1444
Cdd:cd01423 75 VINLPSNRGKRVLDN-----DYVMRRAADDFAVPLITNPKCAKLFIE 116
|
|
| pyrB |
PRK13814 |
aspartate carbamoyltransferase; |
1931-2230 |
3.60e-43 |
|
aspartate carbamoyltransferase;
Pssm-ID: 139876 [Multi-domain] Cd Length: 310 Bit Score: 161.04 E-value: 3.60e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1931 HILSVRQFSKEQMSHLFNVA-HTLRLMVQKERPLDILKGKVMASMFYEVSTRTSSSFAAAMHRLGGSVVHFCESTSSTQK 2009
Cdd:PRK13814 7 HLLNMRSLTRDHIEKLIQRAnYFLTQGMEKNSVFETLKGHVVANLFFEPSTRTRNSFEIAAKRLGAMVLNPNLKISAISK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 2010 GESLVDSVNTMSCYA-DVIVLRHPIPGAVESAARHCRRPV-INAGDGVGEHPTQALLDIFTIREELGTVNGMTITMVGDL 2087
Cdd:PRK13814 87 GETLFDTIKTLEAMGvYFFIVRHSENETPEQIAKQLSSGVvINAGDGNHQHPSQALIDLMTIKQHKPHWNKLCVTIIGDI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 2088 KHGRTVHSLAR-LLTQYRITLRYVAPKNLsMPaeiiDFVASKGIKQeeFNSIEEALPDTDVLYMTRIQKERFSSEKEYNA 2166
Cdd:PRK13814 167 RHSRVANSLMDgLVTMGVPEIRLVGPSSL-LP----DKVGNDSIKK--FTELKPSLLNSDVIVTLRLQKERHDNSVDIDA 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 822092823 2167 CFGQFILTPHIMTGAKRKMVVMHPLP--RVNEISVEVDTDPRAAYFRQAENGMYIRMALLATVLGR 2230
Cdd:PRK13814 240 FRGSFRLTPEKLYSAKPDAIVMHPGPvnREVEINSDVADNQQSVILQQVRNGVAMRMAVLELFLLR 305
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
1470-1816 |
4.81e-40 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 156.10 E-value: 4.81e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1470 LPGLIDVHVHLREP--GATHKEDFSSGTAAALAGGITMVC--AMPNTNPAIIDpnSFTMAQKLAKAGCRCDYAlFVGASS 1545
Cdd:PRK08323 48 MPGGIDPHTHMEMPfgGTVSSDDFETGTRAAACGGTTTIIdfALQPKGQSLRE--ALEAWHGKAAGKAVIDYG-FHMIIT 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1546 D-NAALLPSIAS-STAG---LKMYLndTY-STLKMDNVSLwMEHFEKWPKH--LPIVaHAE---------KQTVA----- 1603
Cdd:PRK08323 125 DwNEVVLDEMPElVEEGitsFKLFM--AYkGALMLDDDEL-LRALQRAAELgaLPMV-HAEngdaiaylqAKLLAegktg 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1604 -------------------AILLvAQLYQRPVHICHVAKKEEILIIRAAKQKGIQVTCEVAPHHLFLCEDNVPVIGKDKA 1664
Cdd:PRK08323 201 peyhalsrppevegeatnrAIML-AELAGAPLYIVHVSCKEALEAIRRARARGQRVFGETCPQYLLLDESEYDGPDWFEG 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1665 QVR---PMLGTREDMEALWENL--DIIDCFATDHAPHSAEEKISE------KPPPGYPGLETMLPLLFTA-VSEGRLTVD 1732
Cdd:PRK08323 280 AKYvmsPPLRDKEHQDALWRGLqdGDLQVVATDHCPFCFEQKKQLgrgdftKIPNGTPGVEDRMPLLFSEgVMTGRITLN 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1733 DIIKRLYENPRKIFSLPAQEDTyVEV---------DLEQEWIIPKHMQFTKSKWTPFEGMKVKGKVMRVVLRGEVAYIDG 1803
Cdd:PRK08323 360 RFVELTSTNPAKIFGLYPRKGT-IAVgadadiviwDPNATKTISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVVVEDG 438
|
410
....*....|...
gi 822092823 1804 QVLVPPGYGQDVK 1816
Cdd:PRK08323 439 EFRGKAGHGRFLK 451
|
|
| OTCace |
pfam00185 |
Aspartate/ornithine carbamoyltransferase, Asp/Orn binding domain; |
2080-2227 |
1.17e-39 |
|
Aspartate/ornithine carbamoyltransferase, Asp/Orn binding domain;
Pssm-ID: 425511 [Multi-domain] Cd Length: 154 Bit Score: 145.06 E-value: 1.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 2080 TITMVGDlKHGRTVHSLARLLTQYRITLRYVAPKNLSMPAEIID----FVASKGIKQEEFNSIEEALPDTDVLYMTRIQK 2155
Cdd:pfam00185 1 KIAYVGD-GHNNVAHSLIIAAAKLGMDVRLATPKGYPPDPEVLDkakkIAEKSGGSIEITDDPAEAVKGADVVYTDVWQS 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 822092823 2156 ERFSSEKE--YNAcFGQFILTPHIMTGAKRKMVVMHPLP--RVNEISVEVDTDPRAAYFRQAENGMYIRMALLATV 2227
Cdd:pfam00185 80 MGQEKEREerLKA-FKPYQVNEELMKLAKKDAIFMHCLPahRGEEVTDDVFDGPRSVVFDQAENRLHAQKALLALL 154
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
1470-1813 |
2.68e-39 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 154.47 E-value: 2.68e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1470 LPGLIDVHVHLREP---GATHKEDFSSGTAAALAGGITMVC--AMPNTNPAIidPNSFTMAQKLAKAGCRCDYAL-FVGA 1543
Cdd:PRK13404 53 LPGGVDSHCHIDQPsgdGIMMADDFYTGTVSAAFGGTTTVIpfAAQHRGQSL--REAVEDYHRRAAGKAVIDYAFhLIVA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1544 SSDNAAL---LPS-IASSTAGLKMYLndTYSTLKMDNV-------------SLWMEHFE-----KW------------PK 1589
Cdd:PRK13404 131 DPTEEVLteeLPAlIAQGYTSFKVFM--TYDDLKLDDRqildvlavarrhgAMVMVHAEnhdmiAWltkrllaagltaPK 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1590 H----LPIVAHAEKqTVAAILLvAQLYQRPVHICHVAKKEEILIIRAAKQKGIQVTCEVAPHHLFLCEDNVPVIGKDKAQ 1665
Cdd:PRK13404 209 YhaisRPMLAEREA-THRAIAL-AELVDVPILIVHVSGREAAEQIRRARGRGLKIFAETCPQYLFLTAEDLDRPGMEGAK 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1666 --VRPMLGTREDMEALWENLD--IIDCFATDHAPHSAEEKISEKP----------PPGYPGLETMLPLLFTA-VSEGRLT 1730
Cdd:PRK13404 287 yiCSPPPRDKANQEAIWNGLAdgTFEVFSSDHAPFRFDDTDGKLAaganpsfkaiANGIPGIETRLPLLFSEgVVKGRIS 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1731 VDDIIKRLYENPRKIFSLPAQEDTYV---EVDL-----EQEWIIPKHMQFTKSKWTPFEGMKVKGKVMRVVLRGEVAYID 1802
Cdd:PRK13404 367 LNRFVALTSTNPAKLYGLYPRKGAIAigaDADIaiwdpDREVTITNADLHHAADYTPYEGMRVTGWPVTVLSRGRVVVED 446
|
410
....*....|.
gi 822092823 1803 GQVLVPPGYGQ 1813
Cdd:PRK13404 447 GELVAERGSGQ 457
|
|
| pyrB |
PRK13376 |
bifunctional aspartate carbamoyltransferase catalytic subunit/aspartate carbamoyltransferase ... |
1929-2229 |
2.61e-37 |
|
bifunctional aspartate carbamoyltransferase catalytic subunit/aspartate carbamoyltransferase regulatory subunit; Provisional
Pssm-ID: 237369 [Multi-domain] Cd Length: 525 Bit Score: 149.53 E-value: 2.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1929 GQHILSVRQFSKEQMSHLFNVAHTLRLMVQKERPLD---ILKGKV-MASMFYEVSTRTSSSF--AAAMHRlGGSVVHFCE 2002
Cdd:PRK13376 7 GRTLAVIEDLSVEEQLFLYEKTRELKQRWYEGEDVSefrIKKRDVgIYIVFVEPSTRTKESFinAAKFHK-NVKVNIFDS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 2003 STSSTQKGESLVDSVNTMSCYAD--VIVLRHPIPG--------AVESAARH-CRRPV-INAGDGVGEHPTQALLDIFTIR 2070
Cdd:PRK13376 86 EHSSFNKQESYTDTFNMLTGYSDysIFIVRTRLEGvcrlleekVSEFASRNgIEVPAfINAGDGKHEHPTQELLDEFTFL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 2071 EELGTVNG-MTITMVGDLKHGRTVHSLARLLTQYR-ITLRYVAPKNLSMPAEIIDFVASKGIKQEEFNSIEEALPDTDVL 2148
Cdd:PRK13376 166 EQNNFDNSfIHIALVGDLLHGRTVHSKVNGLKIFKnVKVDLIAPEELAMPEHYVEKMKKNGFEVRIFSSIEEYLSQKDVA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 2149 ---YMTRIQKERFSS---EKEY----NACFGQFILtPHIMTGAKrkmvVMHPLPRVN---EISVEVDTDPRAAYFRQAEN 2215
Cdd:PRK13376 246 kiwYFTRLQLERMGEdilEKEHilrkAVTFRKEFL-DKLPEGVK----FYHPLPRHKvypTIPTFLDTLPLNGWETQAIN 320
|
330
....*....|....
gi 822092823 2216 GMYIRMALLATVLG 2229
Cdd:PRK13376 321 GYWVRIVLLSMLGG 334
|
|
| PLN02342 |
PLN02342 |
ornithine carbamoyltransferase |
1898-2229 |
3.58e-37 |
|
ornithine carbamoyltransferase
Pssm-ID: 177976 [Multi-domain] Cd Length: 348 Bit Score: 144.55 E-value: 3.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1898 PPPLARILSPQAGQP-QILPHPQTSPLLHPLVG----QHILSVRQFSKEQMSHLFNVAHTLRLMVQK-ERPLDILKGKVM 1971
Cdd:PLN02342 9 RSPSAVSSSSRARRGlVVCAASSSAAAPSPIKGkskpKHFLHIDDFDKEEILGLLDRAKEVKALLKSgDRSFQPFKGKSM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1972 ASMFYEVSTRTSSSFAAAMHRLGGSVVHFCESTSSTQKGESLVDSVNTMSCYADVIVLRHPIPGAVESAARHCRRPVINA 2051
Cdd:PLN02342 89 AMIFTKPSMRTRVSFETGFFLLGGHALYLGPDDIQLGKREETRDIARVLSRYNDIIMARVFAHQDVLDLAEYSSVPVING 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 2052 GDGVgEHPTQALLDIFTIREELGTVNGMTITMVGDlkHGRTVHSLARLLTQYRITLRYVAPKNLSMPAEIIDFVASKGI- 2130
Cdd:PLN02342 169 LTDY-NHPCQIMADALTIIEHIGRLEGTKVVYVGD--GNNIVHSWLLLAAVLPFHFVCACPKGYEPDAKTVEKARAAGIs 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 2131 KQEEFNSIEEALPDTDVLY------MTriQKERFSSEKEynaCFGQFILTPHIMTGAKRKMVVMHPLP--RVNEISVEVD 2202
Cdd:PLN02342 246 KIEITNDPAEAVKGADVVYtdvwasMG--QKEEAEKRKK---AFQGFQVNEALMKLAGPQAYFMHCLPaeRGVEVTDGVM 320
|
330 340
....*....|....*....|....*..
gi 822092823 2203 TDPRAAYFRQAENGMYIRMALLATVLG 2229
Cdd:PLN02342 321 EAPNSIVFPQAENRMHAQNAIMLHQLG 347
|
|
| CPSase_L_D3 |
pfam02787 |
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate ... |
803-883 |
2.77e-36 |
|
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain.
Pssm-ID: 460695 Cd Length: 79 Bit Score: 132.50 E-value: 2.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 803 EELQTPTDKRIFVLAAALHAGYTVERLYELTKIDHWFLHKMKNIADHKKLLETYKqdeSAMPPEIMRKAKQLGFSDKQIA 882
Cdd:pfam02787 1 EELRTPTDERLFAIAEALRRGYSVEEIHELTKIDPWFLDKIKNIVELEKELKEAG---LDLDAELLREAKRLGFSDRQIA 77
|
.
gi 822092823 883 Q 883
Cdd:pfam02787 78 K 78
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
1465-1792 |
4.87e-33 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 134.34 E-value: 4.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1465 QKLIRLPGLIDVHVHLREPGATHKEDFSSGTAAALAGGITMVCAMPNTNPAIIDPNSFTMAQKLAKAGC--RCDY--ALF 1540
Cdd:PRK07369 51 SGLILGPGLVDLYSHSGEPGFEERETLASLAAAAAAGGFTRVAILPDTFPPLDNPATLARLQQQAQQIPpvQLHFwgALT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1541 VGASSDNAALLPSIASSTA-G------------LKMYLndTYSTLKMDNVSLWMEHFE----------KWPKHL---PIV 1594
Cdd:PRK07369 131 LGGQGKQLTELAELAAAGVvGftdgqplenlalLRRLL--EYLKPLGKPVALWPCDRSlagngvmregLLALRLglpGDP 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1595 AHAEKQTVAAILLVAQLYQRPVHICHVAKKEEILIIRAAKQKGIQVTCEVAPHHLFLcedNVPVIGKDKAQVR--PMLGT 1672
Cdd:PRK07369 209 ASAETTALAALLELVAAIGTPVHLMRISTARSVELIAQAKARGLPITASTTWMHLLL---DTEALASYDPNLRldPPLGN 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1673 REDMEALWENLD--IIDCFATDHAPHSAEEKI---SEKpPPGYPGLETMLPLLF-TAVSEGRLTVDDIIKRLYENPRKIF 1746
Cdd:PRK07369 286 PSDRQALIEGVRtgVIDAIAIDHAPYTYEEKTvafAEA-PPGAIGLELALPLLWqNLVETGELSALQLWQALSTNPARCL 364
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 822092823 1747 SL------PAQEDTYVEVDLEQEWIIPKHMQFTKSKWTPFEGMKVKGKVMRV 1792
Cdd:PRK07369 365 GQeppslaPGQPAELILFDPQKTWTVSAQTLHSLSRNTPWLGQTLKGRVLQT 416
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
1441-1800 |
3.05e-32 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 132.11 E-value: 3.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1441 LFVQALK--QIGQAP---RVKTHVDSmtsQKLIRLPGLIDVHVHLREPGATHKEDFSSGTAAALAGGITMVCAMPNTNPA 1515
Cdd:PRK07627 23 LYVAAGKiaAIGQAPagfNADKTIDA---SGLIVCPGLVDLSARLREPGYEYKATLESEMAAAVAGGVTSLVCPPDTDPV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1516 IIDPNSFTM----AQK--------------------------LAKAGCrcdyalfVGASS------DNAALLPSIA-SST 1558
Cdd:PRK07627 100 LDEPGLVEMlkfrARNlnqahvyplgaltvglkgevltemveLTEAGC-------VGFSQanvpvvDTQVLLRALQyAST 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1559 AGLKMYLNDTYSTLKMDNVSlwmeHFEKWPKHL---PIVAHAEKQTVAAILLVAQLYQRPVHICHVAKKEEILIIRAAKQ 1635
Cdd:PRK07627 173 FGFTVWLRPLDAFLGRGGVA----ASGAVASRLglsGVPVAAETIALHTIFELMRVTGARVHLARLSSAAGVALVRAAKA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1636 KGIQVTCEVAPHHLFLCEDNvpvIGKDKAQVR--PMLGTREDMEALWENL--DIIDCFATDHAPHSAEEKI---SEKpPP 1708
Cdd:PRK07627 249 EGLPVTCDVGVNHVHLIDVD---IGYFDSQFRldPPLRSQRDREAIRAALadGTIDAICSDHTPVDDDEKLlpfAEA-TP 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1709 GYPGLETMLPLLFTAVSEGRLTVDDIIKRLYENPRKIFSLPAQE-------DTYVeVDLEQEWIIPKHMQFTKSKWTPFE 1781
Cdd:PRK07627 325 GATGLELLLPLTLKWADEAKVPLARALARITSAPARVLGLPAGRlaegapaDLCV-FDPDAHWRVEPRALKSQGKNTPFL 403
|
410
....*....|....*....
gi 822092823 1782 GMKVKGKVMRVVLRGEVAY 1800
Cdd:PRK07627 404 GYELPGRVRATLVAGQVAF 422
|
|
| PLN02795 |
PLN02795 |
allantoinase |
1470-1803 |
3.28e-32 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 133.75 E-value: 3.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1470 LPGLIDVHVHLREPGATHKEDFSSGTAAALAGGITMVCAMP-NTNPAIIDPNSFTMAQKLAKAGCRCDYALFVGASSDNA 1548
Cdd:PLN02795 98 MPGLIDVHVHLNEPGRTEWEGFPTGTKAAAAGGITTLVDMPlNSFPSTTSVETLELKIEAAKGKLYVDVGFWGGLVPENA 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1549 A---LLPSIASSTA-GLKMYL-----NDTYSTLKmdnvslwmEHFEKWPKHL-----PIVAHAEKQTVAAI--------- 1605
Cdd:PLN02795 178 HnasVLEELLDAGAlGLKSFMcpsgiNDFPMTTA--------THIKAALPVLakygrPLLVHAEVVSPVESdsrldadpr 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1606 LLVAQLYQRP----------------------------VHICHVAKKEEIL-IIRAAKQKGIQVTCEVAPHHL-FLCEDn 1655
Cdd:PLN02795 250 SYSTYLKSRPpsweqeairqllevakdtrpggvaegahVHIVHLSDAESSLeLIKEAKAKGDSVTVETCPHYLaFSAEE- 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1656 VPViGKDKAQVRPMLGTREDMEALWENL--DIIDCFATDHAPHSAEEKISE-----KPPPGYPGLETMLPLLFTAVSEGR 1728
Cdd:PLN02795 329 IPD-GDTRYKCAPPIRDAANRELLWKALldGDIDMLSSDHSPSPPDLKLLEegnflRAWGGISSLQFVLPATWTAGRAYG 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1729 LTVDDIIKRLYENPRKIFSLPA--------QEDTYV-----EVDLEQEWIIpkhmQFTKSKWTPFEGMKVKGKVMRVVLR 1795
Cdd:PLN02795 408 LTLEQLARWWSERPAKLAGLDSkgaiapgkDADIVVwdpeaEFVLDESYPI----YHKHKSLSPYLGTKLSGKVIATFVR 483
|
....*...
gi 822092823 1796 GEVAYIDG 1803
Cdd:PLN02795 484 GNLVFLEG 491
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
1462-1800 |
9.31e-31 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 128.05 E-value: 9.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1462 MTSQKLIRLPGLIDVHVHLREPGATHKEDFSSGTAAALAGGITMVCAMP-NTNPAIIDPNSFTMAQKLAKAGCRCDYALF 1540
Cdd:PRK08044 44 MDASGLVVSPGMVDAHTHISEPGRSHWEGYETGTRAAAKGGITTMIEMPlNQLPATVDRASIELKFDAAKGKLTIDAAQL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1541 VGASSDNAALLPSIAS-STAGLKMYLN--------------DTYSTLK---------------MDNVSLWMEHFEKWPKH 1590
Cdd:PRK08044 124 GGLVSYNLDRLHELDEvGVVGFKCFVAtcgdrgidndfrdvNDWQFYKgaqklgelgqpvlvhCENALICDELGEEAKRE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1591 LPIVAHA---------EKQTVAAILLVAQLYQRPVHICHVAKKEEILIIRAAKQKGIQVTCEVAPHHLFLCEDNVPVIGK 1661
Cdd:PRK08044 204 GRVTAHDyvasrpvftEVEAIRRVLYLAKVAGCRLHVCHISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGT 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1662 dKAQVRPMLGTREDMEALWENL--DIIDCFATDHAPHSAEEKISE--KPPPGYPGLETMLPLLF-TAVSEGRLTVDDIIK 1736
Cdd:PRK08044 284 -LAKCSPPIRDLENQKGMWEKLfnGEIDCLVSDHSPCPPEMKAGNimEAWGGIAGLQNCMDVMFdEAVQKRGMSLPMFGK 362
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 822092823 1737 RLYENPRKIFSL-------PAQEDTYVEVDLEQEWIIPKHMQFTKSKWTPFEGMKVKGKVMRVVLRGEVAY 1800
Cdd:PRK08044 363 LMATNAADIFGLqqkgriaPGKDADFVFIQPNSSYVLKNEDLEYRHKVSPYVGRTIGARITKTILRGDVIY 433
|
|
| PRK09059 |
PRK09059 |
dihydroorotase; Validated |
1465-1800 |
1.49e-27 |
|
dihydroorotase; Validated
Pssm-ID: 181631 [Multi-domain] Cd Length: 429 Bit Score: 118.21 E-value: 1.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1465 QKLIRLPGLIDVHVHLREPGATHKEDFSSGTAAALAGGITMVCAMPNTNPAIIDPNSFTMAQKLAKagcrcDYAL----- 1539
Cdd:PRK09059 54 AGKAVAPGLVDARVFVGEPGAEHRETIASASRAAAAGGVTSIIMMPDTDPVIDDVALVEFVKRTAR-----DTAIvnihp 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1540 -------FVGASSDNAALLpsiasSTAGLKMYLNDTYS---TLKMDNVSLWMEHFEkwpkhLPIVAHAEKQTVAA----- 1604
Cdd:PRK09059 129 aaaitkgLAGEEMTEFGLL-----RAAGAVAFTDGRRSvanTQVMRRALTYARDFD-----AVIVHETRDPDLGGngvmn 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1605 -------------------ILL-----VAQLYQRPVHICHVAKKEEILIIRAAKQKGIQVTCEVAPHHLFLCEDNvpvIG 1660
Cdd:PRK09059 199 eglfaswlglsgipreaevIPLerdlrLAALTRGRYHAAQISCAESAEALRRAKDRGLKVTAGVSINHLSLNEND---IG 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1661 KDKAQVR--PMLGTREDMEALWENLD--IIDCFATDHAPHSAEEK---ISEKPPpGYPGLETMLPLLFTAVSEGRLTVDD 1733
Cdd:PRK09059 276 EYRTFFKlsPPLRTEDDRVAMVEAVAsgTIDIIVSSHDPQDVDTKrlpFSEAAA-GAIGLETLLAAALRLYHNGEVPLLR 354
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 822092823 1734 IIKRLYENPRKIFSLP-------AQEDTYVeVDLEQEWIIPKHMQFTKSKWTPFEGMKVKGKVMRVVLRGEVAY 1800
Cdd:PRK09059 355 LIEALSTRPAEIFGLPagtlkpgAPADIIV-IDLDEPWVVDPEDLKSRSKNTPFEEARFQGRVVRTIVAGKTVY 427
|
|
| PRK14805 |
PRK14805 |
ornithine carbamoyltransferase; Provisional |
1930-2229 |
2.43e-27 |
|
ornithine carbamoyltransferase; Provisional
Pssm-ID: 237819 [Multi-domain] Cd Length: 302 Bit Score: 114.40 E-value: 2.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1930 QHILSVRQFSKEQMSHLFNVAHTLrlmvqKERPLD---ILKGKVMASMFYEVSTRTSSSFAAAMHRLGGSVVHFCESTSS 2006
Cdd:PRK14805 2 KHLLSIKELTQQQLLDLLALAKTI-----KANPAEyrqALAGKSVVMLFEKPSLRTRVSFDIGINKLGGHCLYLDQQNGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 2007 TQKGESLVDSVNTMSCYADVIVLRHPIPGAVESAARHCRRPVINAGDGVgEHPTQALLDIFTIREELGTVNGMTITMVGD 2086
Cdd:PRK14805 77 LGKRESVADFAANLSCWADAIVARVFSHSTIEQLAEHGSVPVINALCDL-YHPCQALADFLTLAEQFGDVSKVKLAYVGD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 2087 lkhGRTV-HSLARLLTQYRITLRYVAPKNLSMPAEII----DFVASKGIKQEEFNSIeEALPDTDVLYM-TRIQKERFSS 2160
Cdd:PRK14805 156 ---GNNVtHSLMYGAAILGATMTVICPPGHFPDGQIVaeaqELAAKSGGKLVLTSDI-EAIEGHDAIYTdTWISMGDDTP 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 822092823 2161 EKEYNACFGQFILTPHIM--TGAKRkmvVMHPLP--RVNEISVEVDTDPRAAYFRQAENGMYIRMALLATVLG 2229
Cdd:PRK14805 232 LAEIKAKFAPYQVNKALMekAGATF---VMHCQPahRGVEITSEVMDGEGSLILQQAENRMHAQNAVLVTLLS 301
|
|
| PRK02102 |
PRK02102 |
ornithine carbamoyltransferase; Validated |
1927-2229 |
1.21e-25 |
|
ornithine carbamoyltransferase; Validated
Pssm-ID: 179366 [Multi-domain] Cd Length: 331 Bit Score: 110.36 E-value: 1.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1927 LVGQHILSVRQFSKEQMSHLFNVAHTLRLMVQKERPLDILKGKVMASMFYEVSTRTSSSFAAAMHRLGGSVVHFCESTSS 2006
Cdd:PRK02102 5 LKGRSFLKLLDFTPEEIEYLIDLSIELKAAKKAGIEHQYLEGKNIALIFEKTSTRTRCAFEVAAIDLGAHVTYLGPNDSQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 2007 TQKGESLVDSVNTMSCYADVIVLR---HPIpgaVESAARHCRRPVINAGDGVgEHPTQALLDIFTIREELGTVNGMTITM 2083
Cdd:PRK02102 85 LGKKESIEDTARVLGRMYDGIEYRgfkQEI---VEELAKYSGVPVWNGLTDE-WHPTQMLADFMTMKEHFGPLKGLKLAY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 2084 VGDlkhGR--TVHSL----ARLLTQYRItlryVAPKNLSMPAEIIDfvASKGIKQEEFNSI------EEALPDTDVLYmT 2151
Cdd:PRK02102 161 VGD---GRnnMANSLmvggAKLGMDVRI----CAPKELWPEEELVA--LAREIAKETGAKItitedpEEAVKGADVIY-T 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 2152 RI---------QKERFSsekeynacfgqfILTPH------IMTGAKRKMVVMHPLP-----------------RVNEISV 2199
Cdd:PRK02102 231 DVwvsmgeedeWEERIK------------LLKPYqvnmdlMKATGNPDVIFMHCLPafhdtetkvgkeiaekyGLKGLEV 298
|
330 340 350
....*....|....*....|....*....|..
gi 822092823 2200 --EVDTDPRAAYFRQAENGMYIRMALLATVLG 2229
Cdd:PRK02102 299 tdEVFESKYSIVFDEAENRMHTIKAVMVATLG 330
|
|
| GATase1_Anthranilate_Synthase |
cd01743 |
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ... |
191-342 |
1.84e-24 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase (ASase). This group contains proteins similar to para-aminobenzoate (PABA) synthase and ASase. These enzymes catalyze similar reactions and produce similar products, PABA and ortho-aminobenzoate (anthranilate). Each enzyme is composed of non-identical subunits: a glutamine amidotransferase subunit (component II) and a subunit that produces an aminobenzoate products (component I). ASase catalyses the synthesis of anthranilate from chorismate and glutamine and is a tetrameric protein comprising two copies each of components I and II. Component II of ASase belongs to the family of triad GTases which hydrolyze glutamine and transfer nascent ammonia between the active sites. In some bacteria, such as Escherichia coli, component II can be much larger than in other organisms, due to the presence of phosphoribosyl-anthranilate transferase (PRTase) activity. PRTase catalyses the second step in tryptophan biosynthesis and results in the addition of 5-phosphoribosyl-1-pyrophosphate to anthranilate to create N-5'-phosphoribosyl-anthranilate. In E.coli, the first step in the conversion of chorismate to PABA involves two proteins: PabA and PabB which co-operate to transfer the amide nitrogen of glutamine to chorismate forming 4-amino-4 deoxychorismate (ADC). PabA acts as a glutamine amidotransferase, supplying an amino group to PabB, which carries out the amination reaction. A third protein PabC then mediates elimination of pyruvate and aromatization to give PABA. Several organisms have bipartite proteins containing fused domains homologous to PabA and PabB commonly called PABA synthases. These hybrid PABA synthases may produce ADC and not PABA.
Pssm-ID: 153214 [Multi-domain] Cd Length: 184 Bit Score: 102.61 E-value: 1.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 191 YNQIRCLCQRGARVTVVPWDQPLDSN----DFDGLFISNGPGNPEYCKETVENIRKVAcveNPKPIFGICLGHQLLSLVI 266
Cdd:cd01743 12 YNLVQYLRELGAEVVVVRNDEITLEElellNPDAIVISPGPGHPEDAGISLEIIRALA---GKVPILGVCLGHQAIAEAF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 267 GAKTYKMKYGNRG------HNQPCIHKGTSR-----CYitsqnHGFAVDPETLPKDWDVLftnanDQTSEGIV----HNH 331
Cdd:cd01743 89 GGKVVRAPEPMHGktseihHDGSGLFKGLPQpftvgRY-----HSLVVDPDPLPDLLEVT-----ASTEDGVImalrHRD 158
|
170
....*....|.
gi 822092823 332 KPLFSVQFHPE 342
Cdd:cd01743 159 LPIYGVQFHPE 169
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
1074-1250 |
3.16e-22 |
|
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.
Pssm-ID: 397079 [Multi-domain] Cd Length: 209 Bit Score: 96.99 E-value: 3.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1074 SDTESAVNFCETVGYPCLVRPSYVLSGAAMNVAYSDTDMEKFLSSAVAVSKE----HPVVISKFIQEAKEIDVDAVAcDG 1149
Cdd:pfam02786 25 ETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAafgnPQVLVEKSLKGPKHIEYQVLR-DA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1150 EVIAIAVSEhVENA-GVHSGDATLVTPPQDINQKTMERIKMIVHAIGQELQVTGPFNLQLI--AKDDQLKVIECNVRVSR 1226
Cdd:pfam02786 104 HGNCITVCN-RECSdQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVEFAldPFSGEYYFIEMNTRLQV 182
|
170 180
....*....|....*....|....
gi 822092823 1227 SFPYVSKTLGVDLVALATRVILGE 1250
Cdd:pfam02786 183 EHALAEKATGYDLAKEAAKIALGY 206
|
|
| MGS |
pfam02142 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
1332-1434 |
4.93e-22 |
|
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the domain is also found in Carbamoyl phosphate synthetase (CPS) where it forms a regulatory domain that binds to the allosteric effector ornithine. This family also includes inosicase. The known structures in this family show a common phosphate binding site.
Pssm-ID: 460462 [Multi-domain] Cd Length: 93 Bit Score: 92.17 E-value: 4.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1332 ELLPTVQTLESLGYNLYASLGTADFYTEHGVKVMAVDWPFEEesDCPNKDKQrnIMDYLEENHFDLVINLSMRNSGGRRl 1411
Cdd:pfam02142 1 GLVELAKALVELGFELLATGGTAKFLREAGIPVTEVVEKTGE--GRPGGRVQ--IGDLIKNGEIDLVINTLYPFKATVH- 75
|
90 100
....*....|....*....|...
gi 822092823 1412 ssfvtKGYRTRRMAIDFSVPLIT 1434
Cdd:pfam02142 76 -----DGYAIRRAAENIDIPGPT 93
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
1034-1252 |
4.00e-21 |
|
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440208 [Multi-domain] Cd Length: 263 Bit Score: 95.32 E-value: 4.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1034 RQQCRILGTSPEFIDNAENRFKFSRMLDTIGISQPRWKELSDTESAVNFCETVGYPCLVRPSYVLSGAAMNVAYSDTDME 1113
Cdd:COG0439 36 AEELGLPGPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1114 KFLSSAVA----VSKEHPVVISKFIqEAKEIDVDAVACDGEVIAIAVSEHvENAGVHSGDATLVTPPqDINQKTMERIKM 1189
Cdd:COG0439 116 AALAEARAeakaGSPNGEVLVEEFL-EGREYSVEGLVRDGEVVVCSITRK-HQKPPYFVELGHEAPS-PLPEELRAEIGE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 822092823 1190 IVHAIGQELQV-TGPFNLQ-LIAKDDQLKVIECNVRVS--RSFPYVSKTLGVDLVALATRVILGEEV 1252
Cdd:COG0439 193 LVARALRALGYrRGAFHTEfLLTPDGEPYLIEINARLGgeHIPPLTELATGVDLVREQIRLALGEPR 259
|
|
| PabA |
COG0512 |
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ... |
191-342 |
1.40e-19 |
|
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 440278 [Multi-domain] Cd Length: 189 Bit Score: 88.56 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 191 YNQIRCLCQRGARVTVVPWDQP----LDSNDFDGLFISNGPGNPEYCKETVENIRKVAcveNPKPIFGICLGHQLLSLVI 266
Cdd:COG0512 12 YNLVQYLGELGAEVVVVRNDEItleeIEALAPDGIVLSPGPGTPEEAGISLEVIRAFA---GKIPILGVCLGHQAIGEAF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 267 GAKTYKMKygnrghnQPcIHKGTSRCYITSQN--------------HGFAVDPETLPkdwDVLFTNAndQTSEGIV---- 328
Cdd:COG0512 89 GGKVVRAP-------EP-MHGKTSPITHDGSGlfaglpnpftatryHSLVVDRETLP---DELEVTA--WTEDGEImgir 155
|
170
....*....|....
gi 822092823 329 HNHKPLFSVQFHPE 342
Cdd:COG0512 156 HRELPIEGVQFHPE 169
|
|
| PRK04284 |
PRK04284 |
ornithine carbamoyltransferase; Provisional |
1927-2230 |
5.36e-19 |
|
ornithine carbamoyltransferase; Provisional
Pssm-ID: 235269 [Multi-domain] Cd Length: 332 Bit Score: 90.57 E-value: 5.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1927 LVGQHILSVRQFSKEQMSHLFNVAHTLRLMVQKERPLDILKGKVMASMFYEVSTRTSSSFAAAMHRLGGSVVHFCESTSS 2006
Cdd:PRK04284 4 LRNRSFLTLLDFTPKEIEYLLDLSEDLKRAKYAGIEVQKLKGKNIALIFEKDSTRTRCAFEVAAYDQGAHVTYLGPTGSQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 2007 TQKGESLVDSVNTMSCYADVIVLRHPIPGAVESAARHCRRPVINaGDGVGEHPTQALLDIFTIREEL-GTVNGMTITMVG 2085
Cdd:PRK04284 84 MGKKESTKDTARVLGGMYDGIEYRGFSQRTVETLAEYSGVPVWN-GLTDEDHPTQVLADFLTAKEHLkKPYKDIKFTYVG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 2086 DlkhGR--TVHSLARLLTQYRITLRYVAPKNLSMPAEIID----FVASKGIKQEEFNSIEEALPDTDVLYM--------- 2150
Cdd:PRK04284 163 D---GRnnVANALMQGAAIMGMDFHLVCPKELNPDDELLNkckeIAAETGGKITITDDIDEGVKGSDVIYTdvwvsmgep 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 2151 TRIQKERFSSEKEYNacfgqfiLTPHIMTGAKRKMVV-MHPLPRVN-------------------EISVEVDTDPRAAYF 2210
Cdd:PRK04284 240 DEVWEERIKLLKPYQ-------VNKEMMKKTGNPNAIfEHCLPSFHdldtkvgkeifekyglkemEVTDEVFESKASVVF 312
|
330 340
....*....|....*....|
gi 822092823 2211 RQAENGMYIRMALLATVLGR 2230
Cdd:PRK04284 313 DEAENRMHTIKAVMVATLGE 332
|
|
| trpG_papA |
TIGR00566 |
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This ... |
191-342 |
9.90e-19 |
|
glutamine amidotransferase of anthranilate synthase or aminodeoxychorismate synthase; This model describes the glutamine amidotransferase domain or peptide of the tryptophan-biosynthetic pathway enzyme anthranilate synthase or of the folate biosynthetic pathway enzyme para-aminobenzoate synthase. In at least one case, a single polypeptide from Bacillus subtilis was shown to have both functions. This model covers a subset of the sequences described by the Pfam model GATase.
Pssm-ID: 273144 [Multi-domain] Cd Length: 188 Bit Score: 86.38 E-value: 9.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 191 YNQIRCLCQRGARVtVVPWDQPLDSNDFDGLF-----ISNGPGNPEYCKETVENIRKVAcveNPKPIFGICLGHQLLSLV 265
Cdd:TIGR00566 13 YNLVQYFCELGAEV-VVKRNDSLTLQEIEALLpllivISPGPCTPNEAGISLEAIRHFA---GKLPILGVCLGHQAMGQA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 266 IGAKT---YKMKYG---NRGHNQPCIHKGTSRCYITSQNHGFAVDPETLPKDWDVLFTNANDQTSEGIVHNHKPLFSVQF 339
Cdd:TIGR00566 89 FGGDVvraNTVMHGktsEIEHNGAGIFRGLFNPLTATRYHSLVVEPETLPTCFPVTAWEEENIEIMAIRHRDLPLEGVQF 168
|
...
gi 822092823 340 HPE 342
Cdd:TIGR00566 169 HPE 171
|
|
| PRK05670 |
PRK05670 |
anthranilate synthase component II; Provisional |
191-342 |
1.05e-17 |
|
anthranilate synthase component II; Provisional
Pssm-ID: 235552 [Multi-domain] Cd Length: 189 Bit Score: 83.26 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 191 YN---QIRCLcqrGARVTVVPWDQP----LDSNDFDGLFISNGPGNPEYCKETVENIRKVAcveNPKPIFGICLGHQLLS 263
Cdd:PRK05670 13 YNlvqYLGEL---GAEVVVYRNDEItleeIEALNPDAIVLSPGPGTPAEAGISLELIREFA---GKVPILGVCLGHQAIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 264 LVIGA-----------KTYKMKygnrgHNQPCIHKGTSRCYITSQNHGFAVDPETLPKDWDVLFTnANDQTSEGIVHNHK 332
Cdd:PRK05670 87 EAFGGkvvrakeimhgKTSPIE-----HDGSGIFAGLPNPFTVTRYHSLVVDRESLPDCLEVTAW-TDDGEIMGVRHKEL 160
|
170
....*....|
gi 822092823 333 PLFSVQFHPE 342
Cdd:PRK05670 161 PIYGVQFHPE 170
|
|
| PRK07765 |
PRK07765 |
aminodeoxychorismate/anthranilate synthase component II; |
191-342 |
4.35e-17 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181107 [Multi-domain] Cd Length: 214 Bit Score: 82.40 E-value: 4.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 191 YNQIRCLCQRGARVTVVPWDQP------LDSNDFDGLFISNGPGNPEYCKETVENIRkvACVENPKPIFGICLGHQLLSL 264
Cdd:PRK07765 14 FNLVQYLGQLGVEAEVWRNDDPrladeaAVAAQFDGVLLSPGPGTPERAGASIDMVR--ACAAAGTPLLGVCLGHQAIGV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 265 VIGA-----------KTYKMKYGNRGhnqpcIHKGTSRCYITSQNHGFAVDPETLPKDWDVLftnanDQTSEGIV----H 329
Cdd:PRK07765 92 AFGAtvdrapellhgKTSSVHHTGVG-----VLAGLPDPFTATRYHSLTILPETLPAELEVT-----ARTDSGVImavrH 161
|
170
....*....|...
gi 822092823 330 NHKPLFSVQFHPE 342
Cdd:PRK07765 162 RELPIHGVQFHPE 174
|
|
| GuaA1 |
COG0518 |
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ... |
181-342 |
6.52e-17 |
|
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP synthase, glutamine amidotransferase domain is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 440284 [Multi-domain] Cd Length: 225 Bit Score: 81.92 E-value: 6.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 181 RITAIDCGI---KYNQI--RCLCQRGARVTVV--------PWDQPLDsnDFDGLFISNGPGNP----EYCKETVENIRKV 243
Cdd:COG0518 1 KILILDHDPfggQYPGLiaRRLREAGIELDVLrvyageilPYDPDLE--DPDGLILSGGPMSVydedPWLEDEPALIREA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 244 acVENPKPIFGICLGHQLLSLVIGAKTYKMKYGNRG------HNQPCIHKGTSRCYITSQNHGFAVDpeTLPKDWDVLFT 317
Cdd:COG0518 79 --FELGKPVLGICYGAQLLAHALGGKVEPGPGREIGwapvelTEADPLFAGLPDEFTVWMSHGDTVT--ELPEGAEVLAS 154
|
170 180
....*....|....*....|....*
gi 822092823 318 NANDQTsEGIVHNhKPLFSVQFHPE 342
Cdd:COG0518 155 SDNCPN-QAFRYG-RRVYGVQFHPE 177
|
|
| MGS |
smart00851 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
1332-1434 |
5.08e-16 |
|
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the domain is also found in Carbamoyl phosphate synthetase (CPS) where it forms a regulatory domain that binds to the allosteric effector ornithine. This family also includes inosicase. The known structures in this family show a common phosphate binding site.
Pssm-ID: 214855 [Multi-domain] Cd Length: 91 Bit Score: 75.20 E-value: 5.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1332 ELLPTVQTLESLGYNLYASLGTADFYTEHGVKVMA--VDWPFEEesdcpnkdkQRNIMDYLEENHFDLVINLSMRNSggr 1409
Cdd:smart00851 1 GLVEFAKRLAELGFELLATGGTAKFLREAGLPVVKtlHPKVHGG---------IPQILDLIKNGEIDLVINTLYPFE--- 68
|
90 100
....*....|....*....|....*
gi 822092823 1410 rlSSFVTKGYRTRRMAIDFSVPLIT 1434
Cdd:smart00851 69 --AQAHEDGYSIRRAAENIDIPGPT 91
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
1473-1745 |
5.15e-16 |
|
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The family includes urease alpha, adenosine deaminase, phosphotriesterase dihydroorotases, allantoinases, hydantoinases, AMP-, adenine and cytosine deaminases, imidazolonepropionase, aryldialkylphosphatase, chlorohydrolases, formylmethanofuran dehydrogenases and others.
Pssm-ID: 238617 [Multi-domain] Cd Length: 275 Bit Score: 80.46 E-value: 5.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1473 LIDVHVHLREPGATH------------------KEDFSSGTAAALAGGITMVCAMPNTNPAIIDPNSFTMAQKLAKAGCR 1534
Cdd:cd01292 1 FIDTHVHLDGSALRGtrlnlelkeaeelspedlYEDTLRALEALLAGGVTTVVDMGSTPPPTTTKAAIEAVAEAARASAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1535 CDYALFVGASSDNA------------ALLPSIASSTAGLKMYLNDTYSTLKMDNVslwMEHFEKWPKH-LPIVAHAEKQT 1601
Cdd:cd01292 81 IRVVLGLGIPGVPAavdedaeallleLLRRGLELGAVGLKLAGPYTATGLSDESL---RRVLEEARKLgLPVVIHAGELP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1602 VA--AILLVAQLYQRP--VHICHVA---KKEEILIIRAakqkgiQVTCEVAPHHLFLcednvpvigkdkaqvrpMLGTRE 1674
Cdd:cd01292 158 DPtrALEDLVALLRLGgrVVIGHVShldPELLELLKEA------GVSLEVCPLSNYL-----------------LGRDGE 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 822092823 1675 DMEALWENLD--IIDCFATDHAPHsaeekisekpppgypGLETMLPLLFTAVSE---GRLTVDDIIKRLYENPRKI 1745
Cdd:cd01292 215 GAEALRRLLElgIRVTLGTDGPPH---------------PLGTDLLALLRLLLKvlrLGLSLEEALRLATINPARA 275
|
|
| GATase1_1 |
cd01741 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
194-344 |
1.09e-15 |
|
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.
Pssm-ID: 153212 [Multi-domain] Cd Length: 188 Bit Score: 77.29 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 194 IRCLCQRGARVTVVPW---DQPLDSNDFDGLFISNGPGNPEYC-----KETVENIRKvaCVENPKPIFGICLGHQLLSLV 265
Cdd:cd01741 20 LREAGAETIEIDVVDVyagELLPDLDDYDGLVILGGPMSVDEDdypwlKKLKELIRQ--ALAAGKPVLGICLGHQLLARA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 266 IGAKTYKMKYGnrghnqPCIhkGTSRCYITSQNH---GFAVDPET-------------LPKDWDVLFTNANDqtsegivH 329
Cdd:cd01741 98 LGGKVGRNPKG------WEI--GWFPVTLTEAGKadpLFAGLPDEfpvfhwhgdtvveLPPGAVLLASSEAC-------P 162
|
170 180
....*....|....*....|
gi 822092823 330 NH-----KPLFSVQFHPEHM 344
Cdd:cd01741 163 NQafrygDRALGLQFHPEER 182
|
|
| PRK03515 |
PRK03515 |
ornithine carbamoyltransferase subunit I; Provisional |
1924-2228 |
1.61e-15 |
|
ornithine carbamoyltransferase subunit I; Provisional
Pssm-ID: 179587 [Multi-domain] Cd Length: 336 Bit Score: 80.14 E-value: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1924 LHPLVGQHILSVRQFSKEQMSHLFNVAHTLRLMVQKERPLDILKGKVMASMFYEVSTRTSSSFAAAMHRLGGSVVhfCES 2003
Cdd:PRK03515 1 MNQFYQRHFLRLLDFTPAELNSLLQLAAKLKADKKNGKEEQKLTGKNIALIFEKDSTRTRCSFEVAAYDQGARVT--YLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 2004 TSSTQKG--ESLVDSVNTMSCYADVIVLRHPIPGAVESAARHCRRPVINagdGVGE--HPTQALLDIFTIREEL--GTVN 2077
Cdd:PRK03515 79 PSGSQIGhkESIKDTARVLGRMYDGIQYRGYGQEIVETLAEYAGVPVWN---GLTNefHPTQLLADLLTMQEHLpgKAFN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 2078 GMTITMVGDLKH--GRTVHSLARLLTqyrITLRYVAPK----NLSMPAEIIDFVASKGIKQEEFNSIEEALPDTDVLYM- 2150
Cdd:PRK03515 156 EMTLAYAGDARNnmGNSLLEAAALTG---LDLRLVAPKacwpEAALVTECRALAQKNGGNITLTEDIAEGVKGADFIYTd 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 2151 --------TRIQKERFSSEKEYNACFGQFILT--PHI------------MTGAKRKMVVMHPLPRVNEISVEVDTDPRAA 2208
Cdd:PRK03515 233 vwvsmgepKEVWAERIALLRPYQVNSKMMQLTgnPQVkflhclpafhddQTTLGKKMAEEYGLHGGMEVTDEVFESAHSI 312
|
330 340
....*....|....*....|.
gi 822092823 2209 YFRQAENGMY-IRMALLATVL 2228
Cdd:PRK03515 313 VFDQAENRLHtIKAVMVATLS 333
|
|
| guaA_Nterm |
TIGR00888 |
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ... |
182-342 |
1.83e-15 |
|
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine de novo biosynthesis is well-conserved. However, it appears to split into two separate polypeptide chains in most of the Archaea. This N-terminal region would be the smaller subunit. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 129966 [Multi-domain] Cd Length: 188 Bit Score: 76.58 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 182 ITAIDCGIKYNQI--RCLCQRGARVTVVPWDQPLD---SNDFDGLFISNGPgNPEYCKETVENIRKVacVENPKPIFGIC 256
Cdd:TIGR00888 1 ILVLDFGSQYTQLiaRRLRELGVYSELVPNTTPLEeirEKNPKGIILSGGP-SSVYAENAPRADEKI--FELGVPVLGIC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 257 LGHQLLSLVIGAKTYKMKYGNRGH------NQPCIHKGTSRCYITSQNHGFAVdpETLPKDWDVLFTNANDQTsEGIVHN 330
Cdd:TIGR00888 78 YGMQLMAKQLGGEVGRAEKREYGKaeleilDEDDLFRGLPDESTVWMSHGDKV--KELPEGFKVLATSDNCPV-AAMAHE 154
|
170
....*....|..
gi 822092823 331 HKPLFSVQFHPE 342
Cdd:TIGR00888 155 EKPIYGVQFHPE 166
|
|
| MGS_CPS_II |
cd01424 |
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate ... |
1319-1436 |
2.16e-15 |
|
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate synthetase (CSP). CSP, a CarA and CarB heterodimer, catalyzes the production of carbamoyl phosphate which is subsequently employed in the metabolic pathways responsible for the synthesis of pyrimidine nucleotides or arginine. The MGS-like domain is the C-terminal domain of CarB and appears to play a regulatory role in CPS function by binding allosteric effector molecules, including UMP and ornithine.
Pssm-ID: 238712 [Multi-domain] Cd Length: 110 Bit Score: 74.05 E-value: 2.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1319 NILLSIgSYKNKSELLPTVQTLESLGYNLYASLGTADFYTEHGVKVMAVdwpfeeesdcpNKDKQR--NIMDYLEENHFD 1396
Cdd:cd01424 2 TVFISV-ADRDKPEAVEIAKRLAELGFKLVATEGTAKYLQEAGIPVEVV-----------NKVSEGrpNIVDLIKNGEIQ 69
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 822092823 1397 LVINLSmrnSGGRrlssFVTKGYRTRRMAIDFSVPLITDI 1436
Cdd:cd01424 70 LVINTP---SGKR----AIRDGFSIRRAALEYKVPYFTTL 102
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
1470-1816 |
3.12e-15 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 81.04 E-value: 3.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1470 LPGLIDVHVHLREP--GATHKEDFSSGTAAALAGGITMVC--AMPnTNPAIIDpnSFTMAQKLAKAGCrCDYALFVGAS- 1544
Cdd:PLN02942 56 MPGGIDPHTHLAMPfmGTETIDDFFSGQAAALAGGTTMHIdfVIP-VNGNLLA--GYEAYEKKAEKSC-MDYGFHMAITk 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1545 -SDNAALLPSIASSTAGL---KMYLndTYSTLKMDNVSLWMEHFEKWPK--HLPIVaHAE-------------------- 1598
Cdd:PLN02942 132 wDDTVSRDMETLVKEKGInsfKFFM--AYKGSLMVTDELLLEGFKRCKSlgALAMV-HAEngdavfegqkrmielgitgp 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1599 -------------KQTVAAILLvAQLYQRPVHICHVAKKEEILIIRAAKQKGIQVTCEVAPHHLFLceDNVPVIGKD--- 1662
Cdd:PLN02942 209 eghalsrppllegEATARAIRL-AKFVNTPLYVVHVMSIDAMEEIARARKSGQRVIGEPVVSGLVL--DDSKLWDPDfti 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1663 --KAQVRPMLGTREDMEALWENLD--IIDCFATDHAPHSAEEKIS-----EKPPPGYPGLETMLPLLF-TAVSEGRLTVD 1732
Cdd:PLN02942 286 asKYVMSPPIRPAGHGKALQAALSsgILQLVGTDHCPFNSTQKAFgkddfRKIPNGVNGIEERMHLVWdTMVESGQISPT 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1733 DIIKRLYENPRKIFS--------LPAQEDTYVEVDLEQEWIIPKHMQFTKSKWTPFEGMKVKGKVMRVVLRGEVAYIDGQ 1804
Cdd:PLN02942 366 DYVRVTSTECAKIFNiyprkgaiLAGSDADIIILNPNSTFTISAKTHHSRIDTNVYEGRRGKGKVEVTISQGRVVWENGE 445
|
410
....*....|..
gi 822092823 1805 VLVPPGYGQDVK 1816
Cdd:PLN02942 446 LKVVRGSGRYIE 457
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
505-716 |
6.28e-15 |
|
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440208 [Multi-domain] Cd Length: 263 Bit Score: 77.22 E-value: 6.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 505 GTPVASIEMTEDRKIFVEKMEEINEHVAPSEAAMSVEQAVAAAERLGYPVLVRSAFALGGLGSGFANNRDEMITLVTQAF 584
Cdd:COG0439 43 GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEAR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 585 AHT------SQVLVDKSLKGwKEIEYEVVrdAYDNCVTVCNM---ENIDPLGIHTGEsivVAPSQtLNDYEYNMLRNTAI 655
Cdd:COG0439 123 AEAkagspnGEVLVEEFLEG-REYSVEGL--VRDGEVVVCSItrkHQKPPYFVELGH---EAPSP-LPEELRAEIGELVA 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 822092823 656 KVIRHLGVV-GECNIQYALNPESEqYYIIEVNARLS--RSSALASKATGYPLAYVAAKLSLGIP 716
Cdd:COG0439 196 RALRALGYRrGAFHTEFLLTPDGE-PYLIEINARLGgeHIPPLTELATGVDLVREQIRLALGEP 258
|
|
| PRK12562 |
PRK12562 |
ornithine carbamoyltransferase subunit F; Provisional |
1930-2230 |
9.42e-15 |
|
ornithine carbamoyltransferase subunit F; Provisional
Pssm-ID: 105755 Cd Length: 334 Bit Score: 77.79 E-value: 9.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1930 QHILSVRQFSKEQMSHLFNVAHTLRLMVQKERPLDILKGKVMASMFYEVSTRTSSSFAAAMHRLGGSVVHFCESTSSTQK 2009
Cdd:PRK12562 7 KHFLKLLDFTPAELNSLLQLAAKLKADKKNGKEVARLTGKNIALIFEKDSTRTRCSFEVAAYDQGARVTYLGPSGSQIGH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 2010 GESLVDSVNTMSCYADVIVLRHPIPGAVESAARHCRRPVINaGDGVGEHPTQALLDIFTIREEL--GTVNGMTITMVGDL 2087
Cdd:PRK12562 87 KESIKDTARVLGRMYDGIQYRGHGQEVVETLAEYAGVPVWN-GLTNEFHPTQLLADLLTMQEHLpgKAFNEMTLVYAGDA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 2088 KH--GRTVHSLARLLTqyrITLRYVAPK----NLSMPAEIIDFVASKGIKQEEFNSIEEALPDTDVLY------MTRIQK 2155
Cdd:PRK12562 166 RNnmGNSMLEAAALTG---LDLRLVAPQacwpEASLVAECSALAQKHGGKITLTEDIAAGVKGADFIYtdvwvsMGEPKE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 2156 ---ERFSSEKEYNACFGQFILT--PHI------------MTGAKRKMVVMHPLPRVNEISVEVDTDPRAAYFRQAENGMY 2218
Cdd:PRK12562 243 kwaERIALLRGYQVNSKMMALTgnPQVkflhclpafhddQTTLGKKMAKEFGLHGGMEVTDEVFESPASIVFDQAENRMH 322
|
330
....*....|..
gi 822092823 2219 IRMALLATVLGR 2230
Cdd:PRK12562 323 TIKAVMVATLAK 334
|
|
| PRK08417 |
PRK08417 |
metal-dependent hydrolase; |
1470-1800 |
9.44e-15 |
|
metal-dependent hydrolase;
Pssm-ID: 236262 [Multi-domain] Cd Length: 386 Bit Score: 78.59 E-value: 9.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1470 LPGLIDVHVhlrepgATHKEDFSSGT-----AAALAGGITMVCAMPNTNPAIIDPNSFTMAQ------------------ 1526
Cdd:PRK08417 29 LPALVDLNV------SLKNDSLSSKNlksleNECLKGGVGSIVLYPDSTPAIDNEIALELINsaqrelpmqifpsirald 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1527 ---KLA------KAGCRCDYAlfvgASSDNAALLPSIA------SSTAGLKMYLNDTYSTLKMDNVSLWMEhfekwpKHL 1591
Cdd:PRK08417 103 edgKLSniatllKKGAKALEL----SSDLDANLLKVIAqyakmlDVPIFCRCEDSSFDDSGVMNDGELSFE------LGL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1592 P-IVAHAEKQTVAAILLVAQLYQRPVHICHVAKKEEILIIRAAKQKGIQVTCEVAPHHLFL----CED-NVpvigkdKAQ 1665
Cdd:PRK08417 173 PgIPSIAETKEVAKMKELAKFYKNKVLFDTLALPRSLELLDKFKSEGEKLLKEVSIHHLILddsaCENfNT------AAK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1666 VRPMLGTREDMEALWENLD--IIDCFATDHAPHSAEEK--ISEKPPPGYPGLETMLPLLFT-AVSEGRLTVDDIIKRLYE 1740
Cdd:PRK08417 247 LNPPLRSKEDRLALLEALKegKIDFLTSLHSAKSNSKKdlAFDEAAFGIDSICEYFSLCYTyLVKEGIITWSELSRFTSY 326
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 822092823 1741 NPRKIFSLPAQEDT------YVEVDLEQEWIIPKhmqftksKWTPFEGMKVKGKVMRVVLRGEVAY 1800
Cdd:PRK08417 327 NPAQFLGLNSGEIEvgkeadLVLFDPNESTIIDD-------NFSLYSGDELYGKIEAVIIKGKLYL 385
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
1032-1254 |
1.94e-14 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 76.85 E-value: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1032 LHRQQCRILGTSPEFIDNAENRFKFSRMLDTIGISQPRWKELSDTES--AVNFCETVGYPCLVRPSYVLSGAAMNVAYSD 1109
Cdd:PRK12767 91 FEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDfkAALAKGELQFPLFVKPRDGSASIGVFKVNDK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1110 TDMEKFLSSAVavskehPVVISKFIQEaKEIDVDA-VACDGEVIAIAVSEHVEnagVHSGDA-TLVTPPQDINQKTMERI 1187
Cdd:PRK12767 171 EELEFLLEYVP------NLIIQEFIEG-QEYTVDVlCDLNGEVISIVPRKRIE---VRAGETsKGVTVKDPELFKLAERL 240
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 822092823 1188 kmivhaiGQELQVTGPFNLQLIAKDDQLKVIECNVRVSRSFPyVSKTLGVDLVALATRVILGEEVEA 1254
Cdd:PRK12767 241 -------AEALGARGPLNIQCFVTDGEPYLFEINPRFGGGYP-LSYMAGANEPDWIIRNLLGGENEP 299
|
|
| PRK14804 |
PRK14804 |
ornithine carbamoyltransferase; Provisional |
1930-2228 |
1.41e-13 |
|
ornithine carbamoyltransferase; Provisional
Pssm-ID: 173265 [Multi-domain] Cd Length: 311 Bit Score: 73.91 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1930 QHILSVRQFSKEQMSHLFNVAhtlrLMVQKERP--LDILKGKVMASMFYEVSTRTSSSFAAAMHRLGGSVVHFCESTSST 2007
Cdd:PRK14804 7 KHLISWEDWSDSEILDLLDFA----VHVKKNRVnyAGHMSGRSLAMLFQKTSTRTRVSFEVAMTEMGGHGIYLDWMASNF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 2008 Q------KGESLVDSVNTMSC----YADVIVLRHpipGAvesaarhcRRPVINAGDGVGeHPTQALLDIFTIREELGTV- 2076
Cdd:PRK14804 83 QlsdidlEARYLSRNVSVIMArlkkHEDLLVMKN---GS--------QVPVINGCDNMF-HPCQSLADIMTIALDSPEIp 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 2077 -NGMTITMVGdlKHGRTVHSLARLLTQYRITLRYVAP--KNLSMPAEIIDFVASKGIKQEEFNsIEEALPDTDVLYMTRI 2153
Cdd:PRK14804 151 lNQKQLTYIG--VHNNVVNSLIGITAALGIHLTLVTPiaAKENIHAQTVERAKKKGTLSWEMN-LHKAVSHADYVYTDTW 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 2154 QKERFSSEKEYNACFGQFI--LTPHIMTGA---KRKMVVMHPLP--RVNEISVEVDTDPRAAYFRQAENGMYIRMALLAT 2226
Cdd:PRK14804 228 LDMEFFNDPSYADKKKQRMelMMPYQINSSlmeKTNAKVMHDMPihAGYEITREVVLSDRSIIFQQAENRLDAQKAVILK 307
|
..
gi 822092823 2227 VL 2228
Cdd:PRK14804 308 LL 309
|
|
| PRK06774 |
PRK06774 |
aminodeoxychorismate synthase component II; |
191-342 |
2.24e-13 |
|
aminodeoxychorismate synthase component II;
Pssm-ID: 180689 [Multi-domain] Cd Length: 191 Bit Score: 70.66 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 191 YNQIRCLCQRGARVTVVPWDQpLDSNDFDGL-----FISNGPGNPEYCKETVENIRKVAcveNPKPIFGICLGHQLLSLV 265
Cdd:PRK06774 13 YNLYQYFCELGTEVMVKRNDE-LQLTDIEQLapshlVISPGPCTPNEAGISLAVIRHFA---DKLPILGVCLGHQALGQA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 266 IGAKTYKMKYGNRG------HNQPCIHKGTSRCYITSQNHGFAVDPETLPKDWDVL-FTNANDQTSE--GIVHNHKPLFS 336
Cdd:PRK06774 89 FGARVVRARQVMHGktsaicHSGQGVFRGLNQPLTVTRYHSLVIAADSLPGCFELTaWSERGGEMDEimGIRHRTLPLEG 168
|
....*.
gi 822092823 337 VQFHPE 342
Cdd:PRK06774 169 VQFHPE 174
|
|
| PRK01713 |
PRK01713 |
ornithine carbamoyltransferase; Provisional |
1927-2228 |
2.59e-13 |
|
ornithine carbamoyltransferase; Provisional
Pssm-ID: 167263 [Multi-domain] Cd Length: 334 Bit Score: 73.48 E-value: 2.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1927 LVGQHILSVRQFSKEQMSHLFNVAHTLRLMVQKERPLDILKGKVMASMFYEVSTRTSSSFAAAMHRLGGSVVHFCESTSS 2006
Cdd:PRK01713 5 LKNRHLLSLVNHTEREIKYLLDLSRDLKRAKYAGTEQQRLKGKNIALIFEKTSTRTRCAFEVAAYDQGAQVTYIDPNSSQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 2007 TQKGESLVDSVNTMSCYADVIVLRHPIPGAVESAARHCRRPVINagdGVGE--HPTQALLDIFTIREELGT-VNGMTITM 2083
Cdd:PRK01713 85 IGHKESMKDTARVLGRMYDAIEYRGFKQSIVNELAEYAGVPVFN---GLTDefHPTQMLADVLTMIENCDKpLSEISYVY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 2084 VGDLKHGRTvHSLARLLTQYRITLRYVAPKNLSMPAEIID----FVASKGIKQEEFNSIEEALPDTDVlymtrIQKERFS 2159
Cdd:PRK01713 162 IGDARNNMG-NSLLLIGAKLGMDVRICAPKALLPEASLVEmcekFAKESGARITVTDDIDKAVKGVDF-----VHTDVWV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 2160 SEKEYNACFGQFI-------LTPHIM--TGaKRKMVVMHPLPRVN---------------------EISVEVDTDPRAAY 2209
Cdd:PRK01713 236 SMGEPLETWGERIkllmpyqVTPELMkrTG-NPKVKFMHCLPAFHnsetkvgrqiaekypelangiEVTEDVFESPMNIA 314
|
330
....*....|....*....
gi 822092823 2210 FRQAENGMYIRMALLATVL 2228
Cdd:PRK01713 315 FEQAENRMHTIKAVMVASL 333
|
|
| GATase1_GMP_Synthase |
cd01742 |
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ... |
206-342 |
2.61e-13 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase. GMP synthetase is a glutamine amidotransferase from the de novo purine biosynthetic pathway. Glutamine amidotransferase (GATase) activity catalyse the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. GMP synthetase catalyses the amination of the nucleotide precursor xanthosine 5'-monophosphate to form GMP. GMP synthetase belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.
Pssm-ID: 153213 [Multi-domain] Cd Length: 181 Bit Score: 70.26 E-value: 2.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 206 VVPWDQPLDS---NDFDGLFISNGP------GNPEYCKETVENIrkvacvenpKPIFGICLGHQLLSLVIGAKTYKMKYG 276
Cdd:cd01742 27 ILPNTTPLEEiklKNPKGIILSGGPssvyeeDAPRVDPEIFELG---------VPVLGICYGMQLIAKALGGKVERGDKR 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 822092823 277 NRGH------NQPCIHKGTSRcyiTSQ---NHGFAVdpETLPKDWDVLFTNANDQTsEGIVHNHKPLFSVQFHPE 342
Cdd:cd01742 98 EYGKaeieidDSSPLFEGLPD---EQTvwmSHGDEV--VKLPEGFKVIASSDNCPV-AAIANEEKKIYGVQFHPE 166
|
|
| PRK13566 |
PRK13566 |
anthranilate synthase component I; |
199-342 |
3.02e-13 |
|
anthranilate synthase component I;
Pssm-ID: 237429 [Multi-domain] Cd Length: 720 Bit Score: 75.34 E-value: 3.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 199 QRGARVTVVPWDQP---LDSNDFDGLFISNGPGNPE--YCKETVEnirkvACVENPKPIFGICLGHQLLSLVIGAKTYKM 273
Cdd:PRK13566 548 QTGAEVTTVRYGFAeemLDRVNPDLVVLSPGPGRPSdfDCKATID-----AALARNLPIFGVCLGLQAIVEAFGGELGQL 622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 274 KYGNRG------HNQPC-IHKGTSRCYITSQNHGFAVDPETLPKDWDVLFTnandqTSEGIV----HNHKPLFSVQFHPE 342
Cdd:PRK13566 623 AYPMHGkpsrirVRGPGrLFSGLPEEFTVGRYHSLFADPETLPDELLVTAE-----TEDGVImaieHKTLPVAAVQFHPE 697
|
|
| PRK14607 |
PRK14607 |
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase; |
221-383 |
7.27e-13 |
|
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
Pssm-ID: 237764 [Multi-domain] Cd Length: 534 Bit Score: 73.60 E-value: 7.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 221 LFISNGPGNPEYCKETVENIRKVACVenpKPIFGICLGHQLLSLVIGAKTYKMKYGNRGHNQPCIHKGT------SRCYI 294
Cdd:PRK14607 48 IVISPGPGRPEEAGISVEVIRHFSGK---VPILGVCLGHQAIGYAFGGKIVHAKRILHGKTSPIDHNGKglfrgiPNPTV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 295 TSQNHGFAVDPETLPKDWDVLfTNANDQTSEGIVHNHKPLFSVQFHPEHMaGPTDLVGLFDVFLDTVRdvkENKAGKSVK 374
Cdd:PRK14607 125 ATRYHSLVVEEASLPECLEVT-AKSDDGEIMGIRHKEHPIFGVQFHPESI-LTEEGKRILKNFLNYQR---EEIDIKSYL 199
|
170
....*....|.
gi 822092823 375 QRLM--EHLTF 383
Cdd:PRK14607 200 KKLVegEDLSF 210
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
397-708 |
1.11e-12 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 71.45 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 397 KVLVLGSGGlsigqagefdysGSQAIKAMKEENIQTILINPNIATVQTSKGLADKVYFLP-IT-PEYVTQVI---KNERP 471
Cdd:PRK12767 3 NILVTSAGR------------RVQLVKALKKSLLKGRVIGADISELAPALYFADKFYVVPkVTdPNYIDRLLdicKKEKI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 472 DGVLLTFGGQTALNCG--VELKKQGVLekykvrVLGTPVASIEMTEDRKIFVEKMEEINEHVAPSEAAMSVEQAVAA--A 547
Cdd:PRK12767 71 DLLIPLIDPELPLLAQnrDRFEEIGVK------VLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDFKAAlaK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 548 ERLGYPVLVRSAFALGGLGSGFANNRDEmitlVTQAFAHTSQVLVDKSLKGwKEIEYEVVRDAYDNCVTVCNMENIDPLG 627
Cdd:PRK12767 145 GELQFPLFVKPRDGSASIGVFKVNDKEE----LEFLLEYVPNLIIQEFIEG-QEYTVDVLCDLNGEVISIVPRKRIEVRA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 628 ihtGESI--VVAPSQTLNDYeynmlrntAIKVIRHLGVVGECNIQYALNPEseQYYIIEVNARLSrssalaskaTGYPLA 705
Cdd:PRK12767 220 ---GETSkgVTVKDPELFKL--------AERLAEALGARGPLNIQCFVTDG--EPYLFEINPRFG---------GGYPLS 277
|
...
gi 822092823 706 YVA 708
Cdd:PRK12767 278 YMA 280
|
|
| PRK08007 |
PRK08007 |
aminodeoxychorismate synthase component 2; |
191-342 |
1.65e-12 |
|
aminodeoxychorismate synthase component 2;
Pssm-ID: 181194 [Multi-domain] Cd Length: 187 Bit Score: 68.40 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 191 YNQIRCLCQRGARVtVVPWDQPLDSNDFDGL-----FISNGPGNPEYCKETVENIRKVAcveNPKPIFGICLGHQLLSLV 265
Cdd:PRK08007 13 WNLYQYFCELGADV-LVKRNDALTLADIDALkpqkiVISPGPCTPDEAGISLDVIRHYA---GRLPILGVCLGHQAMAQA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 266 IGAKTYKMKYGNRGHNQPCIHKGT------SRCYITSQNHGFAVDPETLPKDWDVlftNANDQTSE--GIVHNHKPLFSV 337
Cdd:PRK08007 89 FGGKVVRAAKVMHGKTSPITHNGEgvfrglANPLTVTRYHSLVVEPDSLPACFEV---TAWSETREimGIRHRQWDLEGV 165
|
....*
gi 822092823 338 QFHPE 342
Cdd:PRK08007 166 QFHPE 170
|
|
| PRK07649 |
PRK07649 |
aminodeoxychorismate/anthranilate synthase component II; |
219-342 |
2.17e-12 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181066 [Multi-domain] Cd Length: 195 Bit Score: 67.91 E-value: 2.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 219 DGLFISNGPGNPEYCKETVENIRKVAcveNPKPIFGICLGHQLLSLVIGAKTYKM------KYGNRGHNQPCIHKGTSRC 292
Cdd:PRK07649 45 DFLMISPGPCSPNEAGISMEVIRYFA---GKIPIFGVCLGHQSIAQVFGGEVVRAerlmhgKTSLMHHDGKTIFSDIPNP 121
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 822092823 293 YITSQNHGFAVDPETLPKDWDVlftnaNDQTSEG----IVHNHKPLFSVQFHPE 342
Cdd:PRK07649 122 FTATRYHSLIVKKETLPDCLEV-----TSWTEEGeimaIRHKTLPIEGVQFHPE 170
|
|
| PRK00758 |
PRK00758 |
GMP synthase subunit A; Validated |
181-342 |
2.89e-12 |
|
GMP synthase subunit A; Validated
Pssm-ID: 179112 [Multi-domain] Cd Length: 184 Bit Score: 67.18 E-value: 2.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 181 RITAIDCGIKYNQI--RCLCQRGARVTVVPWDQPLDSND--FDGLFISNGP-----GNpeyCKETVENIrKVacvenpkP 251
Cdd:PRK00758 1 KIVVVDNGGQYNHLihRTLRYLGVDAKIIPNTTPVEEIKafEDGLILSGGPdieraGN---CPEYLKEL-DV-------P 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 252 IFGICLGHQLLSLVIGAKTYKMKYGNRG--------HNQpcIHKGTSRCYITSQNHGFAVdpETLPKDWDVLFTNANDQT 323
Cdd:PRK00758 70 ILGICLGHQLIAKAFGGEVGRGEYGEYAlveveildEDD--ILKGLPPEIRVWASHADEV--KELPDGFEILARSDICEV 145
|
170
....*....|....*....
gi 822092823 324 sEGIVHNHKPLFSVQFHPE 342
Cdd:PRK00758 146 -EAMKHKEKPIYGVQFHPE 163
|
|
| PRK04523 |
PRK04523 |
N-acetylornithine carbamoyltransferase; Reviewed |
1930-2230 |
3.27e-12 |
|
N-acetylornithine carbamoyltransferase; Reviewed
Pssm-ID: 235304 [Multi-domain] Cd Length: 335 Bit Score: 70.16 E-value: 3.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1930 QHILSVRQFSKEQMSHLFNVAHTLRlmvqKERPLDILKGKVMASMFYEVSTRTSSSFAAAMHRLGGSVV----------- 1998
Cdd:PRK04523 4 KHFLNTQDWSRAELDALLTQAAAFK----RNKLGSALKGKSIALVFFNPSLRTRTSFELGAFQLGGHAVvlqpgkdawpi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1999 HFCESTSSTQ-KGESLVDSVNTMSCYADVIVLRHPIPGA----------VESAARHCRRPVINAGDGVgeHPTQALLDIF 2067
Cdd:PRK04523 80 EFELGAVMDGeTEEHIREVARVLSRYVDLIGVRAFPKFVdwskdrqdqvLNSFAKYSTVPVINMETIT--HPCQELAHAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 2068 TIREELG-TVNGMTI------------TMVGD------LKHGRTVhSLARLLTQYRITLRYVApknlsmPAEiiDFVASK 2128
Cdd:PRK04523 158 ALQEHFGtTLRGKKYvltwtyhpkplnTAVANsalliaTRLGMDV-TLLCPTPDYILDERYMD------WAE--QNAAES 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 2129 GIKQEEFNSIEEALPDTDVLYM----TRIQKERFSSEKEYNACFGQFILTPHIMtGAKRKMVVMHPLP-RVN-EISVEVD 2202
Cdd:PRK04523 229 GGSLTVSHDIDSAYAGADVVYAkswgALPFFGNWEPEKPIRDQYQHFIVDERKM-ALTNNGVFSHCLPlRRNvKVTDAVM 307
|
330 340
....*....|....*....|....*...
gi 822092823 2203 TDPRAAYFRQAENGMYIRMALLATVLGR 2230
Cdd:PRK04523 308 DSPNCIAIDEAENRLHVQKAIMAALASQ 335
|
|
| PRK08857 |
PRK08857 |
aminodeoxychorismate/anthranilate synthase component II; |
191-342 |
1.28e-11 |
|
aminodeoxychorismate/anthranilate synthase component II;
Pssm-ID: 181566 [Multi-domain] Cd Length: 193 Bit Score: 65.67 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 191 YNQIRCLCQRGARVTVVPWDQPldsnDFDG--------LFISNGPGNPEYCKETVENIRKVAcveNPKPIFGICLGHQLL 262
Cdd:PRK08857 13 YNLYQYFCELGAQVKVVRNDEI----DIDGiealnpthLVISPGPCTPNEAGISLQAIEHFA---GKLPILGVCLGHQAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 263 SLVIGAKTYKMKYGNRGHNQPCIH------KGTSRCYITSQNHGFAVDPETLPKDWDVL-FTNANDQTSE---GIVHNHK 332
Cdd:PRK08857 86 AQVFGGQVVRARQVMHGKTSPIRHtgrsvfKGLNNPLTVTRYHSLVVKNDTLPECFELTaWTELEDGSMDeimGFQHKTL 165
|
170
....*....|
gi 822092823 333 PLFSVQFHPE 342
Cdd:PRK08857 166 PIEAVQFHPE 175
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
394-718 |
1.28e-11 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 68.80 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 394 RPRKVLVLGS--GGLSIgqagefdysgsqaIKAMKEENIQTILINPN-IATVQTSKGLADKVYFLPITP------EYVTQ 464
Cdd:COG3919 4 MRFRVVVLGGdiNALAV-------------ARSLGEAGVRVIVVDRDpLGPAARSRYVDEVVVVPDPGDdpeafvDALLE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 465 VIKNERPDgVLLTFGgqtalNCGVEL--KKQGVLEKYkVRVLGTPVASIEMTEDRKIFVEKMEEINEHVAPSEAAMSVEQ 542
Cdd:COG3919 71 LAERHGPD-VLIPTG-----DEYVELlsRHRDELEEH-YRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSADD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 543 AVAAAERLGYPVLV--------RSAFALGGLGSGFANNRDEMITLVTQAFAHTSQVLVDkslkgwkeiEYEVVRDAYDNC 614
Cdd:COG3919 144 LDALAEDLGFPVVVkpadsvgyDELSFPGKKKVFYVDDREELLALLRRIAAAGYELIVQ---------EYIPGDDGEMRG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 615 VTVCNMENIDPLGIHTGESIVVAPSQ----TLNDYEYNM-LRNTAIKVIRHLGVVGECNIQYALNPESEQYYIIEVNARL 689
Cdd:COG3919 215 LTAYVDRDGEVVATFTGRKLRHYPPAggnsAARESVDDPeLEEAARRLLEALGYHGFANVEFKRDPRDGEYKLIEINPRF 294
|
330 340
....*....|....*....|....*....
gi 822092823 690 SRSSALASKAtGYPLAYVAAKLSLGIPLP 718
Cdd:COG3919 295 WRSLYLATAA-GVNFPYLLYDDAVGRPLE 322
|
|
| trpG |
CHL00101 |
anthranilate synthase component 2 |
191-344 |
1.42e-11 |
|
anthranilate synthase component 2
Pssm-ID: 214365 [Multi-domain] Cd Length: 190 Bit Score: 65.52 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 191 YNQIRCLCQRGARVTVVPWDQ----PLDSNDFDGLFISNGPGNPEYCKETVENIRKVAcveNPKPIFGICLGHQLLSLVI 266
Cdd:CHL00101 13 YNLVQSLGELNSDVLVCRNDEidlsKIKNLNIRHIIISPGPGHPRDSGISLDVISSYA---PYIPILGVCLGHQSIGYLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 267 GAKTYKMKYGNRG------HNQPCIHKGTSRCYITSQNHGFAVDPETLPKDwdvLFTNAndQTSEGIV----HNH-KPLF 335
Cdd:CHL00101 90 GGKIIKAPKPMHGktskiyHNHDDLFQGLPNPFTATRYHSLIIDPLNLPSP---LEITA--WTEDGLImacrHKKyKMLR 164
|
....*....
gi 822092823 336 SVQFHPEHM 344
Cdd:CHL00101 165 GIQFHPESL 173
|
|
| GATase1 |
cd01653 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
194-268 |
2.45e-11 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.
Pssm-ID: 153210 [Multi-domain] Cd Length: 115 Bit Score: 62.62 E-value: 2.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 194 IRCLCQRGARVTVVPWDQP-----LDSNDFDGLFISNGPGNPEYCKETVENIRKV-ACVENPKPIFGICLGHQLlsLVIG 267
Cdd:cd01653 18 LDALREAGAEVDVVSPDGGpvesdVDLDDYDGLILPGGPGTPDDLARDEALLALLrEAAAAGKPILGICLGAQL--LVLG 95
|
.
gi 822092823 268 A 268
Cdd:cd01653 96 V 96
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
524-788 |
6.22e-11 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 66.98 E-value: 6.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 524 MEEINEHVAP--SEAAMSVEQAVAAAERLGYPVLVRSAFALGGLGSGFANNRDEMitlvTQAFAHTSQ----------VL 591
Cdd:PRK06111 123 MQAAGVPVVPgiTTNLEDAEEAIAIARQIGYPVMLKASAGGGGIGMQLVETEQEL----TKAFESNKKraanffgngeMY 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 592 VDKSLKGWKEIEYEVVRDAYDNCVtvcnmenidplgiHTGE---SI------VV--APSQTLNDYEYNMLRNTAIKVIRH 660
Cdd:PRK06111 199 IEKYIEDPRHIEIQLLADTHGNTV-------------YLWErecSVqrrhqkVIeeAPSPFLDEETRKAMGERAVQAAKA 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 661 LGVVGECNIQYaLNPESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLSLGIPLPVLKNSVTNSTTA---------- 730
Cdd:PRK06111 266 IGYTNAGTIEF-LVDEQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKLSFTQDDIKRSGHAievriyaedp 344
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 822092823 731 -NFEPSLDycvvKVPRWDLSK--FLRVSTKIGSSMK-------SVGEVMAIGRSFEEAFQKALRMVDE 788
Cdd:PRK06111 345 kTFFPSPG----KITDLTLPGgeGVRHDHAVENGVTvtpfydpMIAKLIAHGETREEAISRLHDALEE 408
|
|
| GAT_1 |
cd03128 |
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
194-262 |
8.59e-11 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain.
Pssm-ID: 153222 [Multi-domain] Cd Length: 92 Bit Score: 60.29 E-value: 8.59e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 822092823 194 IRCLCQRGARVTVVPWDQP-----LDSNDFDGLFISNGPGNPEYCKETVENIRKV-ACVENPKPIFGICLGHQLL 262
Cdd:cd03128 18 LDALREAGAEVDVVSPDGGpvesdVDLDDYDGLILPGGPGTPDDLAWDEALLALLrEAAAAGKPVLGICLGAQLL 92
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
1064-1224 |
2.78e-09 |
|
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 396689 [Multi-domain] Cd Length: 169 Bit Score: 58.42 E-value: 2.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1064 GISQPRWKELSDTESAVNFCETVGYPCLV---RPSYvlSGAAMNVAYSDTDMEKFLSSAvavsKEHPVVISKFIQEAKEI 1140
Cdd:pfam02222 4 GLPTPRFMAAESLEELIEAGQELGYPCVVkarRGGY--DGKGQYVVRSEADLPQAWEEL----GDGPVIVEEFVPFDREL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1141 DVDAV-ACDGEVIAIAVSEHVEnagvHSGDATLVTPPQDINQKTMERIKMIVHAIGQELQVTGPFNLQL-IAKDDQLKVI 1218
Cdd:pfam02222 78 SVLVVrSVDGETAFYPVVETIQ----EDGICRLSVAPARVPQAIQAEAQDIAKRLVDELGGVGVFGVELfVTEDGDLLIN 153
|
....*.
gi 822092823 1219 ECNVRV 1224
Cdd:pfam02222 154 ELAPRP 159
|
|
| PRK07200 |
PRK07200 |
aspartate/ornithine carbamoyltransferase family protein; Validated |
1939-2149 |
3.80e-09 |
|
aspartate/ornithine carbamoyltransferase family protein; Validated
Pssm-ID: 235961 [Multi-domain] Cd Length: 395 Bit Score: 61.29 E-value: 3.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1939 SKEQMSHLFNVAHTLRLMVQKERPLDILKGKVMASMFYEVSTRTSSSFAAAMHRLGGSVVHFCESTSSTQKGESLVDSVN 2018
Cdd:PRK07200 30 TPDELKAVLDVADALRALREENISTKVFNSGLGISVFRDNSTRTRFSYASACNLLGLEVQDLDEGKSQIAHGETVRETAN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 2019 TMSCYADVIVLR------------HPIPGAVESAARHC---RRP-VINAGDGVgEHPTQALLDIFTIREELGTVN---GM 2079
Cdd:PRK07200 110 MISFMADVIGIRddmyigkgnaymREVGAAVDDGYKQGvlpQRPtLVNLQCDI-DHPTQSMADLLHLIEHFGGLEnlkGK 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 2080 TITMVGDL--KHGRTV---HSLARLLTQYRITLRYVAPKNLSMPAEIIDfVASK-----GIKQEEFNSIEEALPDTDVLY 2149
Cdd:PRK07200 189 KIAMTWAYspSYGKPLsvpQGIIGLMTRFGMDVTLAHPEGYDLMPEVVE-VAKKnakasGGSFRQVNSMEEAFKDADIVY 267
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
539-724 |
6.59e-09 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 60.89 E-value: 6.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 539 SVEQAVAAAERLGYPVLVRSAFALGGLGSGFANNRDEM-------ITLVTQAFAhTSQVLVDKSLKGWKEIEYEVVRDAY 611
Cdd:PRK07178 139 DLDEALAEAERIGYPVMLKATSGGGGRGIRRCNSREELeqnfprvISEATKAFG-SAEVFLEKCIVNPKHIEVQILADSH 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 612 DNCVTV----CNMENidplgiHTGESIVVAPSQTLNDYEYNMLRNTAIKVIRHLGVVGECNIQYALNPESEqYYIIEVNA 687
Cdd:PRK07178 218 GNVVHLferdCSIQR------RNQKLIEIAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDADGE-VYFMEMNT 290
|
170 180 190
....*....|....*....|....*....|....*..
gi 822092823 688 RLSRSSALASKATGYPLAYVAAKLSLGIPLPVLKNSV 724
Cdd:PRK07178 291 RVQVEHTITEEITGIDIVREQIRIASGLPLSYKQEDI 327
|
|
| PRK06895 |
PRK06895 |
anthranilate synthase component II; |
207-342 |
1.04e-08 |
|
anthranilate synthase component II;
Pssm-ID: 235882 [Multi-domain] Cd Length: 190 Bit Score: 57.05 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 207 VPWD----QPLDSND---FDGLFISNGPGNPEYCKETVENIRKVacvENPKPIFGICLGHQLLSLVIGAKTYKMKYGNRG 279
Cdd:PRK06895 26 VPMQvvnvEDLDLDEvenFSHILISPGPDVPRAYPQLFAMLERY---HQHKSILGVCLGHQTLCEFFGGELYNLNNVRHG 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 822092823 280 HNQPCIHKGTSRCYitsQN----------HGFAVDPETLPKDwdvlfTNANDQTSEGIV----HNHKPLFSVQFHPE 342
Cdd:PRK06895 103 QQRPLKVRSNSPLF---DGlpeefniglyHSWAVSEENFPTP-----LEITAVCDENVVmamqHKTLPIYGVQFHPE 171
|
|
| GATase1_2 |
cd01745 |
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
244-357 |
1.99e-08 |
|
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.
Pssm-ID: 153216 [Multi-domain] Cd Length: 189 Bit Score: 56.43 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 244 ACVENPKPIFGICLGHQLLSLVIGAKTYKMKYGNRGHNQpcihkgtsrcyitsqnhgfAVDpeTLPKDWDVLFTnANDQT 323
Cdd:cd01745 95 AALERGKPILGICRGMQLLNVALGGTLYQDIRVNSLHHQ-------------------AIK--RLADGLRVEAR-APDGV 152
|
90 100 110
....*....|....*....|....*....|....*.
gi 822092823 324 SEGIVH-NHKPLFSVQFHPEHMA-GPTDLVGLFDVF 357
Cdd:cd01745 153 IEAIESpDRPFVLGVQWHPEWLAdTDPDSLKLFEAF 188
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
497-689 |
4.40e-08 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 58.07 E-value: 4.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 497 EKYKVRVLGTPVASIEMTEDrKIFVEK-MEEINEHVAP--SEAAMSVEQAVAAAERLGYPVLVRSAFALGGLGSGFANNR 573
Cdd:PRK08654 96 EKAGIVFIGPSSDVIEAMGS-KINAKKlMKKAGVPVLPgtEEGIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 574 DEMITLV--TQAFAHT----SQVLVDKSLKGWKEIEYEVVRDAYDNCvtvcnmenidplgIHTGES-----------IVV 636
Cdd:PRK08654 175 EELEDAIesTQSIAQSafgdSTVFIEKYLEKPRHIEIQILADKHGNV-------------IHLGDRecsiqrrhqklIEE 241
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 822092823 637 APSQTLNDYEYNMLRNTAIKVIRHLGVVGECNIQYALnpESEQYYIIEVNARL 689
Cdd:PRK08654 242 APSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLY--SNGNFYFLEMNTRL 292
|
|
| Peptidase_C26 |
pfam07722 |
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ... |
244-342 |
1.18e-07 |
|
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze the cleavage of the gamma-glutamyl bond in poly-gamma-glutamyl substrates. They are structurally related to pfam00117, but contain extensions in four loops and at the C terminus.
Pssm-ID: 429620 [Multi-domain] Cd Length: 219 Bit Score: 54.57 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 244 ACVENPKPIFGICLGHQLLSLVIGAKTY---KMKYGNRGHNQPC------------IHKGT--SRCYITSQ---N--HGF 301
Cdd:pfam07722 100 AALARGKPILGICRGFQLLNVALGGTLYqdiQEQPGFTDHREHCqvapyapshavnVEPGSllASLLGSEEfrvNslHHQ 179
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 822092823 302 AVDpeTLPKDWDVLFTnANDQTSEGIVH--NHKPLFSVQFHPE 342
Cdd:pfam07722 180 AID--RLAPGLRVEAV-APDGTIEAIESpnAKGFALGVQWHPE 219
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
495-718 |
1.35e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 56.68 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 495 VLEKYKVRVLGTPVASIEMTEDRKIFVEKMEEINEHVAP-SEAAM-SVEQAVAAAERLGYPVLVRSAFALGGLGSGFANN 572
Cdd:PRK08462 96 ICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPgSDGALkSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVED 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 573 RDEMITLVT-------QAFAHTSqVLVDKSLKGWKEIEYEVVRDAYDNCVTV----CNMENidplgiHTGESIVVAPSQT 641
Cdd:PRK08462 176 ESDLENLYLaaesealSAFGDGT-MYMEKFINNPRHIEVQILGDKHGNVIHVgerdCSLQR------RHQKLIEESPAVV 248
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 822092823 642 LNDYEYNMLRNTAIKVIRHLGVVGECNIQYALNpESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLSLGIPLP 718
Cdd:PRK08462 249 LDEKTRERLHETAIKAAKAIGYEGAGTFEFLLD-SNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEELP 324
|
|
| PLN02335 |
PLN02335 |
anthranilate synthase |
220-342 |
3.24e-07 |
|
anthranilate synthase
Pssm-ID: 177969 [Multi-domain] Cd Length: 222 Bit Score: 53.26 E-value: 3.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 220 GLFISNGPGNPEYCKETVENIRKVAcvenPK-PIFGICLGHQLLSLVIGAKTYKMKYG-NRGHNQPCIH---------KG 288
Cdd:PLN02335 65 GVLISPGPGTPQDSGISLQTVLELG----PLvPLFGVCMGLQCIGEAFGGKIVRSPFGvMHGKSSPVHYdekgeeglfSG 140
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 822092823 289 TSRCYITSQNHGFAVDPETLPKDWDVLFTNANDQTSEGIVHN-HKPLFSVQFHPE 342
Cdd:PLN02335 141 LPNPFTAGRYHSLVIEKDTFPSDELEVTAWTEDGLIMAARHRkYKHIQGVQFHPE 195
|
|
| PRK06849 |
PRK06849 |
hypothetical protein; Provisional |
1037-1224 |
5.10e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 235876 [Multi-domain] Cd Length: 389 Bit Score: 54.28 E-value: 5.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1037 CRILGTSPEFIDNAENRFKFSRMLDTIGISQPRWKELSDTESAVNF-CETVGYPCLVRPSYVLSGAAMNVaysdTDMEKF 1115
Cdd:PRK06849 101 CEVLHFDFELLLLLHNKWEFAEQARSLGLSVPKTYLITDPEAIRNFmFKTPHTPYVLKPIYSRFVRRVDL----LPKEAA 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1116 LSSaVAVSKEHPVVISKFIQeAKEIDVDAVACDGEVIAIA--VSEHVENAGVHSGDATLVTPpqdinqktmeRIKMIVHA 1193
Cdd:PRK06849 177 LKE-LPISKDNPWVMQEFIQ-GKEYCSYSIVRSGELRAHScyKPEYCAGSGAQIAFQPINHP----------RIEEFVTH 244
|
170 180 190
....*....|....*....|....*....|..
gi 822092823 1194 IGQELQVTGPFNLQLI-AKDDQLKVIECNVRV 1224
Cdd:PRK06849 245 FVKELNYTGQISFDFIeTENGDAYPIECNPRT 276
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
504-686 |
3.81e-06 |
|
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).
Pssm-ID: 429483 [Multi-domain] Cd Length: 204 Bit Score: 50.01 E-value: 3.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 504 LGTPVASIEMTEdRKIFVEKMEEINEHVApseaamsveqavaaaERLGYPVLVRSAfalgGLGSGF----ANNRDEMITL 579
Cdd:pfam07478 5 AGLPVVPFVTFT-RADWKLNPKEWCAQVE---------------EALGYPVFVKPA----RLGSSVgvskVESREELQAA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 580 VTQAFAHTSQVLVDKSLKGwKEIEYEVvrdaydncvtvcnMENIDPlgiHTGESIVVAPSQTLNDYE------------- 646
Cdd:pfam07478 65 IEEAFQYDEKVLVEEGIEG-REIECAV-------------LGNEDP---EVSPVGEIVPSGGFYDYEakyiddsaqivvp 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 822092823 647 -------YNMLRNTAIKVIRHLGVVGECNIQYALnPESEQYYIIEVN 686
Cdd:pfam07478 128 adleeeqEEQIQELALKAYKALGCRGLARVDFFL-TEDGEIVLNEVN 173
|
|
| GATase1_Glutamyl_Hydrolase |
cd01747 |
Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 ... |
201-342 |
5.64e-06 |
|
Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase; Type 1 glutamine amidotransferase (GATase1) domain found in gamma-Glutamyl Hydrolase. gamma-Glutamyl Hydrolase catalyzes the cleavage of the gamma-glutamyl chain of folylpoly-gamma-glutamyl substrates and is a central enzyme in folyl and antifolyl poly-gamma-glutamate metabolism. GATase activity involves the removal of the ammonia group from a glutamate molecule and its subsequent transfer to a specific substrate, thus creating a new carbon-nitrogen group on the substrate. gamma-Glutamyl hydrolases belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.
Pssm-ID: 153218 [Multi-domain] Cd Length: 273 Bit Score: 50.40 E-value: 5.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 201 GARVtvVPWDQPLDSNDFDGLFIS-NG---PG-----NPEYCKETVENIRKVACVENPK----PIFGICLGHQLLSLVIG 267
Cdd:cd01747 33 GARV--VPIWINESEEYYDKLFKSiNGilfPGgavdiDTSGYARTAKIIYNLALERNDAgdyfPVWGTCLGFELLTYLTS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 268 ----------AKTYKMKYGNRGHNQPC----------IHKGTSRCyITSQNHGFAVDPETLPKD------WDVLFTNAND 321
Cdd:cd01747 111 getllleateATNSALPLNFTEDALQSrlfkrfppdlLKSLATEP-LTMNNHRYGISPENFTENgllsdfFNVLTTNDDW 189
|
170 180
....*....|....*....|....
gi 822092823 322 QTSEGIV---HNHKPLFSVQFHPE 342
Cdd:cd01747 190 NGVEFIStveAYKYPIYGVQWHPE 213
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
964-1248 |
6.29e-06 |
|
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 439959 [Multi-domain] Cd Length: 289 Bit Score: 50.32 E-value: 6.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 964 IMELRKMGYKTIMVNYnpetvstdydmcDRLYFDEISFEVVMDIYEMENPEGVILSMGGQLPN-NIAMSLHRQQCRILGt 1042
Cdd:COG0189 20 IEAAQRRGHEVEVIDP------------DDLTLDLGRAPELYRGEDLSEFDAVLPRIDPPFYGlALLRQLEAAGVPVVN- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1043 SPEFIDNAENRFKFSRMLDTIGISQPRWKELSDTESAVNFCETVGYPCLVRPSYvlSGAAMNVAYSDTDMEkfLSSAVAV 1122
Cdd:COG0189 87 DPEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGPVVLKPLD--GSGGRGVFLVEDEDA--LESILEA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1123 SKEH---PVVISKFIQEAKEIDVDAVACDGEVIA----IAVSEHVENAGVHSGDATLVTPPQDInqktMERIKMIVHAIG 1195
Cdd:COG0189 163 LTELgsePVLVQEFIPEEDGRDIRVLVVGGEPVAairrIPAEGEFRTNLARGGRAEPVELTDEE----RELALRAAPALG 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 822092823 1196 qeLQVTGpfnLQLIAKDDQLKVIECNVRVsrSFPYVSKTLGVDLVALATRVIL 1248
Cdd:COG0189 239 --LDFAG---VDLIEDDDGPLVLEVNVTP--GFRGLERATGVDIAEAIADYLE 284
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
522-717 |
7.27e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 50.87 E-value: 7.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 522 EKMEEINEHVAP-SEAAM-SVEQAVAAAERLGYPVLVRSAFALGGLGSGFANNRDEMITLVTQAFAHTS------QVLVD 593
Cdd:PRK05586 121 EIMIKAGVPVVPgSEGEIeNEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEEELIKAFNTAKSEAKaafgddSMYIE 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 594 KSLKGWKEIEYEVVRDAYDNCVTV----CNMENidplgiHTGESIVVAPSQTLNDYEYNMLRNTAIKVIRHLGVVGECNI 669
Cdd:PRK05586 201 KFIENPKHIEFQILGDNYGNVVHLgerdCSLQR------RNQKVLEEAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTI 274
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 822092823 670 QYALNpESEQYYIIEVNARLSRSSALASKATGYPLAYVAAKLSLGIPL 717
Cdd:PRK05586 275 EFLLD-KDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEKL 321
|
|
| ATPgrasp_Ter |
pfam15632 |
ATP-grasp in the biosynthetic pathway with Ter operon; This ATP-grasp family is related to ... |
1139-1256 |
1.01e-05 |
|
ATP-grasp in the biosynthetic pathway with Ter operon; This ATP-grasp family is related to carbamoyl phosphate synthetase. These genes are found in the biosynthetic operon associated with the Ter stress response operon and are predicted to be involved in the biosynthesis of a ribo-nucleoside involved in stress response.
Pssm-ID: 434824 [Multi-domain] Cd Length: 131 Bit Score: 47.22 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1139 EIDVDAVACDGEVIAIavsehVENAGVHSGDATLVTPPQDINqktmerikmIVHAIGQELQVTGPFNLQLIAKDDQLKVI 1218
Cdd:pfam15632 15 EYSVDCLAGHGELIAA-----VPRRKGDGGIQTLEDDPELIE---------AARRLAEAFGLDGLFNVQFRYDGDGPKLL 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 822092823 1219 ECNVRVSRSFPYVSKTlGVDLVALATRVILGEEVEAVG 1256
Cdd:pfam15632 81 EINPRMSGGIGYSCLA-GVNLPYLALKLLLGLETPDPV 117
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
539-689 |
1.53e-05 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 49.80 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 539 SVEQAVAAAERLGYPVLVRSAFALGGLGSGFANNRDEMITLV--TQAFAHTS----QVLVDKSLKGWKEIEYEVVRDAYD 612
Cdd:PRK08591 140 DEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELEKAFsmARAEAKAAfgnpGVYMEKYLENPRHIEIQVLADGHG 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 613 NcvtvcnmenidplGIHTGE---SI------VV--APSQTLNDYEYNMLRNTAIKVIRHLGVVGECNIQYaLNPESEQYY 681
Cdd:PRK08591 220 N-------------AIHLGErdcSLqrrhqkVLeeAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEF-LYEKNGEFY 285
|
....*...
gi 822092823 682 IIEVNARL 689
Cdd:PRK08591 286 FIEMNTRI 293
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
1470-1518 |
1.59e-05 |
|
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase superfamily. The family includes Adenine deaminase EC:3.5.4.2 that hydrolyses adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilization as a purine and also as a nitrogen source. This family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases, EC:3.5.1.25 These enzymes catalyze the reaction N-acetyl-D-glucosamine 6-phosphate + H2O <=> D-glucosamine 6-phosphate + acetate. This family includes the catalytic domain of urease alpha subunit. Dihydroorotases (EC:3.5.2.3) are also included.
Pssm-ID: 460401 [Multi-domain] Cd Length: 334 Bit Score: 49.42 E-value: 1.59e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 822092823 1470 LPGLIDVHVHLR--------EPGATHKEDFSSGTAAALAGGITMVCAMPNTNPAIID 1518
Cdd:pfam01979 3 LPGLIDAHVHLEmgllrgipVPPEFAYEALRLGITTMLKSGTTTVLDMGATTSTGIE 59
|
|
| DHOase |
cd01294 |
Dihydroorotase (DHOase) catalyzes the reversible interconversion of carbamoyl aspartate to ... |
1468-1784 |
1.89e-05 |
|
Dihydroorotase (DHOase) catalyzes the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in the pyrimidine biosynthesis. In contrast to the large polyfunctional CAD proteins of higher organisms, this group of DHOases is monofunctional and mainly dimeric.
Pssm-ID: 238619 Cd Length: 335 Bit Score: 49.20 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1468 IRLPGLIDVHVHLREpGATHKedFSSGTAAAlAGGITMVcaMPNTNPAIIDpNSFTMAQK--LAKA--GCRCDY--ALFV 1541
Cdd:cd01294 1 LTIPRPDDMHLHLRD-GAMLK--LVLPYTAR-GFSRAIV--MPNLKPPVTT-TADALAYRerILAAdpGPNFTPlmTLYL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1542 GASSDNAALLPSIASST-AGLKMYLND--TYSTLKMDNVSLWMEHFEKWPKH-LPIVAHAEKQTVAAILL---------V 1608
Cdd:cd01294 74 TENTTPEELREAKKKGGiRGVKLYPAGatTNSQGGVTDLEKIYPVLEAMQKLgMPLLVHGEVPDFKIDVLdreakfipvL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1609 AQLYQR-P---VHICHVAKKEEILIIRAAKQKgiqVTCEVAPHHLFLCEDNVpVIGKDKAQV--RPMLGTREDMEALwen 1682
Cdd:cd01294 154 EPLAQRfPklkIVLEHITTADAVEYVKSCNEN---VAATITPHHLLLTRDDL-LGGGLNPHLycKPVAKRPEDREAL--- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1683 LDIIDC------FATDHAPHSAEEKISEKPPPGYPGLETMLPLLFTAVSE-GRLtvDDIIKRLYENPRKIFSLPAQEDTY 1755
Cdd:cd01294 227 RKAATSghpkffLGSDSAPHPKSNKESSCGCAGIFSAPIALPYLAEVFEEhNAL--DKLEAFASDNGPNFYGLPPNKKTI 304
|
330 340
....*....|....*....|....*....
gi 822092823 1756 VEVdlEQEWIIPKHMQFTKSKWTPFEGMK 1784
Cdd:cd01294 305 TLV--KEPWKVPEKIPFGNNGVVPFRAGE 331
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1035-1253 |
5.13e-05 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 48.17 E-value: 5.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1035 QQCRI--LGTSPEFIDNAENRFKFSRMLDTIGIS-QPRWK-ELSDTESAVNFCETVGYPCLVRPSYVLSGAAMNVAYSDT 1110
Cdd:PRK05586 96 KECNIvfIGPDSETIELMGNKSNAREIMIKAGVPvVPGSEgEIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1111 DMEKFLSSAVAVSK----EHPVVISKFIQEAKEIDVDAVAcdgeviaiavsehvENAG--VHSG--DATLvtppQDINQK 1182
Cdd:PRK05586 176 ELIKAFNTAKSEAKaafgDDSMYIEKFIENPKHIEFQILG--------------DNYGnvVHLGerDCSL----QRRNQK 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1183 TME-----------RIKMIVHAIGQELQV------TGPFnlqLIAKDDQLKVIECNVRVSRSFPYVSKTLGVDLVALATR 1245
Cdd:PRK05586 238 VLEeapspvmteelRKKMGEIAVKAAKAVnyknagTIEF---LLDKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIK 314
|
....*...
gi 822092823 1246 VILGEEVE 1253
Cdd:PRK05586 315 IAYGEKLS 322
|
|
| PLN02889 |
PLN02889 |
oxo-acid-lyase/anthranilate synthase |
214-404 |
5.77e-05 |
|
oxo-acid-lyase/anthranilate synthase
Pssm-ID: 215481 [Multi-domain] Cd Length: 918 Bit Score: 48.31 E-value: 5.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 214 DSNDFDGLFISNGPGNPE------YCKETVENIRKVacvenpkPIFGICLGHQLLSLVIGAKTYKMKYGNRGHNQPCIHK 287
Cdd:PLN02889 128 EEKAFDNIVISPGPGSPTcpadigICLRLLLECRDI-------PILGVCLGHQALGYVHGARIVHAPEPVHGRLSEIEHN 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 288 GtSRCY--ITS-QNHGFAV--------DPETLPKD-----W--------------------------------DVLFTNA 319
Cdd:PLN02889 201 G-CRLFddIPSgRNSGFKVvryhslviDAESLPKElvpiaWtsssdtlsflesqksglvpdayesqigqsgssDPFSSKL 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 320 NDQTS---------------EGIVHNHKPLFSVQFHPEHMAgPTDLVGLFDVFLDTVRDVKENKAGKSVKQRLMEHLTFP 384
Cdd:PLN02889 280 KNGTSwpsshsermqngkilMGIMHSTRPHYGLQFHPESIA-TCYGRQIFKNFREITQDYWLRLRSTSLRRRNSNLTANM 358
|
250 260
....*....|....*....|
gi 822092823 385 GSPDPNAFVRPRKVLVLGSG 404
Cdd:PLN02889 359 QVPDASQLFKVPRRGQLGNG 378
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
1043-1247 |
7.83e-05 |
|
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione synthetases, contains at least three different alpha-L-glutamate ligases. One is RimK, as in E. coli, which adds additional Glu residues to the native Glu-Glu C-terminus of ribosomal protein S6, but not to Lys-Glu mutants. Most species with a member of this subfamily lack an S6 homolog ending in Glu-Glu, however. Members in Methanococcus jannaschii act instead as a tetrahydromethanopterin:alpha-l-glutamate ligase (MJ0620) and a gamma-F420-2:alpha-l-glutamate ligase (MJ1001).
Pssm-ID: 273261 [Multi-domain] Cd Length: 276 Bit Score: 46.96 E-value: 7.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1043 SPEFIDNAENRFKFSRMLDTIGISQPRWKELSDTESAVNFCETVGYPCLVRPSyVLSGAAMNVAYSDTDMEKFLSSAVAV 1122
Cdd:TIGR00768 79 SSDAILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEEIGFPVVLKPV-FGSWGRGVSLARDRQAAESLLEHFEQ 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1123 SKEHPVV--ISKFIQEAKEIDVDAVACDGEVIA----IAVSEHVENagVHSGDATL---VTPPQ-DINQKTMERIKMIVH 1192
Cdd:TIGR00768 158 LNGPQNLflVQEYIKKPGGRDIRVFVVGDEVVAaiyrITSGHWRSN--LARGGKAEpcsLTEEIeELAIKAAKALGLDVA 235
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 822092823 1193 AIgqelqvtgpfnlQLIAKDDQLKVIECNVRVsrSFPYVSKTLGVDLVALATRVI 1247
Cdd:TIGR00768 236 GV------------DLLESEDGLLVNEVNANP--EFKNSVKTTGVNIAGKLLDYI 276
|
|
| PRK14570 |
PRK14570 |
D-alanyl-alanine synthetase A; Provisional |
1081-1141 |
8.52e-05 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173034 [Multi-domain] Cd Length: 364 Bit Score: 47.13 E-value: 8.52e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 822092823 1081 NFCETVGYPCLVRPSYVLSGAAMNVAYSDTDMEKFLSSAVAVskEHPVVISKFIqEAKEID 1141
Cdd:PRK14570 165 DIKEVLGYPVIVKPAVLGSSIGINVAYNENQIEKCIEEAFKY--DLTVVIEKFI-EAREIE 222
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
522-704 |
9.06e-05 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 47.50 E-value: 9.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 522 EKMEEINEHvapseaamsveqavaaAERLGYPVLVRSAFALGGLGSGFANNRDEMI------TLVTQAFAHTSQVLVDKS 595
Cdd:PRK08463 139 ESMEEIKIF----------------ARKIGYPVILKASGGGGGRGIRVVHKEEDLEnafescKREALAYFNNDEVFMEKY 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 596 LKGWKEIEYEVVRDAYDNCVTVCnmENIDPLGIHTGESIVVAPSQTLNDYEYNMLRNTAIKVIRHLGVVGECNIQYALNp 675
Cdd:PRK08463 203 VVNPRHIEFQILGDNYGNIIHLC--ERDCSIQRRHQKVIEIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLD- 279
|
170 180
....*....|....*....|....*....
gi 822092823 676 ESEQYYIIEVNARLSRSSALASKATGYPL 704
Cdd:PRK08463 280 DYNRFYFMEMNTRIQVEHGVTEEITGIDL 308
|
|
| PRK08250 |
PRK08250 |
glutamine amidotransferase; Provisional |
212-269 |
1.24e-04 |
|
glutamine amidotransferase; Provisional
Pssm-ID: 181323 [Multi-domain] Cd Length: 235 Bit Score: 45.73 E-value: 1.24e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 822092823 212 PLDSNDFDGLFISNGPGNP----EYC-----KETVENIRKvaCVENPKPIFGICLGHQLLSLVIGAK 269
Cdd:PRK08250 40 PENADGFDLLIVMGGPQSPrttrEECpyfdsKAEQRLINQ--AIKAGKAVIGVCLGAQLIGEALGAK 104
|
|
| guaA |
PRK00074 |
GMP synthase; Reviewed |
251-342 |
2.32e-04 |
|
GMP synthase; Reviewed
Pssm-ID: 234614 [Multi-domain] Cd Length: 511 Bit Score: 46.19 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 251 PIFGICLGHQLLSLVIGAK---TYKMKYGN---RGHNQPCIHKGTSRCYITSQNHGFAVdpETLPKDWDVLFTNANDQTS 324
Cdd:PRK00074 77 PVLGICYGMQLMAHQLGGKverAGKREYGRaelEVDNDSPLFKGLPEEQDVWMSHGDKV--TELPEGFKVIASTENCPIA 154
|
90
....*....|....*...
gi 822092823 325 eGIVHNHKPLFSVQFHPE 342
Cdd:PRK00074 155 -AIANEERKFYGVQFHPE 171
|
|
| GATase1_PfpI_1 |
cd03169 |
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ... |
200-262 |
1.86e-03 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus; Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus. PfpI is an ATP-independent intracellular proteases which may hydrolyze small peptides to provide a nutritional source. Only Cys of the catalytic triad typical of GATase1 domains is conserved in this group. This Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.
Pssm-ID: 153243 [Multi-domain] Cd Length: 180 Bit Score: 41.48 E-value: 1.86e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 822092823 200 RGARVTV-VPWDQpLDSNDFDGLFISNGPGnPEYC---KETVENIRKVAcvENPKPIFGICLGHQLL 262
Cdd:cd03169 59 PGHRFAVtADFDE-VDPDDYDALVIPGGRA-PEYLrldEKVLAIVRHFA--EANKPVAAICHGPQIL 121
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
1063-1158 |
2.31e-03 |
|
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).
Pssm-ID: 429483 [Multi-domain] Cd Length: 204 Bit Score: 41.53 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 1063 IGISQPRWKELSDtESAVNFCETVGYPCLVRPSYVLSGAAMNVAYSDTDMEKFLssAVAVSKEHPVVISKFIqEAKEIDV 1142
Cdd:pfam07478 13 VTFTRADWKLNPK-EWCAQVEEALGYPVFVKPARLGSSVGVSKVESREELQAAI--EEAFQYDEKVLVEEGI-EGREIEC 88
|
90
....*....|....*.
gi 822092823 1143 dAVACDGEVIAIAVSE 1158
Cdd:pfam07478 89 -AVLGNEDPEVSPVGE 103
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
539-688 |
3.40e-03 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 42.76 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 539 SVEQAVAAAERLGYPVLVRSAFALGGLGSGFANNRDEMITLVTQAF--AHTS----QVLVDKSLKGWKEIEYEVVRDAYD 612
Cdd:COG1038 143 DLEEALAFAEEIGYPVMLKAAAGGGGRGMRVVRSEEELEEAFESARreAKAAfgddEVFLEKYIERPKHIEVQILGDKHG 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 613 NCVtvcnmenidplgiHTGE---SI------VV--APSQTLNDYEYNMLRNTAIKVIRHLGVVGecniqyA-----LNPE 676
Cdd:COG1038 223 NIV-------------HLFErdcSVqrrhqkVVeiAPAPNLDEELREAICEAAVKLAKAVGYVN------AgtvefLVDD 283
|
170
....*....|..
gi 822092823 677 SEQYYIIEVNAR 688
Cdd:COG1038 284 DGNFYFIEVNPR 295
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1073-1146 |
4.61e-03 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 41.89 E-value: 4.61e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 822092823 1073 LSDTESAVNFCETVGYPCLVRPSYVLSGAAMNVAYSDTDMEKFLSSA--VAVS--KEHPVVISKFIQEAKEIDVDAVA 1146
Cdd:PRK08654 138 IEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRVVYSEEELEDAIESTqsIAQSafGDSTVFIEKYLEKPRHIEIQILA 215
|
|
| PfpI |
TIGR01382 |
intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has ... |
187-262 |
5.98e-03 |
|
intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has been solved to 2 Angstrom resolution. It is an ATP-independent intracellular protease that crystallizes as a hexameric ring. Cys-101 is proposed as the active site residue in a catalytic triad with the adjacent His-102 and a Glu residue from an adjacent monomer. A member of this family from Bacillus subtilis, GSP18, has been shown to be expressed in response to several forms of stress. A role in the degradation of small peptides has been suggested. A closely related family consists of the thiamine biosynthesis protein ThiJ and its homologs. [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 273591 [Multi-domain] Cd Length: 166 Bit Score: 39.71 E-value: 5.98e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 822092823 187 CGIKYNqirCLCQRGARVTVVPWDQPLDSNDFDGLFISNGPGnPEYCKETVENIRKV-ACVENPKPIFGICLGHQLL 262
Cdd:TIGR01382 33 SKEAGT---TVGKHGYSVTVDATIDEVNPEEYDALVIPGGRA-PEYLRLNNKAVRLVrEFVEKGKPVAAICHGPQLL 105
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
397-603 |
6.01e-03 |
|
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, General function prediction only]; D-alanine-D-alanine ligase or related ATP-grasp enzyme is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440794 [Multi-domain] Cd Length: 303 Bit Score: 41.25 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 397 KVLVLgSGGLSigqaGEFD---YSGSQAIKAMKEENIQTILInpniatvqtskgladkvyflPITPEYVTQVIKNERPDG 473
Cdd:COG1181 2 RVAVL-FGGRS----AEREvslKSGRAVAAALDKAGYDVVPI--------------------GIDVEDLPAALKELKPDV 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 474 VLL----TFGGQTALncgvelkkQGVLEKYKVRVLGTPVASIEMTED----RKIFveKMEEINehVAPSEAAMSVEQAVA 545
Cdd:COG1181 57 VFPalhgRGGEDGTI--------QGLLELLGIPYTGSGVLASALAMDkaltKRVL--AAAGLP--TPPYVVLRRGELADL 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 822092823 546 AA--ERLGYPVLVRSAFAlgglGSGF----ANNRDEMITLVTQAFAHTSQVLVDKSLKGwKEIE 603
Cdd:COG1181 125 EAieEELGLPLFVKPARE----GSSVgvskVKNAEELAAALEEAFKYDDKVLVEEFIDG-REVT 183
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
531-598 |
8.47e-03 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 40.48 E-value: 8.47e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822092823 531 VAPSEAAMSVEQAVAAAERLGYPVLVRSafALGG--LGSGFANNRDEMITLVTQAFAHTSQVLVDKSLKG 598
Cdd:PRK01372 113 TPPWIVLTREEDLLAAIDKLGLPLVVKP--AREGssVGVSKVKEEDELQAALELAFKYDDEVLVEKYIKG 180
|
|
| GATase1_PfpI_like |
cd03134 |
A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus ... |
213-262 |
9.70e-03 |
|
A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus furiosus; A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus furiosus. This group includes proteins similar to PfpI from P. furiosus. and PH1704 from Pyrococcus horikoshii. These enzymes are ATP-independent intracellular proteases and may hydrolyze small peptides to provide a nutritional source. Only Cys of the catalytic triad typical of GATase1 domains is conserved in this group. This Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For PH1704, it is believed that this Cys together with a different His in one monomer and Glu (from an adjacent monomer) forms a different catalytic triad from the typical GATase1domain. PfpI is homooligomeric. Protease activity is only found for oligomeric forms of PH1704.
Pssm-ID: 153228 [Multi-domain] Cd Length: 165 Bit Score: 39.06 E-value: 9.70e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 822092823 213 LDSNDFDGLFIsngPG--NPEY---CKETVENIRKVAcvENPKPIFGICLGHQLL 262
Cdd:cd03134 58 VDADDYDALVI---PGgtNPDKlrrDPDAVAFVRAFA--EAGKPVAAICHGPWVL 107
|
|
| |
