|
Name |
Accession |
Description |
Interval |
E-value |
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
1-1115 |
0e+00 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 1830.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 1 MPKRNDIKSVMVIGSGPIVIGQAAEFDYSGTQACRVLREEGIRVILVNSNPATIMTDPEMADATYIEPIATPILERIIAK 80
Cdd:PRK05294 1 MPKRTDIKKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 81 ERPDALLPTLGGQTALNAAVALGEAGVLKKYNVELIGASLEAIDRGEDRESFKEVVEAAGAESARSDIAHTLEEVDAIAE 160
Cdd:PRK05294 81 ERPDAILPTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 161 RFGFPLVVRPSFTMGGLGSGIAHNTEELHRIAGAGIHYSPTDEVLIEEGIEGWKEYELELMRDRNDNVVVVCPIENVDPV 240
Cdd:PRK05294 161 EIGYPVIIRPSFTLGGTGGGIAYNEEELEEIVERGLDLSPVTEVLIEESLLGWKEYEYEVMRDKNDNCIIVCSIENIDPM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 241 GVHTGDSITVAPVFTLTDREYQKLRDIGIAIIRGVGVDTGGCNIQFAMHPATGRIIVIEMNPRVSRSSALASKATGFPIA 320
Cdd:PRK05294 241 GVHTGDSITVAPAQTLTDKEYQMLRDASIAIIREIGVETGGCNVQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPIA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 321 KIATKLALGYTLDEIQNDITKSTPASFEPTIDYVVTKVPRFAFEKFPGADPTLTTSMKSVGEAMALAGNFQESLGKAMRS 400
Cdd:PRK05294 321 KVAAKLAVGYTLDEIKNDITGKTPASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALRS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 401 IDKRDMGFswSGEKPGEQEVAELLEAMKVPTEHRYLQIMRAIWGGATEEQIFASTKIDPWFVKQFMLINDTAMQVRD-AE 479
Cdd:PRK05294 401 LEIGVTGL--DEDLFEEESLEELREELKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELKEnGL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 480 TLSPRLLKKAKLAGLSDLQIARLRGLgdaGENTVRELRWNYGLHPVYKTVDTCAAEFDAVTPYYYSCYADESELRKRDRE 559
Cdd:PRK05294 479 PLDAELLREAKRLGFSDARIAKLLGV---TEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYEEECESNPSDRK 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 560 AVIILGSGPNRIGQGIEFDYTCVHAVQELgKDC--DTIMVNCNPETVSTDYDMSDRLYFEPLTFEDVIEIYEAEKKmgpi 637
Cdd:PRK05294 556 KVLVLGSGPNRIGQGIEFDYCCVHAVLAL-REAgyETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKP---- 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 638 KGVIVQLGGQTPLSLAARLKAAGVPILGTTPESIDLAENRELFGEVLRAEKLNAPRFGTALSLEEALDAAHSIGYPVLVR 717
Cdd:PRK05294 631 KGVIVQFGGQTPLKLAKALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPVLVR 710
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 718 PSYVLGGRGMEIVYDDAQLEKYVNRALNeakadtvVSGRlpSPLLIDKFLQDAIEIDVDALFDGDELYIGGIMEHIEEAG 797
Cdd:PRK05294 711 PSYVLGGRAMEIVYDEEELERYMREAVK-------VSPD--HPVLIDKFLEGAIEVDVDAICDGEDVLIGGIMEHIEEAG 781
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 798 VHSGDAACTLPPSTLSDDQIRRLREATYAIAKGCGVCGLINVQYAFMANTLYVIEANPRASRTVPFASKATGVALAKAAA 877
Cdd:PRK05294 782 VHSGDSACSLPPQTLSEEIIEEIREYTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKIAA 861
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 878 RIMAGETIAQQRANGLLLPHGdggdvrlgqqVAIKESVLPFKRFRtpvgkTVDILLGPEMRSTGEVMGFDRDFPHAFAKS 957
Cdd:PRK05294 862 RVMLGKKLAELGYTKGLIPPY----------VAVKEAVFPFNKFP-----GVDPLLGPEMKSTGEVMGIDRTFGEAFAKA 926
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 958 QLSAYEgGLPTSGNVFISVNDTDKRQLPLFAVRLVELGFQIWATEGTASVLRRYGIESKIVDKItarvdsdpdapvqidk 1037
Cdd:PRK05294 927 QLAAGN-RLPTSGTVFLSVRDRDKEEVVELAKRLLELGFKILATSGTAKFLREAGIPVELVNKV---------------- 989
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 651883668 1038 AEGSvgKNVVELIEEGTIDLILNTPNSRGSRSDGYSIRAAAIAADVPQFTTMTEFSAVLLAIEAVKANDYQVMSIQEH 1115
Cdd:PRK05294 990 HEGR--PHIVDLIKNGEIDLVINTPTGRQAIRDGFSIRRAALEYKVPYITTLAGARAAVKAIEALKFGELEVRSLQEY 1065
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
2-1099 |
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: 1444.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 2 PKRNDIKSVMVIGSGPIVIGQAAEFDYSGTQACRVLREEGIRVILVNSNPATIMTDPEMADATYIEPIATPILERIIAKE 81
Cdd:TIGR01369 1 PKRTDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 82 RPDALLPTLGGQTALNAAVALGEAGVLKKYNVELIGASLEAIDRGEDRESFKEVVEAAGAESARSDIAHTLEEVDAIAER 161
Cdd:TIGR01369 81 RPDAILPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 162 FGFPLVVRPSFTMGGLGSGIAHNTEELHRIAGAGIHYSPTDEVLIEEGIEGWKEYELELMRDRNDNVVVVCPIENVDPVG 241
Cdd:TIGR01369 161 IGYPVIVRPAFTLGGTGGGIAYNREELKEIAERALSASPINQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPMG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 242 VHTGDSITVAPVFTLTDREYQKLRDIGIAIIRGVGVDtGGCNIQFAMHPATGRIIVIEMNPRVSRSSALASKATGFPIAK 321
Cdd:TIGR01369 241 VHTGDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIE-GGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 322 IATKLALGYTLDEIQNDITKSTPASFEPTIDYVVTKVPRFAFEKFPGADPTLTTSMKSVGEAMALAGNFQESLGKAMRSI 401
Cdd:TIGR01369 320 VAAKLAVGYTLDELKNPVTGTTPASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 402 DKRDMGFSWSGEKPGEQEvaELLEAMKVPTEHRYLQIMRAIWGGATEEQIFASTKIDPWFVKQFMLINDTAMQVRD--AE 479
Cdd:TIGR01369 400 EIGATGFDLPDREVEPDE--DLWRALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEvkLT 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 480 TLSPRLLKKAKLAGLSDLQIARLRGLGDAgenTVRELRWNYGLHPVYKTVDTCAAEFDAVTPYYYSCYADES-ELRKRDR 558
Cdd:TIGR01369 478 DLDPELLRRAKKLGFSDAQIARLIGVTEA---EVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERdDVPFTDK 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 559 EAVIILGSGPNRIGQGIEFDYTCVHAVQELGKDCD-TIMVNCNPETVSTDYDMSDRLYFEPLTFEDVIEIYEAEKkmgpI 637
Cdd:TIGR01369 555 KKVLVLGSGPNRIGQGVEFDYCCVHAVLALRELGYeTIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEK----P 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 638 KGVIVQLGGQTPLSLAARLKAAGVPILGTTPESIDLAENRELFGEVLRAEKLNAPRFGTALSLEEALDAAHSIGYPVLVR 717
Cdd:TIGR01369 631 EGVIVQFGGQTPLNLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVR 710
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 718 PSYVLGGRGMEIVYDDAQLEKYVNRALNeakadtvVSGrlPSPLLIDKFLQDAIEIDVDALFDGDELYIGGIMEHIEEAG 797
Cdd:TIGR01369 711 PSYVLGGRAMEIVYNEEELRRYLEEAVA-------VSP--EHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEEAG 781
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 798 VHSGDAACTLPPSTLSDDQIRRLREATYAIAKGCGVCGLINVQYAFMANTLYVIEANPRASRTVPFASKATGVALAKAAA 877
Cdd:TIGR01369 782 VHSGDSTCVLPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAV 861
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 878 RIMAGETIAQQranGLLLPHGDGGdvrlgqqVAIKESVLPFKRFRtpvgkTVDILLGPEMRSTGEVMGFDRDFPHAFAKS 957
Cdd:TIGR01369 862 RVMLGKKLEEL---GVGKEKEPKY-------VAVKEPVFSFSKLA-----GVDPVLGPEMKSTGEVMGIGRDLAEAFLKA 926
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 958 QLSAYEgGLPTSGNVFISVNDTDKRQLPLFAVRLVELGFQIWATEGTASVLRRYGIESKIVDKITARvdsdpdapvqidk 1037
Cdd:TIGR01369 927 QLSSGN-RIPKKGSVLLSVRDKDKEELLDLARKLAEKGYKLYATEGTAKFLGEAGIKPELVLKVSEG------------- 992
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 651883668 1038 aegsvGKNVVELIEEGTIDLILNTP-NSRGSRSDGYSIRAAAIAADVPQFTTMTEFSAVLLAI 1099
Cdd:TIGR01369 993 -----RPNILDLIKNGEIELVINTTsKGAGTATDGYKIRREALDYGVPLITTLNTAEAFAEAL 1050
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
1-1118 |
0e+00 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 1371.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 1 MPKRNDIKSVMVIGSGPIVIGQAAEFDYSGTQACRVLREEGIRVILVNSNPATIMTDPEMADATYIEPIATPILERIIAK 80
Cdd:PRK12815 1 MPKDTDIQKILVIGSGPIVIGQAAEFDYSGTQACLALKEEGYQVVLVNPNPATIMTDPAPADTVYFEPLTVEFVKRIIAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 81 ERPDALLPTLGGQTALNAAVALGEAGVLKKYNVELIGASLEAIDRGEDRESFKEVVEAAGAESARSDIAHTLEEVDAIAE 160
Cdd:PRK12815 81 EKPDALLATLGGQTALNLAVKLHEDGILEQYGVELLGTNIEAIQKGEDRERFRALMKELGEPVPESEIVTSVEEALAFAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 161 RFGFPLVVRPSFTMGGLGSGIAHNTEELHRIAGAGIHYSPTDEVLIEEGIEGWKEYELELMRDRNDNVVVVCPIENVDPV 240
Cdd:PRK12815 161 KIGFPIIVRPAYTLGGTGGGIAENLEELEQLFKQGLQASPIHQCLLEESIAGWKEIEYEVMRDRNGNCITVCNMENIDPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 241 GVHTGDSITVAPVFTLTDREYQKLRDIGIAIIRGVGVdTGGCNIQFAMHPATGRIIVIEMNPRVSRSSALASKATGFPIA 320
Cdd:PRK12815 241 GIHTGDSIVVAPSQTLTDDEYQMLRSASLKIISALGV-VGGCNIQFALDPKSKQYYLIEVNPRVSRSSALASKATGYPIA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 321 KIATKLALGYTLDEIQNDITKSTPASFEPTIDYVVTKVPRFAFEKFPGADPTLTTSMKSVGEAMALAGNFQESLGKAMRS 400
Cdd:PRK12815 320 KIAAKLAVGYTLNELKNPVTGLTYASFEPALDYVVVKFPRWPFDKFGYADRTLGTQMKATGEVMAIGRNFESAFQKALRS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 401 IDKRDMGFSwSGEKPGEQEVAELLEAMKVPTEHRYLQIMRAIWGGATEEQIFASTKIDPWFVKQFMLINDTAMQVR-DAE 479
Cdd:PRK12815 400 LEIKRNGLS-LPIELSGKSDEELLQDLRHPDDRRLFALLEALRRGITYEEIHELTKIDPFFLQKFEHIVALEKKLAeDGL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 480 TLSPRLLKKAKLAGLSDLQIARLRGLgdaGENTVRELRWNYGLHPVYKTVDTCAAEFDAVTPYYYSCYADESELRK-RDR 558
Cdd:PRK12815 479 DLSADLLRKVKEKGFSDALLAELTGV---TEEEVRALRKKLGIRPSYKMVDTCAAEFEAKTPYYYSTYFGESEAEPsSEK 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 559 EAVIILGSGPNRIGQGIEFDYTCVHAVQELGK-DCDTIMVNCNPETVSTDYDMSDRLYFEPLTFEDVIEIYEAEKkmgpI 637
Cdd:PRK12815 556 KKVLILGSGPIRIGQGIEFDYSSVHAAFALKKeGYETIMINNNPETVSTDYDTADRLYFEPLTLEDVLNVAEAEN----I 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 638 KGVIVQLGGQTPLSLAARLKAAGVPILGTTPESIDLAENRELFGEVLRAEKLNAPRFGTALSLEEALDAAHSIGYPVLVR 717
Cdd:PRK12815 632 KGVIVQFGGQTAINLAKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEEEAFAFAKRIGYPVLIR 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 718 PSYVLGGRGMEIVYDDAQLEKYvnraLNEAKAdtvvsgrLPSPLLIDKFLqDAIEIDVDALFDGDELYIGGIMEHIEEAG 797
Cdd:PRK12815 712 PSYVIGGQGMAVVYDEPALEAY----LAENAS-------QLYPILIDQFI-DGKEYEVDAISDGEDVTIPGIIEHIEQAG 779
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 798 VHSGDAACTLPPSTLSDDQIRRLREATYAIAKGCGVCGLINVQYAFMANTLYVIEANPRASRTVPFASKATGVALAKAAA 877
Cdd:PRK12815 780 VHSGDSIAVLPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVLANDEIYVLEVNPRASRTVPFVSKATGVPLAKLAT 859
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 878 RIMAGETIAQQRANGLLLPHGDggdvrlgqQVAIKESVLPFKRFRtpvgkTVDILLGPEMRSTGEVMGFDRDFPHAFAKS 957
Cdd:PRK12815 860 KVLLGKSLAELGYPNGLWPGSP--------FIHVKMPVFSYLKYP-----GVDNTLGPEMKSTGEVMGIDKDLEEALYKG 926
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 958 QlSAYEGGLPTSGNVFISVNDTDKRQLPLFAVRLVELGFQIWATEGTASVLRRYGIESKIVDKITarvdsdpdapvqidk 1037
Cdd:PRK12815 927 Y-EASDLHIPSYGTIFISVRDEDKPEVTKLARRFAQLGFKLLATEGTANWLAEEGITTGVVEKVQ--------------- 990
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 1038 aEGSvgKNVVELIEEGTIDLILNTPNSRGSRSDGYSIRAAAIAADVPQFTTMTEFSAVLLAIEAVKANDYQVMSIQEHAR 1117
Cdd:PRK12815 991 -EGS--PSLLERIKQHRIVLVVNTSLSDSASEDAIKIRDEALSTHIPVFTELETAQAFLQVLESLALTTQPIQELQEKHK 1067
|
.
gi 651883668 1118 E 1118
Cdd:PRK12815 1068 Q 1068
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
3-1114 |
0e+00 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 1269.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 3 KRNDIKSVMVIGSGPIVIGQAAEFDYSGTQACRVLREEGIRVILVNSNPATIMTDPEMADATYIEPIATPILERIIAKER 82
Cdd:PLN02735 19 KRTDLKKIMILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATIMTDPETADRTYIAPMTPELVEQVIAKER 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 83 PDALLPTLGGQTALNAAVALGEAGVLKKYNVELIGASLEAIDRGEDRESFKEVVEAAGAESARSDIAHTLEEVDAIAERF 162
Cdd:PLN02735 99 PDALLPTMGGQTALNLAVALAESGILEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPPSGIATTLDECFEIAEDI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 163 G-FPLVVRPSFTMGGLGSGIAHNTEELHRIAGAGIHYSPTDEVLIEEGIEGWKEYELELMRDRNDNVVVVCPIENVDPVG 241
Cdd:PLN02735 179 GeFPLIIRPAFTLGGTGGGIAYNKEEFETICKAGLAASITSQVLVEKSLLGWKEYELEVMRDLADNVVIICSIENIDPMG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 242 VHTGDSITVAPVFTLTDREYQKLRDIGIAIIRGVGVDTGGCNIQFAMHPATGRIIVIEMNPRVSRSSALASKATGFPIAK 321
Cdd:PLN02735 259 VHTGDSITVAPAQTLTDKEYQRLRDYSVAIIREIGVECGGSNVQFAVNPVDGEVMIIEMNPRVSRSSALASKATGFPIAK 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 322 IATKLALGYTLDEIQNDITKSTPASFEPTIDYVVTKVPRFAFEKFPGADPTLTTSMKSVGEAMALAGNFQESLGKAMRSI 401
Cdd:PLN02735 339 MAAKLSVGYTLDQIPNDITLKTPASFEPSIDYVVTKIPRFAFEKFPGSQPILTTQMKSVGEAMALGRTFQESFQKALRSL 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 402 dkrDMGFS-WSGEKPGEQE--VAELLEAMKVPTEHRYLQIMRAIWGGATEEQIFASTKIDPWFVKQFMLINDTA--MQVR 476
Cdd:PLN02735 419 ---ETGFSgWGCAKVKELDwdWEQLKYKLRVPNPDRIHAIYAAMKKGMTVDEIHELTFIDPWFLTQLKELVDVEqfLKSR 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 477 DAETLSPRLLKKAKLAGLSDLQIARLRGlgdAGENTVRELRWNYGLHPVYKTVDTCAAEFDAVTPYYYSCYADESELRKR 556
Cdd:PLN02735 496 SLSELSKDDFYEVKRRGFSDKQIAFATK---STEKEVRSKRLSLGVTPSYKRVDTCAAEFEANTPYMYSSYDGECESAPT 572
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 557 DREAVIILGSGPNRIGQGIEFDYTCVHAVQELGK-DCDTIMVNCNPETVSTDYDMSDRLYFEPLTFEDVIEIYEAEKKmg 635
Cdd:PLN02735 573 NKKKVLILGGGPNRIGQGIEFDYCCCHASFALQDaGYETIMMNSNPETVSTDYDTSDRLYFEPLTVEDVLNVIDLERP-- 650
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 636 piKGVIVQLGGQTPLSLAARLK----------AAG---VPILGTTPESIDLAENRELFGEVLRAEKLNAPRFGTALSLEE 702
Cdd:PLN02735 651 --DGIIVQFGGQTPLKLALPIQkyldknpppsASGngnVKIWGTSPDSIDAAEDRERFNAILNELKIEQPKGGIARSEAD 728
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 703 ALDAAHSIGYPVLVRPSYVLGGRGMEIVYDDAQLEKYVNRALNeakadtVVSGRlpsPLLIDKFLQDAIEIDVDALFDGD 782
Cdd:PLN02735 729 ALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDKLKTYLETAVE------VDPER---PVLVDKYLSDATEIDVDALADSE 799
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 783 -ELYIGGIMEHIEEAGVHSGDAACTLPPSTLSDDQIRRLREATYAIAKGCGVCGLINVQYAF-MANTLYVIEANPRASRT 860
Cdd:PLN02735 800 gNVVIGGIMEHIEQAGVHSGDSACSLPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYAItPSGEVYIIEANPRASRT 879
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 861 VPFASKATGVALAKAAARIMAGETIAQQRANGLLLPhgdggdvrlgQQVAIKESVLPFKRFrtpvgKTVDILLGPEMRST 940
Cdd:PLN02735 880 VPFVSKAIGHPLAKYASLVMSGKSLKDLGFTEEVIP----------AHVSVKEAVLPFDKF-----QGCDVLLGPEMRST 944
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 941 GEVMGFDRDFPHAFAKSQLSAYEgGLPTSGNVFISVNDTDKRQLPLFAVRLVELGFQIWATEGTASVLRRYGIESKIVDK 1020
Cdd:PLN02735 945 GEVMGIDYEFSKAFAKAQIAAGQ-RLPLSGTVFISLNDLTKPHLVPIARGFLELGFRIVSTSGTAHFLELAGIPVERVLK 1023
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 1021 ItarvdsdpdapvqidkAEGSvgKNVVELIEEGTIDLILNTPNSRG-SRSDGYSIRAAAIAADVPQFTTMTEFSAVLLAI 1099
Cdd:PLN02735 1024 L----------------HEGR--PHAGDMLANGQIQLMVITSSGDAlDQKDGRQLRRMALAYKVPIITTVAGALATAQAV 1085
|
1130
....*....|....*
gi 651883668 1100 EAVKANDYQVMSIQE 1114
Cdd:PLN02735 1086 KSLKECPIEMIALQD 1100
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
13-566 |
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: 699.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 13 IGSGPIVIGQAAEFDYSGTQACRVLREEGIRVILVNSNPATIMTDPEMADATYIEPIATPILERIIAKERPDALLPTLGG 92
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 93 QTALNAAVALGEAGVLKkyNVELIGASLEAIDRGEDRESFKEVVEAAGAESARSDIAHTLEEVDAIAERFGFPLVVRPSF 172
Cdd:COG0458 81 QTALNLAVELEEAGILE--GVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 173 TMGGLGSGIAHNTEELHRIAGAGIHYSPTDEVLIEEGIEGWKEYELELMRDRNDNVVVVCPIENVDPVGVHTGDSITVAP 252
Cdd:COG0458 159 VLGGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRDGEDNVIIVGIMEHIEPAGVHSGDSICVAP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 253 VFTLTDREYQKLRDIGIAIIRGVGVDtGGCNIQFAMHpaTGRIIVIEMNPRVSRSSALASKATGFPIAKIATKLALGYTL 332
Cdd:COG0458 239 PQTLSDKEYQRLRDATLKIARALGVV-GLCNIQFAVD--DGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 333 DEIQNDiTKstpasFEPTIDYVVTKVPRFAFEKFPGADPTLTTSMKSVGEAMALAGNFQESLGKAMRSIDKRDMGFSWSG 412
Cdd:COG0458 316 DELGND-TG-----FEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGTVLLS 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 413 EKPGEQEVAELLEAmkvPTEHRYLQIMRAIWGGATEEQIFASTKIDPWFVKQFMLINDTAMQVRDaETLSPRLLKKAKLA 492
Cdd:COG0458 390 LVADDDKEEALLLA---RRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDEIELEE-IILVINTLLGAKSL 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 651883668 493 GLSDLQIARLRglgDAGENTVRELRWNYGLHPVYKTVDTCAAEFDAVTPYYYSCYADESELRKRDREAVIILGS 566
Cdd:COG0458 466 GDSDGIIRRAL---AAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYYYSTYEYENESEETEEPKVVVIGS 536
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
564-1116 |
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: 653.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 564 LGSGPNRIGQGIEFDYTCVHAVQELGKD-CDTIMVNCNPETVSTDYDMSDRLYFEPLTFEDVIEIYEAEKkmgpIKGVIV 642
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEgYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEK----PDGVIV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 643 QLGGQTPLSLAARLKAA----GVPILGTTPESIDLAENRELFGEVLRAEKLNAPRFGTALSLEEALDAAHSIGYPVLVRP 718
Cdd:COG0458 77 QFGGQTALNLAVELEEAgileGVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 719 SYVLGGRGMEIVYDDAQLEKYVNRALNeakadtvVSGRlpSPLLIDKFLQDAIEIDVDALFDG-DELYIGGIMEHIEEAG 797
Cdd:COG0458 157 SYVLGGRGMGIVYNEEELEEYLERALK-------VSPD--HPVLIDESLLGAKEIEVDVVRDGeDNVIIVGIMEHIEPAG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 798 VHSGDAACTLPPSTLSDDQIRRLREATYAIAKGCGVCGLINVQYAFMANTLYVIEANPRASRTVPFASKATGVALAKAAA 877
Cdd:COG0458 228 VHSGDSICVAPPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGRVYVIEVNPRASRSSPFASKATGYPIAKIAA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 878 RIMAGETIAQQRANGLLLPHGDggdvrlgqQVAIKESVLPFKRFrtpvgKTVDILLGPEMRSTGEVMGFDRDFPHAFAKS 957
Cdd:COG0458 308 KLALGYTLDELGNDTGFEPTLD--------YVVVKEPVFPFEKF-----PGVDPVLGPEMKSTGEVMGIGRTFEEALQKA 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 958 QLSAyEGGLPtsGNVFIS-VNDTDKRQLPLFAVRLVELGFQIWATEGTASVLRRYGIESKIVDKITarvdsdpdapvqid 1036
Cdd:COG0458 375 LRSL-EIGLP--GTVLLSlVADDDKEEALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLS-------------- 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 1037 kaEGSvgKNVVELIEEGTIDLILNTPNSRGSRSDGYSIRAAAIAADVPQFTTMTEFSAVLLAIEAVKANDYQVMSIQEHA 1116
Cdd:COG0458 438 --EGR--PIIVDEIELEEIILVINTLLGAKSLGDSDGIIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYY 513
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
128-333 |
1.04e-71 |
|
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: 237.59 E-value: 1.04e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 128 DRESFKEVVEAAGAESARSDIA--HTLEEVDAIAERFGFPLVVRPSFTMGGLGSGIAHNTEELHRIAGAGIHYSPT---- 201
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGpvETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAafgn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 202 DEVLIEEGIEGWKEYELELMRDRNDNVVVVCPIENVDPVgvHTGDSITVAPVFTLTDREYQKLRDIGIAIIRGVGVdTGG 281
Cdd:pfam02786 81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGY-VGA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 651883668 282 CNIQFAMHPATGRIIVIEMNPRVSRSSALASKATGFPIAKIATKLALGYTLD 333
Cdd:pfam02786 158 GTVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| CPSase_L_D3 |
smart01096 |
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ... |
423-547 |
1.54e-43 |
|
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: 154.14 E-value: 1.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 423 LLEAMKVPTEHRYLQIMRAIWGGATEEQIFASTKIDPWFVKQFMLINDTAMQVRD--AETLSPRLLKKAKLAGLSDLQIA 500
Cdd:smart01096 1 LLEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKggLDELDADLLRKAKRLGFSDRQIA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 651883668 501 RLRGLGdagENTVRELRWNYGLHPVYKTVDTCAAEFDAVTPYYYSCY 547
Cdd:smart01096 81 KLLGVT---EAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
695-885 |
2.90e-37 |
|
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: 139.36 E-value: 2.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 695 GTALSLEEALDAAHSIGYPVLVRPSYVLGGRGMEIVYDDAQLEKYVNRALNEAKADTVVSGrlpspLLIDKFLQDAIEID 774
Cdd:pfam02786 22 GPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGNPQ-----VLVEKSLKGPKHIE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 775 VDALFDG-DELYIGGIMEHIEEagVHSGDAACTLPPSTLSDDQIRRLREATYAIAKGCGVCGLINVQYAF--MANTLYVI 851
Cdd:pfam02786 97 YQVLRDAhGNCITVCNRECSDQ--RRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVEFALdpFSGEYYFI 174
|
170 180 190
....*....|....*....|....*....|....
gi 651883668 852 EANPRASRTVPFASKATGVALAKAAARIMAGETI 885
Cdd:pfam02786 175 EMNTRLQVEHALAEKATGYDLAKEAAKIALGYPL 208
|
|
| MGS_CPS_II |
cd01424 |
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate ... |
970-1096 |
2.34e-36 |
|
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: 132.99 E-value: 2.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 970 GNVFISVNDTDKRQLPLFAVRLVELGFQIWATEGTASVLRRYGIESKIVDKItarvdsdpdapvqidkAEGSvgKNVVEL 1049
Cdd:cd01424 1 GTVFISVADRDKPEAVEIAKRLAELGFKLVATEGTAKYLQEAGIPVEVVNKV----------------SEGR--PNIVDL 62
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 651883668 1050 IEEGTIDLILNTPNSRGSRSDGYSIRAAAIAADVPQFTTMTEFSAVL 1096
Cdd:cd01424 63 IKNGEIQLVINTPSGKRAIRDGFSIRRAALEYKVPYFTTLDTARAAV 109
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
74-329 |
6.38e-27 |
|
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: 111.12 E-value: 6.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 74 LERIIAKERPDALLptlggqtALNAAVALGEAGVLKKYNveLIGASLEAIDRGEDRESFKEVVEAAGAESARSDIAHTLE 153
Cdd:COG0439 9 AAELARETGIDAVL-------SESEFAVETAAELAEELG--LPGPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 154 EVDAIAERFGFPLVVRPSFTMGGLGSGIAHNTEEL----HRIAGAGIHYSPTDEVLIEEGIEGwKEYELE-LMRDRNdnv 228
Cdd:COG0439 80 EALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELeaalAEARAEAKAGSPNGEVLVEEFLEG-REYSVEgLVRDGE--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 229 VVVCPI---ENVDPVGVHTGDsitVAPVFtLTDREYQKLRDIGIAIIRGVGVDTGGCNIQFAMHPAtGRIIVIEMNPRVS 305
Cdd:COG0439 156 VVVCSItrkHQKPPYFVELGH---EAPSP-LPEELRAEIGELVARALRALGYRRGAFHTEFLLTPD-GEPYLIEINARLG 230
|
250 260
....*....|....*....|....*.
gi 651883668 306 --RSSALASKATGFPIAKIATKLALG 329
Cdd:COG0439 231 geHIPPLTELATGVDLVREQIRLALG 256
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
622-883 |
1.45e-26 |
|
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: 110.35 E-value: 1.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 622 EDVIEIYEAEKKMGPIKGVIVqlGGQTPLSLAARL-KAAGVPilGTTPESIDLAENRELFGEVLRAEKLNAPRFGTALSL 700
Cdd:COG0439 3 DAIIAAAAELARETGIDAVLS--ESEFAVETAAELaEELGLP--GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 701 EEALDAAHSIGYPVLVRPSYVLGGRGMEIVYDDAQLEKYVNRALNEAKAdtvvsGRLPSPLLIDKFLqDAIEIDVDALFD 780
Cdd:COG0439 79 EEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKA-----GSPNGEVLVEEFL-EGREYSVEGLVR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 781 GDELYIGGIMEHIEEA--GVHSGDAActlpPSTLSDDQIRRLREATYAIAKGCGV-CGLINVQYAFMAN-TLYVIEANPR 856
Cdd:COG0439 153 DGEVVVCSITRKHQKPpyFVELGHEA----PSPLPEELRAEIGELVARALRALGYrRGAFHTEFLLTPDgEPYLIEINAR 228
|
250 260
....*....|....*....|....*....
gi 651883668 857 AS--RTVPFASKATGVALAKAAARIMAGE 883
Cdd:COG0439 229 LGgeHIPPLTELATGVDLVREQIRLALGE 257
|
|
| CPSase_L_D3 |
pfam02787 |
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate ... |
425-502 |
7.21e-20 |
|
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: 84.74 E-value: 7.21e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 651883668 425 EAMKVPTEHRYLQIMRAIWGGATEEQIFASTKIDPWFVKQFMLINDTAMQVRDA-ETLSPRLLKKAKLAGLSDLQIARL 502
Cdd:pfam02787 1 EELRTPTDERLFAIAEALRRGYSVEEIHELTKIDPWFLDKIKNIVELEKELKEAgLDLDAELLREAKRLGFSDRQIAKL 79
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
17-329 |
4.39e-19 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 90.76 E-value: 4.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 17 PIVIGqaaeFDYSGTQACRVLREEGIRVILVNSNPATIMT------------DPEMADATYIEpiatpILERIIAKERPD 84
Cdd:COG3919 8 VVVLG----GDINALAVARSLGEAGVRVIVVDRDPLGPAArsryvdevvvvpDPGDDPEAFVD-----ALLELAERHGPD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 85 ALLPTlgGQTALNAAVALGEAgvLKKYnVELIGASLEAIDRGEDRESFKEVVEAAGAESARSDIAHTLEEVDAIAERFGF 164
Cdd:COG3919 79 VLIPT--GDEYVELLSRHRDE--LEEH-YRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSADDLDALAEDLGF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 165 PLVVRPS--------FTMGGLGSGIAHNTEEL----HRIAGAGIhysptdEVLIEEGIEGWKEYE--LELMRDRNDNVVV 230
Cdd:COG3919 154 PVVVKPAdsvgydelSFPGKKKVFYVDDREELlallRRIAAAGY------ELIVQEYIPGDDGEMrgLTAYVDRDGEVVA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 231 VCpienvdpVG-VHTGDSITV-APVFTLTdREYQKLRDIGIAIIRGVGVdTGGCNIQFAMHPATGRIIVIEMNPRVSRSS 308
Cdd:COG3919 228 TF-------TGrKLRHYPPAGgNSAARES-VDDPELEEAARRLLEALGY-HGFANVEFKRDPRDGEYKLIEINPRFWRSL 298
|
330 340
....*....|....*....|.
gi 651883668 309 ALASKAtGFPIAKIATKLALG 329
Cdd:COG3919 299 YLATAA-GVNFPYLLYDDAVG 318
|
|
| MGS |
pfam02142 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
987-1087 |
7.81e-18 |
|
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: 79.46 E-value: 7.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 987 FAVRLVELGFQIWATEGTASVLRRYGIESKIVDKITArvDSDPDAPVQIdkaegsvgknvVELIEEGTIDLILNTPNS-R 1065
Cdd:pfam02142 5 LAKALVELGFELLATGGTAKFLREAGIPVTEVVEKTG--EGRPGGRVQI-----------GDLIKNGEIDLVINTLYPfK 71
|
90 100
....*....|....*....|..
gi 651883668 1066 GSRSDGYSIRAAAIAADVPQFT 1087
Cdd:pfam02142 72 ATVHDGYAIRRAAENIDIPGPT 93
|
|
| MGS |
smart00851 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
987-1087 |
4.51e-17 |
|
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: 77.13 E-value: 4.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 987 FAVRLVELGFQIWATEGTASVLRRYGIE--SKIVDKITarvdsdpdapvqidkaEGSvgKNVVELIEEGTIDLILNT--P 1062
Cdd:smart00851 5 FAKRLAELGFELLATGGTAKFLREAGLPvvKTLHPKVH----------------GGI--PQILDLIKNGEIDLVINTlyP 66
|
90 100
....*....|....*....|....*
gi 651883668 1063 NSRGSRSDGYSIRAAAIAADVPQFT 1087
Cdd:smart00851 67 FEAQAHEDGYSIRRAAENIDIPGPT 91
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
653-883 |
6.24e-17 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 85.19 E-value: 6.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 653 AARLKAAGVPILGTTPESI----DLAENRELfgevlrAEKLNAPRF----GTALSLEEALDAAHSIGYPVLVRPSYVLGG 724
Cdd:PRK12833 95 AEAVEAAGLIFVGPDAQTIrtmgDKARARRT------ARRAGVPTVpgsdGVVASLDAALEVAARIGYPLMIKAAAGGGG 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 725 RGMEIVYDDAQLEKYVNRALNEAKADTVVSGrlpspLLIDKFLQDAIEIDVDALFDGdelyiggimehieEAGVHSGDAA 804
Cdd:PRK12833 169 RGIRVAHDAAQLAAELPLAQREAQAAFGDGG-----VYLERFIARARHIEVQILGDG-------------ERVVHLFERE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 805 CTL-----------PPSTLSDDQIRRLREATYAIAKGCGVCGLINVQYAFMANT--LYVIEANPRASRTVPFASKATGVA 871
Cdd:PRK12833 231 CSLqrrrqkileeaPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDDARgeFYFIEMNTRIQVEHPVTEAITGID 310
|
250
....*....|..
gi 651883668 872 LAKAAARIMAGE 883
Cdd:PRK12833 311 LVQEMLRIADGE 322
|
|
| MGS_CPS_I_III |
cd01423 |
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases ... |
971-1100 |
1.32e-13 |
|
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: 68.10 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 971 NVFISVNDTDKRQLPLFAVRLVELGFQIWATEGTASVLRRYGIESKIVDKITArvDSDPDAPVQidkaegsvgknvVELI 1050
Cdd:cd01423 2 GILISIGSYSKPELLPTAQKLSKLGYKLYATEGTADFLLENGIPVTPVAWPSE--EPQNDKPSL------------RELL 67
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 651883668 1051 EEGTIDLILNTPNSRGSR--SDGYSIRAAAIAADVPQFttmTEFSAVLLAIE 1100
Cdd:cd01423 68 AEGKIDLVINLPSNRGKRvlDNDYVMRRAADDFAVPLI---TNPKCAKLFIE 116
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
635-888 |
1.52e-13 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 74.29 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 635 GPIKGVIVQLGGQtplsLAAR--LKAAGVPILGTTPESIDlaenrelfgevlraeklnaprfgtalSLEEALDAAHSIGY 712
Cdd:PRK06111 104 GPSADIIAKMGSK----IEARraMQAAGVPVVPGITTNLE--------------------------DAEEAIAIARQIGY 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 713 PVLVRPSYVLGGRGMEIVYDDAQLEKYVnrALNEAKADTVVSGrlpSPLLIDKFLQDA--IEIDVDALFDGDELYIG--- 787
Cdd:PRK06111 154 PVMLKASAGGGGIGMQLVETEQELTKAF--ESNKKRAANFFGN---GEMYIEKYIEDPrhIEIQLLADTHGNTVYLWere 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 788 -GIMEH----IEEAgvhsgdaactlpPSTLSDDQIR-RLREATYAIAKGCGVCGLINVQYAF-MANTLYVIEANPRASRT 860
Cdd:PRK06111 229 cSVQRRhqkvIEEA------------PSPFLDEETRkAMGERAVQAAKAIGYTNAGTIEFLVdEQKNFYFLEMNTRLQVE 296
|
250 260 270
....*....|....*....|....*....|
gi 651883668 861 VPFASKATGVALAKAAARIMAGE--TIAQQ 888
Cdd:PRK06111 297 HPVTEEITGIDLVEQQLRIAAGEklSFTQD 326
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
60-314 |
3.13e-13 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 72.22 E-value: 3.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 60 MADATYIEPIAT-----PILERIIAKERPDALLPTLGGQTALNAAvalgEAGVLKKYNVELIGASLEAIDRGEDRESFKE 134
Cdd:PRK12767 42 FADKFYVVPKVTdpnyiDRLLDICKKEKIDLLIPLIDPELPLLAQ----NRDRFEEIGVKVLVSSKEVIEICNDKWLTYE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 135 VVEAAGAESARSDIAHTLEEVDAI--AERFGFPLVVRPSFTMGGLGSGIAHNTEELHRIagagIHYSPtdEVLIEEGIEG 212
Cdd:PRK12767 118 FLKENGIPTPKSYLPESLEDFKAAlaKGELQFPLFVKPRDGSASIGVFKVNDKEELEFL----LEYVP--NLIIQEFIEG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 213 wKEYELELMRDRNDNVVVVCPIENVDPVGVHTGDSITVapvftltdrEYQKLRDIGIAIIRGVGVDtGGCNIQFAMHPat 292
Cdd:PRK12767 192 -QEYTVDVLCDLNGEVISIVPRKRIEVRAGETSKGVTV---------KDPELFKLAERLAEALGAR-GPLNIQCFVTD-- 258
|
250 260
....*....|....*....|..
gi 651883668 293 GRIIVIEMNPRVSRSSALASKA 314
Cdd:PRK12767 259 GEPYLFEINPRFGGGYPLSYMA 280
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
622-888 |
1.88e-12 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 69.91 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 622 EDVIEIYEAEKkmgpIKGVIVqlGGQTPLSLAA----RLKAAGVPILGTTPESIDLAENRELFGEVLRAEKLNAPRFGTA 697
Cdd:PRK12767 59 DRLLDICKKEK----IDLLIP--LIDPELPLLAqnrdRFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLP 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 698 LSLEEAL--DAAHSIGYPVLVRPSYVLGGRGMEIVYDDAQLEKYVNRALNeakadtvvsgrlpspLLIDKFLQDaIEIDV 775
Cdd:PRK12767 133 ESLEDFKaaLAKGELQFPLFVKPRDGSASIGVFKVNDKEELEFLLEYVPN---------------LIIQEFIEG-QEYTV 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 776 DALFDGDELYIGGI-MEHIEeagVHSG--DAACTLPPSTLsDDQIRRLREATYAIakgcgvcGLINVQYAFMANTLYVIE 852
Cdd:PRK12767 197 DVLCDLNGEVISIVpRKRIE---VRAGetSKGVTVKDPEL-FKLAERLAEALGAR-------GPLNIQCFVTDGEPYLFE 265
|
250 260 270
....*....|....*....|....*....|....*.
gi 651883668 853 ANPRASRTVPFASKAtGVALAKAAARIMAGETIAQQ 888
Cdd:PRK12767 266 INPRFGGGYPLSYMA-GANEPDWIIRNLLGGENEPI 300
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
635-883 |
2.52e-12 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 70.78 E-value: 2.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 635 GPIKGVIVQLGGQtplsLAAR--LKAAGVPILGTTPESIDlaenrelfgevlraeklnaprfgtalSLEEALDAAHSIGY 712
Cdd:PRK08654 104 GPSSDVIEAMGSK----INAKklMKKAGVPVLPGTEEGIE--------------------------DIEEAKEIAEEIGY 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 713 PVLVRPSYVLGGRGMEIVYDDAQLEKYVNRALNEAKA---DTVVsgrlpsplLIDKFLQDA--IEIDVDALFDGDELYIG 787
Cdd:PRK08654 154 PVIIKASAGGGGIGMRVVYSEEELEDAIESTQSIAQSafgDSTV--------FIEKYLEKPrhIEIQILADKHGNVIHLG 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 788 ----GIM-EH---IEEAgvhsgdaactlpPSTLSDDQIR-RLREATYAIAKGCGVCGLINVQYAFMANTLYVIEANPRAS 858
Cdd:PRK08654 226 drecSIQrRHqklIEEA------------PSPIMTPELReRMGEAAVKAAKAINYENAGTVEFLYSNGNFYFLEMNTRLQ 293
|
250 260
....*....|....*....|....*
gi 651883668 859 RTVPFASKATGVALAKAAARIMAGE 883
Cdd:PRK08654 294 VEHPITEMVTGIDIVKEQIKIAAGE 318
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
652-886 |
8.13e-12 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 69.78 E-value: 8.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 652 LAARLKAAGVPILGTTPESIDLAEN----RELfgevlrAEKLNAPRF-GT---ALSLEEALDAAHSIGYPVLVRPSYVLG 723
Cdd:PRK12999 95 FARACAEAGITFIGPTAEVLRLLGDkvaaRNA------AIKAGVPVIpGSegpIDDIEEALEFAEEIGYPIMLKASAGGG 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 724 GRGMEIVYDDAQLEKYVNRALNEAKA----DTVvsgrlpsplLIDKFLQDAIEIDVDALfdGDELyiGGIMeHIEEAgvh 799
Cdd:PRK12999 169 GRGMRIVRSEEELEEAFERAKREAKAafgnDEV---------YLEKYVENPRHIEVQIL--GDKH--GNVV-HLYER--- 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 800 sgDaaCTL-----------PPSTLSDDQIRRLREATYAIAKGCGVCGLINVQyaF---MANTLYVIEANPR--ASRTVpf 863
Cdd:PRK12999 232 --D--CSVqrrhqkvveiaPAPGLSEELRERICEAAVKLARAVGYVNAGTVE--FlvdADGNFYFIEVNPRiqVEHTV-- 303
|
250 260
....*....|....*....|...
gi 651883668 864 ASKATGVALAKAAARIMAGETIA 886
Cdd:PRK12999 304 TEEVTGIDIVQSQILIAEGATLH 326
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
664-886 |
1.21e-11 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 68.20 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 664 LGTTPESIDLAENRELFGEVLRaeKLNAPRF----GTALSLEEALDAAHSIGYPVLVRPSYVLGGRGMEIVYDDAQLEKY 739
Cdd:PRK05586 103 IGPDSETIELMGNKSNAREIMI--KAGVPVVpgseGEIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEEELIKA 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 740 VNRALNEAKA----DTvvsgrlpspLLIDKFLQDAIEIDVDALfdGDELyiGGImehieeagVHSGDAACTL-------- 807
Cdd:PRK05586 181 FNTAKSEAKAafgdDS---------MYIEKFIENPKHIEFQIL--GDNY--GNV--------VHLGERDCSLqrrnqkvl 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 808 ---PPSTLSDDQIRRLREATYAIAKGCGVCGLINVQYAF-MANTLYVIEANPRASRTVPFASKATGVALAKAAARIMAGE 883
Cdd:PRK05586 240 eeaPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLdKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGE 319
|
...
gi 651883668 884 TIA 886
Cdd:PRK05586 320 KLS 322
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
653-886 |
1.76e-11 |
|
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: 68.95 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 653 AARL--KAAGVPILGTTPESIDlaenrelfgevlraeklnaprfgtalSLEEALDAAHSIGYPVLVRPSYVLGGRGMEIV 730
Cdd:COG1038 121 AARAaaIEAGVPVIPGTEGPVD--------------------------DLEEALAFAEEIGYPVMLKAAAGGGGRGMRVV 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 731 YDDAQLEKYVNRALNEAKA----DTVvsgrlpsplLIDKFLQDAIEIDVDALfdGDELyiGGIMeH-------------- 792
Cdd:COG1038 175 RSEEELEEAFESARREAKAafgdDEV---------FLEKYIERPKHIEVQIL--GDKH--GNIV-Hlferdcsvqrrhqk 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 793 -IEEAgvhsgdaactlPPSTLSDDQIRRLREATYAIAKgcgvcgliNVQYA------FM---ANTLYVIEANPR--ASRT 860
Cdd:COG1038 241 vVEIA-----------PAPNLDEELREAICEAAVKLAK--------AVGYVnagtveFLvddDGNFYFIEVNPRiqVEHT 301
|
250 260
....*....|....*....|....*.
gi 651883668 861 VpfASKATGVALAKAAARIMAGETIA 886
Cdd:COG1038 302 V--TEEVTGIDIVQSQILIAEGYSLD 325
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
21-302 |
2.14e-11 |
|
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: 66.28 E-value: 2.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 21 GQAAEFD---YSGTQACRVLREEGIRVILVNSNPATIMTDpemadatyiepiatpileriIAKERPDALLPTLGGqtaln 97
Cdd:COG1181 9 GRSAEREvslKSGRAVAAALDKAGYDVVPIGIDVEDLPAA--------------------LKELKPDVVFPALHG----- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 98 aavALGE----AGVLKKYNVELIGASLEAIDRGEDRESFKEVVEAAGAESARSDI--AHTLEEVDAIAERFGFPLVVRPS 171
Cdd:COG1181 64 ---RGGEdgtiQGLLELLGIPYTGSGVLASALAMDKALTKRVLAAAGLPTPPYVVlrRGELADLEAIEEELGLPLFVKPA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 172 FtmggLGS--GI--AHNTEELHRIAGAGIHYSptDEVLIEEGIEGwKEYELELMrdRNDNVVVVCPIENVDPVGV----- 242
Cdd:COG1181 141 R----EGSsvGVskVKNAEELAAALEEAFKYD--DKVLVEEFIDG-REVTVGVL--GNGGPRALPPIEIVPENGFydyea 211
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 651883668 243 --HTGDSITVAPVfTLTDREYQKLRDIGIAI-----IRGVG-VDtggcniqfAMHPATGRIIVIEMNP 302
Cdd:COG1181 212 kyTDGGTEYICPA-RLPEELEERIQELALKAfralgCRGYArVD--------FRLDEDGEPYLLEVNT 270
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
105-339 |
1.53e-09 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 61.65 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 105 AGVLKKYNVELIGASLEAIDRGEDRESFKEVVEAA------GAESARSDIAHTLEevdaIAERFGFPLVVRPSFTMGGLG 178
Cdd:PRK05586 92 AKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAgvpvvpGSEGEIENEEEALE----IAKEIGYPVMVKASAGGGGRG 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 179 SGIAHNTEELHRIAGAGIHYSPT----DEVLIEEGIEGWKEYELELMRDRNDNVVVVCpiENVDPVGVHTGDSITVAPVF 254
Cdd:PRK05586 168 IRIVRSEEELIKAFNTAKSEAKAafgdDSMYIEKFIENPKHIEFQILGDNYGNVVHLG--ERDCSLQRRNQKVLEEAPSP 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 255 TLTDREYQKLRDIGIAIIRGVGVDTGGcNIQFAMHpATGRIIVIEMNPRVSRSSALASKATGFPIAKIATKLALGYTLDE 334
Cdd:PRK05586 246 VMTEELRKKMGEIAVKAAKAVNYKNAG-TIEFLLD-KDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEKLSI 323
|
....*
gi 651883668 335 IQNDI 339
Cdd:PRK05586 324 KQEDI 328
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
699-883 |
1.57e-09 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 61.74 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 699 SLEEALDAAHSIGYPVLVRPSYVLGGRGMEIVYDDAQLEKYVNRALNEAKA----DTVvsgrlpsplLIDKFLQDAIEID 774
Cdd:PRK08591 140 DEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELEKAFSMARAEAKAafgnPGV---------YMEKYLENPRHIE 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 775 VDALFDGDelyiGGImehieeagVHSGDAACTL-----------PPSTLSDDQIRRLREATYAIAKGCGVCGLINVQYAF 843
Cdd:PRK08591 211 IQVLADGH----GNA--------IHLGERDCSLqrrhqkvleeaPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLY 278
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 651883668 844 MAN-TLYVIEANPRASRTVPFASKATGVALAKAAARIMAGE 883
Cdd:PRK08591 279 EKNgEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGE 319
|
|
| MGS-like |
cd00532 |
MGS-like domain. This domain composes the whole protein of methylglyoxal synthetase, which ... |
972-1095 |
1.98e-09 |
|
MGS-like domain. This domain composes the whole protein of methylglyoxal synthetase, which catalyzes the enolization of dihydroxyacetone phosphate (DHAP) to produce methylglyoxal. The family also includes the C-terminal domain in carbamoyl phosphate synthetase (CPS) where it catalyzes the last phosphorylation of a coaboxyphosphate intermediate to form the product carbamoyl phosphate and may also play a regulatory role. This family also includes inosine monophosphate cyclohydrolase. The known structures in this family show a common phosphate binding site.
Pssm-ID: 238297 [Multi-domain] Cd Length: 112 Bit Score: 56.37 E-value: 1.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 972 VFISVNDTDKRQLPLFAVRLVELGFQIWATEGTASVLRRYGIESKIVDKITArvDSDPdapvqidkaegsvgkNVVELIE 1051
Cdd:cd00532 2 VFLSVSDHVKAMLVDLAPKLSSDGFPLFATGGTSRVLADAGIPVRAVSKRHE--DGEP---------------TVDAAIA 64
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 651883668 1052 E-GTIDLILNTPNSRGSRS---DGYSIRAAAIAADVPQFTTMTEFSAV 1095
Cdd:cd00532 65 EkGKFDVVINLRDPRRDRCtdeDGTALLRLARLYKIPVTTPNATAMFV 112
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
30-340 |
4.85e-09 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 60.00 E-value: 4.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 30 GTQACRVLR---EEGIRVILVNSNPATIMTDPEMADATYiePIATPI-------LERIIA---KERPDALLPTLGgqtAL 96
Cdd:PRK08654 11 GEIAIRVMRacrELGIKTVAVYSEADKNALFVKYADEAY--PIGPAPpsksylnIERIIDvakKAGADAIHPGYG---FL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 97 NAAVALGEAgvLKKYNVELIGASLEAIDRGEDRESFKEVVEAAG------AESARSDIahtlEEVDAIAERFGFPLVVRP 170
Cdd:PRK08654 86 AENPEFAKA--CEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGvpvlpgTEEGIEDI----EEAKEIAEEIGYPVIIKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 171 SFTMGGLGSGIAHNTEEL-------HRIAGAGIHYSptdEVLIEEGIEGWKEYELELMRDRNDNVvvvcpienvdpvgVH 243
Cdd:PRK08654 160 SAGGGGIGMRVVYSEEELedaiestQSIAQSAFGDS---TVFIEKYLEKPRHIEIQILADKHGNV-------------IH 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 244 TGDS-----------ITVAPVFTLTDREYQKLRDIGIAIIRGVGVDTGGcNIQFAMhpATGRIIVIEMNPRVSRSSALAS 312
Cdd:PRK08654 224 LGDRecsiqrrhqklIEEAPSPIMTPELRERMGEAAVKAAKAINYENAG-TVEFLY--SNGNFYFLEMNTRLQVEHPITE 300
|
330 340
....*....|....*....|....*...
gi 651883668 313 KATGFPIAKIATKLALGYTLDEIQNDIT 340
Cdd:PRK08654 301 MVTGIDIVKEQIKIAAGEELSFKQEDIT 328
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
150-302 |
1.30e-07 |
|
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: 53.47 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 150 HTLEEVDAIAERFGFPLVVRPSFTMGGLGSGIAHNTEELHRIAGAGIHYSPTdeVLIEEGIEGwKEYELELMrdRNDNVV 229
Cdd:pfam07478 23 NPKEWCAQVEEALGYPVFVKPARLGSSVGVSKVESREELQAAIEEAFQYDEK--VLVEEGIEG-REIECAVL--GNEDPE 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 651883668 230 VVCPIENVDPVGV---HTGDSITVAPVFT---LTDREYQKLRDIGIAIIRGVGVdTGGCNIQFaMHPATGRIIVIEMNP 302
Cdd:pfam07478 98 VSPVGEIVPSGGFydyEAKYIDDSAQIVVpadLEEEQEEQIQELALKAYKALGC-RGLARVDF-FLTEDGEIVLNEVNT 174
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
620-873 |
1.81e-07 |
|
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: 53.89 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 620 TFEDVIEIYEAEKKMGPIKGVIVQ-LGGQTPLSLAARLKAAGVPILgTTPESIDLAENRELFGEVLRAEKLNAPRFGTAL 698
Cdd:TIGR00768 32 PPAINLTFNEGPRALAELDVVIVRiVSMFRGLAVLRYLESLGVPVI-NSSDAILNAGDKFLSHQLLAKAGIPLPRTGLAG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 699 SLEEALDAAHSIGYPVLVRPSYVLGGRGMEIVYDDAQLEKyVNRALNEAKADTVVsgrlpspLLIDKFLQDAIEIDVDAL 778
Cdd:TIGR00768 111 SPEEALKLIEEIGFPVVLKPVFGSWGRGVSLARDRQAAES-LLEHFEQLNGPQNL-------FLVQEYIKKPGGRDIRVF 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 779 FDGDELyIGGIMEHIEE---AGVHSGDAA--CTLppstlsDDQIRRLR-EATYAIakGCGVCGlinVQYAFMANTLYVIE 852
Cdd:TIGR00768 183 VVGDEV-VAAIYRITSGhwrSNLARGGKAepCSL------TEEIEELAiKAAKAL--GLDVAG---VDLLESEDGLLVNE 250
|
250 260
....*....|....*....|...
gi 651883668 853 ANPrasrTVPF--ASKATGVALA 873
Cdd:TIGR00768 251 VNA----NPEFknSVKTTGVNIA 269
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
634-905 |
2.72e-07 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 54.43 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 634 MGPIKGVIVQLGGQTplslAAR--LKAAGVPILGTTpesidlaenrelfgevlraEKLNAPrfgtalSLEEALDAAHSIG 711
Cdd:PRK08463 102 IGPKSEVIRKMGNKN----IARylMKKNGIPIVPGT-------------------EKLNSE------SMEEIKIFARKIG 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 712 YPVLVRPSYVLGGRGMEIVYDDAQLEKYVNRALNEAKA----DTVvsgrlpsplLIDKFLQDAIEIDVDALFDGdelyIG 787
Cdd:PRK08463 153 YPVILKASGGGGGRGIRVVHKEEDLENAFESCKREALAyfnnDEV---------FMEKYVVNPRHIEFQILGDN----YG 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 788 GImehieeagVHSGDAACTL-----------PPSTLSDDQIRRLREATYAIAKGCGVCGLINVQYAF-MANTLYVIEANP 855
Cdd:PRK08463 220 NI--------IHLCERDCSIqrrhqkvieiaPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLdDYNRFYFMEMNT 291
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 651883668 856 RASRTVPFASKATGVALAKAAARIMAGETIAQQRANglLLPHGDGGDVRL 905
Cdd:PRK08463 292 RIQVEHGVTEEITGIDLIVRQIRIAAGEILDLEQSD--IKPRGFAIEARI 339
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
695-888 |
9.46e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 52.82 E-value: 9.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 695 GTALSLEEALDAAHSIGYPVLVRPSYVLGGRGMEIVYDDAQLEKYVNRALNEAkadtvVSGRLPSPLLIDKFLQDAIEID 774
Cdd:PRK08462 138 GALKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVEDESDLENLYLAAESEA-----LSAFGDGTMYMEKFINNPRHIE 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 775 VDALfdGDELyiGGImehieeagVHSGDAACTL----------PPSTLSDDQIR-RLREATYAIAKGCGVCGLINVQYAF 843
Cdd:PRK08462 213 VQIL--GDKH--GNV--------IHVGERDCSLqrrhqklieeSPAVVLDEKTReRLHETAIKAAKAIGYEGAGTFEFLL 280
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 651883668 844 MAN-TLYVIEANPRASRTVPFASKATGVALAKAAARIMAGETIAQQ 888
Cdd:PRK08462 281 DSNlDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEELPSQ 326
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
651-883 |
1.02e-06 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 52.93 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 651 SLAARLkaaGVPilGTTPESIDLAENRELFGEVLRAEKLNAPRFGTALSLEEALDAAHSIGYPVLVRPSYVLGGRGMEIV 730
Cdd:PRK02186 87 EVARRL---GLP--AANTEAIRTCRDKKRLARTLRDHGIDVPRTHALALRAVALDALDGLTYPVVVKPRMGSGSVGVRLC 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 731 YDDAQLEKYVNRALNEAKADTVVSGRLPSPllidkflqdaiEIDVDALFDGDELYIGGIMEHIEEAGVHSGDAACTLPPS 810
Cdd:PRK02186 162 ASVAEAAAHCAALRRAGTRAALVQAYVEGD-----------EYSVETLTVARGHQVLGITRKHLGPPPHFVEIGHDFPAP 230
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 651883668 811 TLSDDQIRRLREATYAIAKGCGVCGLINVQYAFMANTLYVIEANPR-ASRTVPFA-SKATGVALAKAAARIMAGE 883
Cdd:PRK02186 231 LSAPQRERIVRTVLRALDAVGYAFGPAHTELRVRGDTVVIIEINPRlAGGMIPVLlEEAFGVDLLDHVIDLHLGV 305
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
632-883 |
1.02e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 52.80 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 632 KKMGPIKGVIVQLGGQTplslAAR--LKAAGVPIlgtTPESidlaenrelfgevlraeklnaprFGTALSLEEALDAAHS 709
Cdd:PRK07178 100 KFIGPSAEVIRRMGDKT----EARraMIKAGVPV---TPGS-----------------------EGNLADLDEALAEAER 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 710 IGYPVLVRPSYVLGGRGMEIVYDDAQLEKYVNRALNEAkadTVVSGRlpSPLLIDKFLQDAIEIDVDALFDgdelYIGGI 789
Cdd:PRK07178 150 IGYPVMLKATSGGGGRGIRRCNSREELEQNFPRVISEA---TKAFGS--AEVFLEKCIVNPKHIEVQILAD----SHGNV 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 790 mehieeagVHSGDAACTL-----------PPSTLSDDQIRRLREATYAIAKGCGVCGLINVQYAFMA-NTLYVIEANPRA 857
Cdd:PRK07178 221 --------VHLFERDCSIqrrnqklieiaPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDAdGEVYFMEMNTRV 292
|
250 260
....*....|....*....|....*.
gi 651883668 858 SRTVPFASKATGVALAKAAARIMAGE 883
Cdd:PRK07178 293 QVEHTITEEITGIDIVREQIRIASGL 318
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
1-339 |
1.38e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 52.06 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 1 MPKRndIKSVMVIGSGPIvigqaaefdysgtqACRVLR---EEGIRVILVNSN------PA-----TIMTDPEMADATYI 66
Cdd:PRK12833 1 MPSR--IRKVLVANRGEI--------------AVRIIRaarELGMRTVAACSDadrdslAArmadeAVHIGPSHAAKSYL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 67 EPIAtpilerIIAKER---PDALLPTLGGqTALNAAVA--LGEAGVLkkynveLIGASLEAIDRGEDRESFKEVVEAAGA 141
Cdd:PRK12833 65 NPAA------ILAAARqcgADAIHPGYGF-LSENAAFAeaVEAAGLI------FVGPDAQTIRTMGDKARARRTARRAGV 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 142 ES--ARSDIAHTLEEVDAIAERFGFPLVVRPSFTMGGLGSGIAHNTEELHR---IAGAGIHYSPTD-EVLIEEGIEGWKE 215
Cdd:PRK12833 132 PTvpGSDGVVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQLAAelpLAQREAQAAFGDgGVYLERFIARARH 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 216 YELELMRDRNDnvvVVCPIENVDPVGVHTGDSITVAPVFTLTDREYQKLRDIGIAIIRGVGVDTGGcNIQFAMHPATGRI 295
Cdd:PRK12833 212 IEVQILGDGER---VVHLFERECSLQRRRQKILEEAPSPSLTPAQRDALCASAVRLARQVGYRGAG-TLEYLFDDARGEF 287
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 651883668 296 IVIEMNPRVSRSSALASKATGFPIAKIATKLALGYTLDEIQNDI 339
Cdd:PRK12833 288 YFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEPLRFAQGDI 331
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
683-862 |
2.52e-06 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 50.49 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 683 VLRAEKLNAPRFGTALSLEEALDAAHSIGYPVLVRPsyVLGGR--GMEIVYDDAQLEKYVNRAL---NEAKADTVVSGR- 756
Cdd:PRK01372 105 VWQAAGLPTPPWIVLTREEDLLAAIDKLGLPLVVKP--AREGSsvGVSKVKEEDELQAALELAFkydDEVLVEKYIKGRe 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 757 LPSPLLIDKFLqDAIEIDVDALF-DGDELYIGGIMEHIEEAGvhsgdaactLPPSTLsdDQIRRLREATYAIAkGCGVCG 835
Cdd:PRK01372 183 LTVAVLGGKAL-PVIEIVPAGEFyDYEAKYLAGGTQYICPAG---------LPAEIE--AELQELALKAYRAL-GCRGWG 249
|
170 180 190
....*....|....*....|....*....|
gi 651883668 836 LINvqyaFM---ANTLYVIEANprasrTVP 862
Cdd:PRK01372 250 RVD----FMldeDGKPYLLEVN-----TQP 270
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
83-336 |
2.55e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 51.26 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 83 PDALLPTLGGQTALNAAVALG----------------EAGVLKKYNVELIGASLEAIDRGEDRESFKEVVEAA------G 140
Cdd:PRK07178 53 ADPLAGYLNPRRLVNLAVETGcdalhpgygflsenaeLAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAgvpvtpG 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 141 AESARSDIAHTLEEvdaiAERFGFPLVVRPsfTMGGLGSGI--AHNTEELHR-----IAGAGIHYSPTdEVLIEEGIEGW 213
Cdd:PRK07178 133 SEGNLADLDEALAE----AERIGYPVMLKA--TSGGGGRGIrrCNSREELEQnfprvISEATKAFGSA-EVFLEKCIVNP 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 214 KEYELELMRDRNDNVVVV----CPIENvdpvgvHTGDSITVAPVFTLTDREYQKLRDIGIAIIRGVGVDTGGcNIQFAMh 289
Cdd:PRK07178 206 KHIEVQILADSHGNVVHLferdCSIQR------RNQKLIEIAPSPQLTPEQRAYIGDLAVRAAKAVGYENAG-TVEFLL- 277
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 651883668 290 PATGRIIVIEMNPRVSRSSALASKATGFPIAK----IATKLALGYTLDEIQ 336
Cdd:PRK07178 278 DADGEVYFMEMNTRVQVEHTITEEITGIDIVReqirIASGLPLSYKQEDIQ 328
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
18-339 |
4.48e-06 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 50.58 E-value: 4.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 18 IVIGQAAEFDYSGTQACRVLReegIRVILVNSNPATIMTDPEMADATY---IEPI-----ATPILEriIAKE-RPDALLP 88
Cdd:PRK08463 5 ILIANRGEIAVRVIRACRDLH---IKSVAIYTEPDRECLHVKIADEAYrigTDPIkgyldVKRIVE--IAKAcGADAIHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 89 TLGGQTAlNA--AVALGEAGVLkkynveLIGASLEAIDRGEDRESFKEVVE------AAGAESARSdiaHTLEEVDAIAE 160
Cdd:PRK08463 80 GYGFLSE-NYefAKAVEDAGII------FIGPKSEVIRKMGNKNIARYLMKkngipiVPGTEKLNS---ESMEEIKIFAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 161 RFGFPLVVRPSFTMGGLGSGIAHNTEELHRIAGA----GIHYSPTDEVLIEEGIEGWKEYELELMRDRNDNVVVVCpiEN 236
Cdd:PRK08463 150 KIGYPVILKASGGGGGRGIRVVHKEEDLENAFESckreALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLC--ER 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 237 VDPVGVHTGDSITVAPVFTLTDREYQKLRDIGIAIIRGVGVDTGGcNIQFAMHPaTGRIIVIEMNPRVSRSSALASKATG 316
Cdd:PRK08463 228 DCSIQRRHQKVIEIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAG-TIEFLLDD-YNRFYFMEMNTRIQVEHGVTEEITG 305
|
330 340
....*....|....*....|...
gi 651883668 317 FPIAKIATKLALGYTLDEIQNDI 339
Cdd:PRK08463 306 IDLIVRQIRIAAGEILDLEQSDI 328
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
109-339 |
4.86e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 50.41 E-value: 4.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 109 KKYNVELIGASLEAIDRGEDRESFKEVVEAA------GAESARSDIahtlEEVDAIAERFGFPLVVRPSFTMGGLGSGIA 182
Cdd:PRK06111 96 KEEGIVFIGPSADIIAKMGSKIEARRAMQAAgvpvvpGITTNLEDA----EEAIAIARQIGYPVMLKASAGGGGIGMQLV 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 183 HNTEELhRIAGAGIHYSPTD-----EVLIEEGIEGWKEYELELMRDRNDNVVVV----CPIENvdpvgvHTGDSITVAPV 253
Cdd:PRK06111 172 ETEQEL-TKAFESNKKRAANffgngEMYIEKYIEDPRHIEIQLLADTHGNTVYLwereCSVQR------RHQKVIEEAPS 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 254 FTLTDREYQKLRDIGIAIIRGVGVdTGGCNIQFAMHPAtGRIIVIEMNPRVSRSSALASKATGFPIAKIATKLALGYTLD 333
Cdd:PRK06111 245 PFLDEETRKAMGERAVQAAKAIGY-TNAGTIEFLVDEQ-KNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKLS 322
|
....*.
gi 651883668 334 EIQNDI 339
Cdd:PRK06111 323 FTQDDI 328
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
35-321 |
2.34e-05 |
|
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: 47.63 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 35 RVLREEGIRVILVNsnpatimtdpemADATYIEPIATPILERIIAKERPDALLP-TLGGQTALNAAVALGEAGVLkkynv 113
Cdd:COG0189 21 EAAQRRGHEVEVID------------PDDLTLDLGRAPELYRGEDLSEFDAVLPrIDPPFYGLALLRQLEAAGVP----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 114 eLIGaSLEAIDRGEDRESFKEVVEAAGAESARSDIAHTLEEVDAIAERFGFPLVVRPSFTMGGLGSGIAHNTEELHRIAg 193
Cdd:COG0189 84 -VVN-DPEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDALESIL- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 194 AGIHYSPTDEVLIEEGIEGWKEYELelmrdR----NDNVVVVC---PIENVDPVGVHTGDSITVAPvftLTDREyqklRD 266
Cdd:COG0189 161 EALTELGSEPVLVQEFIPEEDGRDI-----RvlvvGGEPVAAIrriPAEGEFRTNLARGGRAEPVE---LTDEE----RE 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 651883668 267 IGIAIIRGVGVDTGGcnIQFAMHPatGRIIVIEMNPrvsrSSALA--SKATGFPIAK 321
Cdd:COG0189 229 LALRAAPALGLDFAG--VDLIEDD--DGPLVLEVNV----TPGFRglERATGVDIAE 277
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
137-304 |
7.78e-05 |
|
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: 44.55 E-value: 7.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 137 EAAGAESARSDIAHTLEEVDAIAERFGFPLVVRPSfTMG--GLGSGIAHNTEELH---RIAGAGihysptdEVLIEEGIE 211
Cdd:pfam02222 1 QKLGLPTPRFMAAESLEELIEAGQELGYPCVVKAR-RGGydGKGQYVVRSEADLPqawEELGDG-------PVIVEEFVP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 212 gwKEYELELM--RDRNDNVVVVCPIENVDpvgvHTGDSITVAPVFTLTDREYQKLRDIGIAIIR---GVGVdtggcniqF 286
Cdd:pfam02222 73 --FDRELSVLvvRSVDGETAFYPVVETIQ----EDGICRLSVAPARVPQAIQAEAQDIAKRLVDelgGVGV--------F 138
|
170 180
....*....|....*....|.
gi 651883668 287 AMH---PATGRIIVIEMNPRV 304
Cdd:pfam02222 139 GVElfvTEDGDLLINELAPRP 159
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
107-349 |
8.44e-05 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 46.28 E-value: 8.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 107 VLKKYNVELIGASLEAIDRGEDRESFKEVVEAAGAESAR-SDIA-HTLEEVDAIAERFGFPLVVRPSFTMGGLGSGIAHN 184
Cdd:PRK08462 96 ICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPgSDGAlKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVED 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 185 TEELHRiagagIHYSPTDEVL---------IEEGIEGWKEYELELMRDRNDNVVVV----CPIENvdpvgvHTGDSITVA 251
Cdd:PRK08462 176 ESDLEN-----LYLAAESEALsafgdgtmyMEKFINNPRHIEVQILGDKHGNVIHVgerdCSLQR------RHQKLIEES 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 252 PVFTLTDREYQKLRDIGIAIIRGVGVDTGGcNIQFaMHPATGRIIVIEMNPRVSRSSALASKATGFPIAKIATKLALGYT 331
Cdd:PRK08462 245 PAVVLDEKTRERLHETAIKAAKAIGYEGAG-TFEF-LLDSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEE 322
|
250 260
....*....|....*....|....*...
gi 651883668 332 LDE----------IQNDITKSTPASFEP 349
Cdd:PRK08462 323 LPSqesiklkghaIECRITAEDPKKFYP 350
|
|
| ATPgrasp_Ter |
pfam15632 |
ATP-grasp in the biosynthetic pathway with Ter operon; This ATP-grasp family is related to ... |
810-883 |
7.04e-04 |
|
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: 40.67 E-value: 7.04e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 651883668 810 STLSDDQirRLREATYAIAKGCGVCGLINVQYAFMANTLYVIEANPRASRTVPfASKATGVALAKAAARIMAGE 883
Cdd:pfam15632 41 QTLEDDP--ELIEAARRLAEAFGLDGLFNVQFRYDGDGPKLLEINPRMSGGIG-YSCLAGVNLPYLALKLLLGL 111
|
|
| purT |
PRK09288 |
formate-dependent phosphoribosylglycinamide formyltransferase; |
673-750 |
1.08e-03 |
|
formate-dependent phosphoribosylglycinamide formyltransferase;
Pssm-ID: 236454 [Multi-domain] Cd Length: 395 Bit Score: 42.82 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 673 LAENRELfgevLR---AEKLNAP--RFGTALSLEEALDAAHSIGYPVLVRPsyVLG--GRGMEIVYDDAQLEKYVNRALN 745
Cdd:PRK09288 110 LTMNREG----IRrlaAEELGLPtsPYRFADSLEELRAAVEEIGYPCVVKP--VMSssGKGQSVVRSPEDIEKAWEYAQE 183
|
....*
gi 651883668 746 EAKAD 750
Cdd:PRK09288 184 GGRGG 188
|
|
| ATP-grasp_2 |
pfam08442 |
ATP-grasp domain; |
133-264 |
1.14e-03 |
|
ATP-grasp domain;
Pssm-ID: 400651 [Multi-domain] Cd Length: 202 Bit Score: 41.48 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 133 KEVVEAAGAESARSDIAHTLEEVDAIAERFG-FPLVVRPSFTMGGLGSG----IAHNTEELHRIAGA-----------GI 196
Cdd:pfam08442 8 KEIFAKYGIPVPRGEVATSPEEAEEIAKKLGgKVYVVKAQVLAGGRGKAggvkLAKSPEEAKEVAKEmlgknlvtkqtGP 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 651883668 197 HYSPTDEVLIEEGIEGWKEYELELMRDRNDN-VVVVCPIE---NVDPVGVHTGDSI---TVAPVFTLTDREYQKL 264
Cdd:pfam08442 88 DGQPVNKVLVEEALDIKKEYYLSIVLDRASKgPVIIASTEggvDIEEVAAKNPEKIhkfPIDPLKGLTPYQAREI 162
|
|
| PurH |
COG0138 |
AICAR transformylase/IMP cyclohydrolase PurH [Nucleotide transport and metabolism]; AICAR ... |
974-1022 |
3.30e-03 |
|
AICAR transformylase/IMP cyclohydrolase PurH [Nucleotide transport and metabolism]; AICAR transformylase/IMP cyclohydrolase PurH is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439908 Cd Length: 512 Bit Score: 41.55 E-value: 3.30e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 651883668 974 ISVndTDKRQLPLFAVRLVELGFQIWATEGTASVLRRYGIESKIVDKIT 1022
Cdd:COG0138 8 ISV--SDKTGLVEFARALVELGVEIISTGGTAKALREAGIPVTEVSEVT 54
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
672-738 |
5.48e-03 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 40.91 E-value: 5.48e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 651883668 672 DLAENRELFGEVLRAEKLNAPRFGTALSLEEALDAAHSIGYPVLVRPSYVLGGRGMEI-VYDDAQLEK 738
Cdd:PRK14016 210 DIACDKELTKRLLAAAGVPVPEGRVVTSAEDAWEAAEEIGYPVVVKPLDGNHGRGVTVnITTREEIEA 277
|
|
| ddl |
PRK01966 |
D-alanine--D-alanine ligase; |
84-218 |
6.14e-03 |
|
D-alanine--D-alanine ligase;
Pssm-ID: 234993 [Multi-domain] Cd Length: 333 Bit Score: 40.10 E-value: 6.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 84 DALLPTLGGqtalnaavALGE----AGVLKKYNVELIGASLEAIDRGEDRESFKEVVEAAGAESA------RSDIAHTLe 153
Cdd:PRK01966 83 DVVFPVLHG--------PPGEdgtiQGLLELLGIPYVGCGVLASALSMDKILTKRLLAAAGIPVApyvvltRGDWEEAS- 153
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 651883668 154 eVDAIAERFGFPLVVRPSftmgGLGS--GI--AHNTEELHriagAGIH----YSPtdEVLIEEGIEGwKEYEL 218
Cdd:PRK01966 154 -LAEIEAKLGLPVFVKPA----NLGSsvGIskVKNEEELA----AALDlafeYDR--KVLVEQGIKG-REIEC 214
|
|
| PLN02891 |
PLN02891 |
IMP cyclohydrolase |
951-1022 |
9.60e-03 |
|
IMP cyclohydrolase
Pssm-ID: 178479 [Multi-domain] Cd Length: 547 Bit Score: 39.77 E-value: 9.60e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 651883668 951 PHAFAKSQLSAYEGGLPtsgNVFISVndTDKRQLPLFAVRLVELGFQIWATEGTASVLRRYGIESKIVDKIT 1022
Cdd:PLN02891 7 AARAPAQPQSSPSSGKK---QALISL--SDKTDLALLANGLQELGYTIVSTGGTASALEAAGVSVTKVEELT 73
|
|
|