|
Name |
Accession |
Description |
Interval |
E-value |
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
1-1053 |
0e+00 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 2012.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 1 MPKRTDIQKIMVIGSGPIIIGQAAEFDYAGTQACLSLKEEGYEVVLVNSNPATIMTDKEIADKVYIEPITLEFVTRILRK 80
Cdd:PRK05294 1 MPKRTDIKKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 81 ERPDALLPTLGGQTGLNMAMELSKNGILDELGVELLGTKLSAIDQAEDRDLFKQLMEELNQPIPESEIVNTVEEAVAFAA 160
Cdd:PRK05294 81 ERPDAILPTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 161 TIGYPVIVRPAFTLGGTGGGMCANEEELREIAENGLKLSPVTQCLIERSIAGFKEIEYEVMRDSADNALVVCNMENFDPV 240
Cdd:PRK05294 161 EIGYPVIIRPSFTLGGTGGGIAYNEEELEEIVERGLDLSPVTEVLIEESLLGWKEYEYEVMRDKNDNCIIVCSIENIDPM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 241 GIHTGDSIVFAPAQTMSDYENQMLRDASLSIIRALKIE-GGCNVQLALDPHSFKYYVIEVNPRVSRSSALASKATGYPIA 319
Cdd:PRK05294 241 GVHTGDSITVAPAQTLTDKEYQMLRDASIAIIREIGVEtGGCNVQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPIA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 320 KLAAKIAVGLTLDEVINPVTGSTYAMFEPALDYVVAKIPRFPFDKFEKGERRLGTQMKATGEVMAIGRNIEESLLKACRS 399
Cdd:PRK05294 321 KVAAKLAVGYTLDEIKNDITGKTPASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALRS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 400 LEIGVHHNEMPELASVSDDALIEKVVKAQDDRLFYVSEAIRRGYTPEEIAELTKIDIFYLDKLLHIFEIEQELGAHPQDL 479
Cdd:PRK05294 401 LEIGVTGLDEDLFEEESLEELREELKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELKENGLPL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 480 D--VLKTAKLNGFSDRKIAELWETTADQVRQLRLENKIVPVYKMVDTCAAEFDSETPYFYSTYGWENESIKSDKESVLVL 557
Cdd:PRK05294 481 DaeLLREAKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYEEECESNPSDRKKVLVL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 558 GSGPIRIGQGVEFDYATVHSVKAIQAAGYEAIIMNSNPETVSTDFSVSDKLYFEPLTFEDVMNVIDLEQPKGVIVQFGGQ 637
Cdd:PRK05294 561 GSGPNRIGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKPKGVIVQFGGQ 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 638 TAINLAEPLAKAGVTILGTQVADLDRAEDRDLFEQALKELDIPQPPGQTATNEEEAALAARKIGFPVLVRPSYVLGGRAM 717
Cdd:PRK05294 641 TPLKLAKALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPVLVRPSYVLGGRAM 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 718 EIVENEEDLRSYMRTAVKASPDHPVLVDSYIVG-QECEVDAISDGENVLIPGIMEHIERAGVHSGDSMAVYPPQTLSQKV 796
Cdd:PRK05294 721 EIVYDEEELERYMREAVKVSPDHPVLIDKFLEGaIEVDVDAICDGEDVLIGGIMEHIEEAGVHSGDSACSLPPQTLSEEI 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 797 QETIADYTKRLAIGLNCLGMMNIQFVIKDEKVYVIEVNPRASRTVPFLSKVTNIPMAQVATKLILGQKLEELGYQDGLYP 876
Cdd:PRK05294 801 IEEIREYTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKIAARVMLGKKLAELGYTKGLIP 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 877 EStrVHIKAPVFSFTKLAKVDSLLGPEMKSTGEVMGSDTTLEKALYKAFEASYLHLPTFGNVVFTIADDAKEEALDLARR 956
Cdd:PRK05294 881 PY--VAVKEAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKAQLAAGNRLPTSGTVFLSVRDRDKEEVVELAKR 958
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 957 FQNIGYGILATEGTAAFFASHGLQSQPVGKIGDDDKDIPSFVRKGRIQAIINTvGTKRTADEDGEQIRRSAIEHGVPLFT 1036
Cdd:PRK05294 959 LLELGFKILATSGTAKFLREAGIPVELVNKVHEGRPHIVDLIKNGEIDLVINT-PTGRQAIRDGFSIRRAALEYKVPYIT 1037
|
1050
....*....|....*..
gi 447049177 1037 AIDTANAMLKVLESRSF 1053
Cdd:PRK05294 1038 TLAGARAAVKAIEALKF 1054
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
2-1048 |
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: 1652.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 2 PKRTDIQKIMVIGSGPIIIGQAAEFDYAGTQACLSLKEEGYEVVLVNSNPATIMTDKEIADKVYIEPITLEFVTRILRKE 81
Cdd:TIGR01369 1 PKRTDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 82 RPDALLPTLGGQTGLNMAMELSKNGILDELGVELLGTKLSAIDQAEDRDLFKQLMEELNQPIPESEIVNTVEEAVAFAAT 161
Cdd:TIGR01369 81 RPDAILPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 162 IGYPVIVRPAFTLGGTGGGMCANEEELREIAENGLKLSPVTQCLIERSIAGFKEIEYEVMRDSADNALVVCNMENFDPVG 241
Cdd:TIGR01369 161 IGYPVIVRPAFTLGGTGGGIAYNREELKEIAERALSASPINQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPMG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 242 IHTGDSIVFAPAQTMSDYENQMLRDASLSIIRALKIEGGCNVQLALDPHSFKYYVIEVNPRVSRSSALASKATGYPIAKL 321
Cdd:TIGR01369 241 VHTGDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 322 AAKIAVGLTLDEVINPVTGSTYAMFEPALDYVVAKIPRFPFDKFEKGERRLGTQMKATGEVMAIGRNIEESLLKACRSLE 401
Cdd:TIGR01369 321 AAKLAVGYTLDELKNPVTGTTPASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSLE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 402 IGVHHNEMPELASVSDDALIEKVVKAQDDRLFYVSEAIRRGYTPEEIAELTKIDIFYLDKLLHIFEIEQEL---GAHPQD 478
Cdd:TIGR01369 401 IGATGFDLPDREVEPDEDLWRALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELeevKLTDLD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 479 LDVLKTAKLNGFSDRKIAELWETTADQVRQLRLENKIVPVYKMVDTCAAEFDSETPYFYSTYGWE-NESIKSDKESVLVL 557
Cdd:TIGR01369 481 PELLRRAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGErDDVPFTDKKKVLVL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 558 GSGPIRIGQGVEFDYATVHSVKAIQAAGYEAIIMNSNPETVSTDFSVSDKLYFEPLTFEDVMNVIDLEQPKGVIVQFGGQ 637
Cdd:TIGR01369 561 GSGPNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQFGGQ 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 638 TAINLAEPLAKAGVTILGTQVADLDRAEDRDLFEQALKELDIPQPPGQTATNEEEAALAARKIGFPVLVRPSYVLGGRAM 717
Cdd:TIGR01369 641 TPLNLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRAM 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 718 EIVENEEDLRSYMRTAVKASPDHPVLVDSYI-VGQECEVDAISDGENVLIPGIMEHIERAGVHSGDSMAVYPPQTLSQKV 796
Cdd:TIGR01369 721 EIVYNEEELRRYLEEAVAVSPEHPVLIDKYLeDAVEVDVDAVSDGEEVLIPGIMEHIEEAGVHSGDSTCVLPPQTLSAEI 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 797 QETIADYTKRLAIGLNCLGMMNIQFVIKDEKVYVIEVNPRASRTVPFLSKVTNIPMAQVATKLILGQKLEELGYqdGLYP 876
Cdd:TIGR01369 801 VDRIKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLEELGV--GKEK 878
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 877 ESTRVHIKAPVFSFTKLAKVDSLLGPEMKSTGEVMGSDTTLEKALYKAFEASYLHLPTFGNVVFTIADDAKEEALDLARR 956
Cdd:TIGR01369 879 EPKYVAVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRIPKKGSVLLSVRDKDKEELLDLARK 958
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 957 FQNIGYGILATEGTAAFFASHGLQSQPVGKIGDDDKDIPSFVRKGRIQAIINTVGTKRTADEDGEQIRRSAIEHGVPLFT 1036
Cdd:TIGR01369 959 LAEKGYKLYATEGTAKFLGEAGIKPELVLKVSEGRPNILDLIKNGEIELVINTTSKGAGTATDGYKIRREALDYGVPLIT 1038
|
1050
....*....|..
gi 447049177 1037 AIDTANAMLKVL 1048
Cdd:TIGR01369 1039 TLNTAEAFAEAL 1050
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
1-1050 |
0e+00 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 1561.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 1 MPKRTDIQKIMVIGSGPIIIGQAAEFDYAGTQACLSLKEEGYEVVLVNSNPATIMTDKEIADKVYIEPITLEFVTRILRK 80
Cdd:PRK12815 1 MPKDTDIQKILVIGSGPIVIGQAAEFDYSGTQACLALKEEGYQVVLVNPNPATIMTDPAPADTVYFEPLTVEFVKRIIAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 81 ERPDALLPTLGGQTGLNMAMELSKNGILDELGVELLGTKLSAIDQAEDRDLFKQLMEELNQPIPESEIVNTVEEAVAFAA 160
Cdd:PRK12815 81 EKPDALLATLGGQTALNLAVKLHEDGILEQYGVELLGTNIEAIQKGEDRERFRALMKELGEPVPESEIVTSVEEALAFAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 161 TIGYPVIVRPAFTLGGTGGGMCANEEELREIAENGLKLSPVTQCLIERSIAGFKEIEYEVMRDSADNALVVCNMENFDPV 240
Cdd:PRK12815 161 KIGFPIIVRPAYTLGGTGGGIAENLEELEQLFKQGLQASPIHQCLLEESIAGWKEIEYEVMRDRNGNCITVCNMENIDPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 241 GIHTGDSIVFAPAQTMSDYENQMLRDASLSIIRALKIEGGCNVQLALDPHSFKYYVIEVNPRVSRSSALASKATGYPIAK 320
Cdd:PRK12815 241 GIHTGDSIVVAPSQTLTDDEYQMLRSASLKIISALGVVGGCNIQFALDPKSKQYYLIEVNPRVSRSSALASKATGYPIAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 321 LAAKIAVGLTLDEVINPVTGSTYAMFEPALDYVVAKIPRFPFDKFEKGERRLGTQMKATGEVMAIGRNIEESLLKACRSL 400
Cdd:PRK12815 321 IAAKLAVGYTLNELKNPVTGLTYASFEPALDYVVVKFPRWPFDKFGYADRTLGTQMKATGEVMAIGRNFESAFQKALRSL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 401 EIGVHHNEMP-ELASVSDDALIEKVVKAQDDRLFYVSEAIRRGYTPEEIAELTKIDIFYLDKLLHIFEIEQELGAHPQDL 479
Cdd:PRK12815 401 EIKRNGLSLPiELSGKSDEELLQDLRHPDDRRLFALLEALRRGITYEEIHELTKIDPFFLQKFEHIVALEKKLAEDGLDL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 480 --DVLKTAKLNGFSDRKIAELWETTADQVRQLRLENKIVPVYKMVDTCAAEFDSETPYFYSTYGWENESIKS-DKESVLV 556
Cdd:PRK12815 481 saDLLRKVKEKGFSDALLAELTGVTEEEVRALRKKLGIRPSYKMVDTCAAEFEAKTPYYYSTYFGESEAEPSsEKKKVLI 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 557 LGSGPIRIGQGVEFDYATVHSVKAIQAAGYEAIIMNSNPETVSTDFSVSDKLYFEPLTFEDVMNVIDLEQPKGVIVQFGG 636
Cdd:PRK12815 561 LGSGPIRIGQGIEFDYSSVHAAFALKKEGYETIMINNNPETVSTDYDTADRLYFEPLTLEDVLNVAEAENIKGVIVQFGG 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 637 QTAINLAEPLAKAGVTILGTQVADLDRAEDRDLFEQALKELDIPQPPGQTATNEEEAALAARKIGFPVLVRPSYVLGGRA 716
Cdd:PRK12815 641 QTAINLAKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEEEAFAFAKRIGYPVLIRPSYVIGGQG 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 717 MEIVENEEDLRSYMRTAvkASPDHPVLVDSYIVGQECEVDAISDGENVLIPGIMEHIERAGVHSGDSMAVYPPQTLSQKV 796
Cdd:PRK12815 721 MAVVYDEPALEAYLAEN--ASQLYPILIDQFIDGKEYEVDAISDGEDVTIPGIIEHIEQAGVHSGDSIAVLPPQSLSEEQ 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 797 QETIADYTKRLAIGLNCLGMMNIQFVIKDEKVYVIEVNPRASRTVPFLSKVTNIPMAQVATKLILGQKLEELGYQDGLYP 876
Cdd:PRK12815 799 QEKIRDYAIKIAKKLGFRGIMNIQFVLANDEIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLGKSLAELGYPNGLWP 878
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 877 ESTRVHIKAPVFSFTKLAKVDSLLGPEMKSTGEVMGSDTTLEKALYKAFEASYLHLPTFGNVVFTIADDAKEEALDLARR 956
Cdd:PRK12815 879 GSPFIHVKMPVFSYLKYPGVDNTLGPEMKSTGEVMGIDKDLEEALYKGYEASDLHIPSYGTIFISVRDEDKPEVTKLARR 958
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 957 FQNIGYGILATEGTAAFFASHGLQSQPVGKIGDDDKDIPSfVRKGRIQAIINTVGTKRTADEDGEQIRRSAIEHGVPLFT 1036
Cdd:PRK12815 959 FAQLGFKLLATEGTANWLAEEGITTGVVEKVQEGSPSLLE-RIKQHRIVLVVNTSLSDSASEDAIKIRDEALSTHIPVFT 1037
|
1050
....*....|....
gi 447049177 1037 AIDTANAMLKVLES 1050
Cdd:PRK12815 1038 ELETAQAFLQVLES 1051
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
3-1050 |
0e+00 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 1177.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 3 KRTDIQKIMVIGSGPIIIGQAAEFDYAGTQACLSLKEEGYEVVLVNSNPATIMTDKEIADKVYIEPITLEFVTRILRKER 82
Cdd:PLN02735 19 KRTDLKKIMILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATIMTDPETADRTYIAPMTPELVEQVIAKER 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 83 PDALLPTLGGQTGLNMAMELSKNGILDELGVELLGTKLSAIDQAEDRDLFKQLMEELNQPIPESEIVNTVEEAVAFAATI 162
Cdd:PLN02735 99 PDALLPTMGGQTALNLAVALAESGILEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPPSGIATTLDECFEIAEDI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 163 G-YPVIVRPAFTLGGTGGGMCANEEELREIAENGLKLSPVTQCLIERSIAGFKEIEYEVMRDSADNALVVCNMENFDPVG 241
Cdd:PLN02735 179 GeFPLIIRPAFTLGGTGGGIAYNKEEFETICKAGLAASITSQVLVEKSLLGWKEYELEVMRDLADNVVIICSIENIDPMG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 242 IHTGDSIVFAPAQTMSDYENQMLRDASLSIIRALKIE-GGCNVQLALDPHSFKYYVIEVNPRVSRSSALASKATGYPIAK 320
Cdd:PLN02735 259 VHTGDSITVAPAQTLTDKEYQRLRDYSVAIIREIGVEcGGSNVQFAVNPVDGEVMIIEMNPRVSRSSALASKATGFPIAK 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 321 LAAKIAVGLTLDEVINPVTGSTYAMFEPALDYVVAKIPRFPFDKFEKGERRLGTQMKATGEVMAIGRNIEESLLKACRSL 400
Cdd:PLN02735 339 MAAKLSVGYTLDQIPNDITLKTPASFEPSIDYVVTKIPRFAFEKFPGSQPILTTQMKSVGEAMALGRTFQESFQKALRSL 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 401 EIGVHHNEMPELASVSDD--ALIEKVVKAQDDRLFYVSEAIRRGYTPEEIAELTKIDIFYLDKLLHIFEIEQELGAHP-Q 477
Cdd:PLN02735 419 ETGFSGWGCAKVKELDWDweQLKYKLRVPNPDRIHAIYAAMKKGMTVDEIHELTFIDPWFLTQLKELVDVEQFLKSRSlS 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 478 DL--DVLKTAKLNGFSDRKIAELWETTADQVRQLRLENKIVPVYKMVDTCAAEFDSETPYFYSTYGWENESIKSDKESVL 555
Cdd:PLN02735 499 ELskDDFYEVKRRGFSDKQIAFATKSTEKEVRSKRLSLGVTPSYKRVDTCAAEFEANTPYMYSSYDGECESAPTNKKKVL 578
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 556 VLGSGPIRIGQGVEFDYATVHSVKAIQAAGYEAIIMNSNPETVSTDFSVSDKLYFEPLTFEDVMNVIDLEQPKGVIVQFG 635
Cdd:PLN02735 579 ILGGGPNRIGQGIEFDYCCCHASFALQDAGYETIMMNSNPETVSTDYDTSDRLYFEPLTVEDVLNVIDLERPDGIIVQFG 658
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 636 GQTAINLAEPLAKA-------------GVTILGTQVADLDRAEDRDLFEQALKELDIPQPPGQTATNEEEAALAARKIGF 702
Cdd:PLN02735 659 GQTPLKLALPIQKYldknpppsasgngNVKIWGTSPDSIDAAEDRERFNAILNELKIEQPKGGIARSEADALAIAKRIGY 738
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 703 PVLVRPSYVLGGRAMEIVENEEDLRSYMRTAVKASPDHPVLVDSYIV-GQECEVDAISDGE-NVLIPGIMEHIERAGVHS 780
Cdd:PLN02735 739 PVVVRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDPERPVLVDKYLSdATEIDVDALADSEgNVVIGGIMEHIEQAGVHS 818
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 781 GDSMAVYPPQTLSQKVQETIADYTKRLAIGLNCLGMMNIQF-VIKDEKVYVIEVNPRASRTVPFLSKVTNIPMAQVATKL 859
Cdd:PLN02735 819 GDSACSLPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYaITPSGEVYIIEANPRASRTVPFVSKAIGHPLAKYASLV 898
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 860 ILGQKLEELGYQDGLYPEstRVHIKAPVFSFTKLAKVDSLLGPEMKSTGEVMGSDTTLEKALYKAFEASYLHLPTFGNVV 939
Cdd:PLN02735 899 MSGKSLKDLGFTEEVIPA--HVSVKEAVLPFDKFQGCDVLLGPEMRSTGEVMGIDYEFSKAFAKAQIAAGQRLPLSGTVF 976
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 940 FTIADDAKEEALDLARRFQNIGYGILATEGTAAFFASHGLQSQPVGKIGDDDKDIPSFVRKGRIQAIINTVGTKRTADED 1019
Cdd:PLN02735 977 ISLNDLTKPHLVPIARGFLELGFRIVSTSGTAHFLELAGIPVERVLKLHEGRPHAGDMLANGQIQLMVITSSGDALDQKD 1056
|
1050 1060 1070
....*....|....*....|....*....|.
gi 447049177 1020 GEQIRRSAIEHGVPLFTAIDTANAMLKVLES 1050
Cdd:PLN02735 1057 GRQLRRMALAYKVPIITTVAGALATAQAVKS 1087
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
13-559 |
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: 786.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 13 IGSGPIIIGQAAEFDYAGTQACLSLKEEGYEVVLVNSNPATIMTDKEIADKVYIEPITLEFVTRILRKERPDALLPTLGG 92
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 93 QTGLNMAMELSKNGILDelGVELLGTKLSAIDQAEDRDLFKQLMEELNQPIPESEIVNTVEEAVAFAATIGYPVIVRPAF 172
Cdd:COG0458 81 QTALNLAVELEEAGILE--GVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 173 TLGGTGGGMCANEEELREIAENGLKLSPVTQCLIERSIAGFKEIEYEVMRDSADNALVVCNMENFDPVGIHTGDSIVFAP 252
Cdd:COG0458 159 VLGGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRDGEDNVIIVGIMEHIEPAGVHSGDSICVAP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 253 AQTMSDYENQMLRDASLSIIRALKIEGGCNVQLALDphSFKYYVIEVNPRVSRSSALASKATGYPIAKLAAKIAVGLTLD 332
Cdd:COG0458 239 PQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVD--DGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 333 EVINPvTGstyamFEPALDYVVAKIPRFPFDKFEKGERRLGTQMKATGEVMAIGRNIEESLLKACRSLEIGVHHNEMPEL 412
Cdd:COG0458 317 ELGND-TG-----FEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGTVLLSL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 413 ASvSDDALIEKVVKAQDDRLFYVSEAIRRGYTPEEIAELTKIDIFYLDKLLHIFEIEQELGAHPQDLDVLKTAKLNGFSD 492
Cdd:COG0458 391 VA-DDDKEEALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDEIELEEIILVINTLLGAKSLGDSD 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447049177 493 RKIAELWETTADQVRQLRLENKIVPVYKMVDTCAAEFDSETPYFYSTYGWENESIKSDKESVLVLGS 559
Cdd:COG0458 470 GIIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYYYSTYEYENESEETEEPKVVVIGS 536
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
557-1057 |
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: 722.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 557 LGSGPIRIGQGVEFDYATVHSVKAIQAAGYEAIIMNSNPETVSTDFSVSDKLYFEPLTFEDVMNVIDLEQPKGVIVQFGG 636
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 637 QTAINLAEPLAKA----GVTILGTQVADLDRAEDRDLFEQALKELDIPQPPGQTATNEEEAALAARKIGFPVLVRPSYVL 712
Cdd:COG0458 81 QTALNLAVELEEAgileGVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSYVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 713 GGRAMEIVENEEDLRSYMRTAVKASPDHPVLVDSYIVG-QECEVDAISDGE-NVLIPGIMEHIERAGVHSGDSMAVYPPQ 790
Cdd:COG0458 161 GGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGaKEIEVDVVRDGEdNVIIVGIMEHIEPAGVHSGDSICVAPPQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 791 TLSQKVQETIADYTKRLAIGLNCLGMMNIQFVIKDEKVYVIEVNPRASRTVPFLSKVTNIPMAQVATKLILGQKLEELGY 870
Cdd:COG0458 241 TLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLDELGN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 871 QDGLYPESTRVHIKAPVFSFTKLAKVDSLLGPEMKSTGEVMGSDTTLEKALYKAFEASYLHLPtfGNVVFT-IADDAKEE 949
Cdd:COG0458 321 DTGFEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLP--GTVLLSlVADDDKEE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 950 ALDLARRFQNIGYGILATEGTAAFFASHGLQSQPVGKIGDDDKDIPSFVRKGRIQAIINTVGTKRTADEDGEQIRRSAIE 1029
Cdd:COG0458 399 ALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDEIELEEIILVINTLLGAKSLGDSDGIIRRALAA 478
|
490 500
....*....|....*....|....*...
gi 447049177 1030 HGVPLFTAIDTANAMLKVLESRSFVTEA 1057
Cdd:COG0458 479 KVPYVTTLAAAAAAALAIKAVETEAGEF 506
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
128-332 |
5.95e-92 |
|
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: 291.90 E-value: 5.95e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 128 DRDLFKQLMEELNQPIPESEI--VNTVEEAVAFAATIGYPVIVRPAFTLGGTGGGMCANEEELREIAENGLKLSPVT--- 202
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAgpVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAfgn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 203 -QCLIERSIAGFKEIEYEVMRDSADNALVVCNMENFDPVgiHTGDSIVFAPAQTMSDYENQMLRDASLSIIRALKIEGGC 281
Cdd:pfam02786 81 pQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447049177 282 NVQLALDPHSFKYYVIEVNPRVSRSSALASKATGYPIAKLAAKIAVGLTLD 332
Cdd:pfam02786 159 TVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
544-925 |
4.36e-72 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 260.48 E-value: 4.36e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 544 NESIKSDKESVLVLGSGPIRIGQGVEFDYATVHSVKAIQAAGYEAIIMNSNPETVSTDFSVSDKLYFEPLTFEDVMNVID 623
Cdd:PLN02735 16 KAGKRTDLKKIMILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATIMTDPETADRTYIAPMTPELVEQVIA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 624 LEQPKGVIVQFGGQTAINLAEPLA------KAGVTILGTQVADLDRAEDRDLFEQALKELDIPQPPGQTATNEEEAALAA 697
Cdd:PLN02735 96 KERPDALLPTMGGQTALNLAVALAesgileKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPPSGIATTLDECFEIA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 698 RKIG-FPVLVRPSYVLGGRAMEIVENEEDLRSYMRTAVKASPDHPVLVDSYIVG-QECEVDAISD-GENVLIPGIMEHIE 774
Cdd:PLN02735 176 EDIGeFPLIIRPAFTLGGTGGGIAYNKEEFETICKAGLAASITSQVLVEKSLLGwKEYELEVMRDlADNVVIICSIENID 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 775 RAGVHSGDSMAVYPPQTLSQKVQETIADYTKRL--AIGLNClGMMNIQFVI--KDEKVYVIEVNPRASRTVPFLSKVTNI 850
Cdd:PLN02735 256 PMGVHTGDSITVAPAQTLTDKEYQRLRDYSVAIirEIGVEC-GGSNVQFAVnpVDGEVMIIEMNPRVSRSSALASKATGF 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 851 PMAQVATKLILGQKLEE------LGYQDGLYPESTRVHIKAPVFSFTKLAKVDSLLGPEMKSTGEVMGSDTTLEKALYKA 924
Cdd:PLN02735 335 PIAKMAAKLSVGYTLDQipnditLKTPASFEPSIDYVVTKIPRFAFEKFPGSQPILTTQMKSVGEAMALGRTFQESFQKA 414
|
.
gi 447049177 925 F 925
Cdd:PLN02735 415 L 415
|
|
| CPSase_L_D3 |
smart01096 |
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ... |
420-540 |
3.37e-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: 3.37e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 420 LIEKVVKAQDDRLFYVSEAIRRGYTPEEIAELTKIDIFYLDKLLHIFEIEQEL---GAHPQDLDVLKTAKLNGFSDRKIA 496
Cdd:smart01096 1 LLEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELkkgGLDELDADLLRKAKRLGFSDRQIA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 447049177 497 ELWETTADQVRQLRLENKIVPVYKMVDTCAAEFDSETPYFYSTY 540
Cdd:smart01096 81 KLLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
|
|
| MGS_CPS_II |
cd01424 |
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate ... |
936-1046 |
7.22e-39 |
|
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: 139.92 E-value: 7.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 936 GNVVFTIADDAKEEALDLARRFQNIGYGILATEGTAAFFASHGLQSQPVGKIGDDDKDIPSFVRKGRIQAIINTVGTKRt 1015
Cdd:cd01424 1 GTVFISVADRDKPEAVEIAKRLAELGFKLVATEGTAKYLQEAGIPVEVVNKVSEGRPNIVDLIKNGEIQLVINTPSGKR- 79
|
90 100 110
....*....|....*....|....*....|.
gi 447049177 1016 ADEDGEQIRRSAIEHGVPLFTAIDTANAMLK 1046
Cdd:cd01424 80 AIRDGFSIRRAALEYKVPYFTTLDTARAAVE 110
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
666-866 |
4.90e-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: 138.59 E-value: 4.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 666 DRDLFEQALKELDIPQPPGQTAT--NEEEAALAARKIGFPVLVRPSYVLGGRAMEIVENEEDLRSYMRTAVKASP----D 739
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAGPveTEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPaafgN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 740 HPVLVDSYIVG-QECEVDAISDGE-NVLIPGIMEHIERagVHSGDSMAVYPPQTLSQKVQETIADYTKRLAIGLNCLGMM 817
Cdd:pfam02786 81 PQVLVEKSLKGpKHIEYQVLRDAHgNCITVCNRECSDQ--RRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447049177 818 NIQFVI--KDEKVYVIEVNPRASRTVPFLSKVTNIPMAQVATKLILGQKLE 866
Cdd:pfam02786 159 TVEFALdpFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| CPSase_L_D3 |
pfam02787 |
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate ... |
422-498 |
1.30e-29 |
|
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: 112.47 E-value: 1.30e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447049177 422 EKVVKAQDDRLFYVSEAIRRGYTPEEIAELTKIDIFYLDKLLHIFEIEQELGAHPQDLD--VLKTAKLNGFSDRKIAEL 498
Cdd:pfam02787 1 EELRTPTDERLFAIAEALRRGYSVEEIHELTKIDPWFLDKIKNIVELEKELKEAGLDLDaeLLREAKRLGFSDRQIAKL 79
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
663-864 |
1.59e-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: 109.96 E-value: 1.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 663 RAEDRDLFEQALKELDIPQPPGQTATNEEEAALAARKIGFPVLVRPSYVLGGRAMEIVENEEDLRSYMRTAVK----ASP 738
Cdd:COG0439 51 AMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAeakaGSP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 739 DHPVLVDSYIVGQECEVDAISDGENVLIPGIMEHIeRAGVHSGDSMAVYPPQtLSQKVQETIADYTKRL--AIGLNClGM 816
Cdd:COG0439 131 NGEVLVEEFLEGREYSVEGLVRDGEVVVCSITRKH-QKPPYFVELGHEAPSP-LPEELRAEIGELVARAlrALGYRR-GA 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 447049177 817 MNIQFVI-KDEKVYVIEVNPRAS--RTVPFLSKVTNIPMAQVATKLILGQK 864
Cdd:COG0439 208 FHTEFLLtPDGEPYLIEINARLGgeHIPPLTELATGVDLVREQIRLALGEP 258
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
71-329 |
1.74e-24 |
|
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: 104.18 E-value: 1.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 71 LEFVTRILRKERPDALLPtlGGQTGLNMAMELSkngilDELGveLLGTKLSAIDQAEDRDLFKQLMEELNQPIPESEIVN 150
Cdd:COG0439 6 IAAAAELARETGIDAVLS--ESEFAVETAAELA-----EELG--LPGPSPEAIRAMRDKVLMREALAAAGVPVPGFALVD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 151 TVEEAVAFAATIGYPVIVRPAftlGGTGG-GM--CANEEEL----REIAENGLKLSPVTQCLIERSIAGfKEIEYEVMrd 223
Cdd:COG0439 77 SPEEALAFAEEIGYPVVVKPA---DGAGSrGVrvVRDEEELeaalAEARAEAKAGSPNGEVLVEEFLEG-REYSVEGL-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 224 SADNALVVCNM---ENFDPVGIHTGDSivfAPAQtMSDYENQMLRDASLSIIRALKI-EGGCNVQLALDPHSfKYYVIEV 299
Cdd:COG0439 151 VRDGEVVVCSItrkHQKPPYFVELGHE---APSP-LPEELRAEIGELVARALRALGYrRGAFHTEFLLTPDG-EPYLIEI 225
|
250 260 270
....*....|....*....|....*....|..
gi 447049177 300 NPRVS--RSSALASKATGYPIAKLAAKIAVGL 329
Cdd:COG0439 226 NARLGgeHIPPLTELATGVDLVREQIRLALGE 257
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
36-353 |
7.50e-23 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 101.93 E-value: 7.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 36 SLKEEGYEVVLVNSNPATIMTDKEIADKVYIEP-------ITLEFVTRILRKERPDALLPTlgGQTGLNMameLSKNgiL 108
Cdd:COG3919 23 SLGEAGVRVIVVDRDPLGPAARSRYVDEVVVVPdpgddpeAFVDALLELAERHGPDVLIPT--GDEYVEL---LSRH--R 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 109 DELG--VELLGTKLSAIDQAEDRDLFKQLMEELNQPIPESEIVNTVEEAVAFAATIGYPVIVRPA--------FTLGGTG 178
Cdd:COG3919 96 DELEehYRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSADDLDALAEDLGFPVVVKPAdsvgydelSFPGKKK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 179 GGMCANEEELRE----IAENGLKLspvtqcLIERSIAGFKEIEYEVmrdsadNALVVCNMEnfdPVGIHTG-----DSIV 249
Cdd:COG3919 176 VFYVDDREELLAllrrIAAAGYEL------IVQEYIPGDDGEMRGL------TAYVDRDGE---VVATFTGrklrhYPPA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 250 F-APAQTMSDYENQmLRDASLSIIRALKIEGGCNVQLALDPHSFKYYVIEVNPRVSRSSALASKAtGYPIAKLAAKIAVG 328
Cdd:COG3919 241 GgNSAARESVDDPE-LEEAARRLLEALGYHGFANVEFKRDPRDGEYKLIEINPRFWRSLYLATAA-GVNFPYLLYDDAVG 318
|
330 340
....*....|....*....|....*..
gi 447049177 329 LTLDEVINPVTG--STYAMFEPALDYV 353
Cdd:COG3919 319 RPLEPVPAYREGvlWRVLPGDLLLRYL 345
|
|
| MGS |
smart00851 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
949-1036 |
2.90e-21 |
|
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: 89.07 E-value: 2.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 949 EALDLARRFQNIGYGILATEGTAAFFASHGL--QSQPVGKIGDDDKDIPSFVRKGRIQAIINTV-GTKRTADEDGEQIRR 1025
Cdd:smart00851 1 GLVEFAKRLAELGFELLATGGTAKFLREAGLpvVKTLHPKVHGGIPQILDLIKNGEIDLVINTLyPFEAQAHEDGYSIRR 80
|
90
....*....|.
gi 447049177 1026 SAIEHGVPLFT 1036
Cdd:smart00851 81 AAENIDIPGPT 91
|
|
| MGS |
pfam02142 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
949-1036 |
5.27e-20 |
|
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: 85.62 E-value: 5.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 949 EALDLARRFQNIGYGILATEGTAAFFASHGLQSQPV-GKIG----DDDKDIPSFVRKGRIQAIINTVGTKRTADEDGEQI 1023
Cdd:pfam02142 1 GLVELAKALVELGFELLATGGTAKFLREAGIPVTEVvEKTGegrpGGRVQIGDLIKNGEIDLVINTLYPFKATVHDGYAI 80
|
90
....*....|...
gi 447049177 1024 RRSAIEHGVPLFT 1036
Cdd:pfam02142 81 RRAAENIDIPGPT 93
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
646-875 |
1.46e-18 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 88.02 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 646 LAKAGVTILGTQVADLDRAEDRDLFEQALKELDIPQPPGQTATNEE--EAALAARKIGFPVLVRPSYVLGGRAMEIVENE 723
Cdd:PRK12767 91 FEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEdfKAALAKGELQFPLFVKPRDGSASIGVFKVNDK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 724 EDLRSYMRTAVKaspdhpVLVDSYIVGQECEVDAISDGENVLIpgimeHI---ERAGVHSGDSMavyppQTLSQKVQEtI 800
Cdd:PRK12767 171 EELEFLLEYVPN------LIIQEFIEGQEYTVDVLCDLNGEVI-----SIvprKRIEVRAGETS-----KGVTVKDPE-L 233
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447049177 801 ADYTKRLAIGLNCLGMMNIQFVIKDEKVYVIEVNPRASRTVPFLSKV-TNIPMAQVAtKLILGQKLEELG-YQDGLY 875
Cdd:PRK12767 234 FKLAERLAEALGARGPLNIQCFVTDGEPYLFEINPRFGGGYPLSYMAgANEPDWIIR-NLLGGENEPIIGeYKEGLY 309
|
|
| MGS_CPS_I_III |
cd01423 |
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases ... |
937-1041 |
4.00e-14 |
|
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: 69.64 E-value: 4.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 937 NVVFTIADDAKEEALDLARRFQNIGYGILATEGTAAFFASHGLQSQPV----GKIGDDDKDIPSFVRKGRIQAIIN--TV 1010
Cdd:cd01423 2 GILISIGSYSKPELLPTAQKLSKLGYKLYATEGTADFLLENGIPVTPVawpsEEPQNDKPSLRELLAEGKIDLVINlpSN 81
|
90 100 110
....*....|....*....|....*....|.
gi 447049177 1011 GTKRTADEDgEQIRRSAIEHGVPLFTAIDTA 1041
Cdd:cd01423 82 RGKRVLDND-YVMRRAADDFAVPLITNPKCA 111
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
672-860 |
5.58e-14 |
|
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: 73.99 E-value: 5.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 672 QALKELDIPQPPGQTATNEEEAALAA--RKIGFPVLVRPsyVLGG--RAMEIVENEEDLRSYMRTAVKAspDHPVLVDSY 747
Cdd:COG1181 101 RVLAAAGLPTPPYVVLRRGELADLEAieEELGLPLFVKP--AREGssVGVSKVKNAEELAAALEEAFKY--DDKVLVEEF 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 748 IVGQECEVdAISDGENVLIPGIMEHIERAGV-------HSGDSMAVYPPQtLSQKVQETIADYTKRLAIGLNCLGM---- 816
Cdd:COG1181 177 IDGREVTV-GVLGNGGPRALPPIEIVPENGFydyeakyTDGGTEYICPAR-LPEELEERIQELALKAFRALGCRGYarvd 254
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 447049177 817 MniqFVIKDEKVYVIEVNP-----RASrTVPFLSKVTNIPMAQVATKLI 860
Cdd:COG1181 255 F---RLDEDGEPYLLEVNTlpgmtPTS-LLPKAAAAAGISYEELIERII 299
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
553-875 |
3.63e-13 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 72.65 E-value: 3.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 553 SVLVLGSGPIrigqgvefDYATVHSVKAiqaAGYEAIIMNSNPETVS------TDFSVSDKLYFEPLTFEDVMNVIDLEQ 626
Cdd:COG3919 7 RVVVLGGDIN--------ALAVARSLGE---AGVRVIVVDRDPLGPAarsryvDEVVVVPDPGDDPEAFVDALLELAERH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 627 PKGVIVQFGGQTAINLAE--PLAKAGVTILGTQVADLDRAEDRDLFEQALKELDIPQPPGQTATNEEEAALAARKIGFPV 704
Cdd:COG3919 76 GPDVLIPTGDEYVELLSRhrDELEEHYRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSADDLDALAEDLGFPV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 705 LVRPSY--------VLGGRAMEIVENEEDLRSYMRTAVKAspDHPVLV-------DSYIVGQECEVDaiSDGENVLIPG- 768
Cdd:COG3919 156 VVKPADsvgydelsFPGKKKVFYVDDREELLALLRRIAAA--GYELIVqeyipgdDGEMRGLTAYVD--RDGEVVATFTg 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 769 --IMEHIERAGVHSGdSMAVYPPQtlsqkvqetIADYTKRL--AIGLNclGMMNIQFVI--KDEKVYVIEVNPRASRTVP 842
Cdd:COG3919 232 rkLRHYPPAGGNSAA-RESVDDPE---------LEEAARRLleALGYH--GFANVEFKRdpRDGEYKLIEINPRFWRSLY 299
|
330 340 350
....*....|....*....|....*....|....*...
gi 447049177 843 FlskVT----NIPMAQVAtkLILGQKLE-ELGYQDGLY 875
Cdd:COG3919 300 L---ATaagvNFPYLLYD--DAVGRPLEpVPAYREGVL 332
|
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
664-836 |
5.82e-13 |
|
ATP-grasp domain; No functional information or experimental verification of function is known in this family. This family appears to be an ATP-grasp domain (Pers. obs. A Bateman).
Pssm-ID: 396979 [Multi-domain] Cd Length: 160 Bit Score: 67.80 E-value: 5.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 664 AEDRDLFEQALKELDIPQPpgQTATNEEeaalaARKIGFPVLVRPSYVLGGRAMEIVENEEDLRSYMrtavkaspdHPVL 743
Cdd:pfam02655 1 ASDKLKTYKALKNAGVPTP--ETLQAEE-----LLREEKKYVVKPRDGCGGEGVRKVENGREDEAFI---------ENVL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 744 VDSYIVGQECEVDAISDGENVLI----PGIMEHIERAGVHSGDSMAVypPQTLSQKVQETIADYTKRLAiglNCLGMMNI 819
Cdd:pfam02655 65 VQEFIEGEPLSVSLLSDGEKALPlsvnRQYIDNGGSGFVYAGNVTPS--RTELKEEIIELAEEVVECLP---GLRGYVGV 139
|
170
....*....|....*..
gi 447049177 820 QFVIKDEKVYVIEVNPR 836
Cdd:pfam02655 140 DLVLKDNEPYVIEVNPR 156
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
109-328 |
6.68e-12 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 69.24 E-value: 6.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 109 DELGVELLGTKLSAIDQAEDRDLFKQLMEELNQP-IPES-EIVNTVEEAVAFAATIGYPVIVRPAftLGGTGGGMCA--N 184
Cdd:PRK08654 96 EKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPvLPGTeEGIEDIEEAKEIAEEIGYPVIIKAS--AGGGGIGMRVvyS 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 185 EEELRE-------IAENGLKLSPVtqcLIERSIAGFKEIEYEVMRDSADNAlvvcnmenfdpvgIHTGDS---------- 247
Cdd:PRK08654 174 EEELEDaiestqsIAQSAFGDSTV---FIEKYLEKPRHIEIQILADKHGNV-------------IHLGDRecsiqrrhqk 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 248 -IVFAPAQTMSDYENQMLRDASLSIIRALKIEGGCNVQLALDphSFKYYVIEVNPRVSRSSALASKATGYPIAKLAAKIA 326
Cdd:PRK08654 238 lIEEAPSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYS--NGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIA 315
|
..
gi 447049177 327 VG 328
Cdd:PRK08654 316 AG 317
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
83-331 |
7.85e-12 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 68.98 E-value: 7.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 83 PDALLPTLGGQTGLNMAME------------LSKNGILDEL----GVELLGTKLSAIDQAEDRDLFKQLMEELNQPI-PE 145
Cdd:PRK07178 53 ADPLAGYLNPRRLVNLAVEtgcdalhpgygfLSENAELAEIcaerGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVtPG 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 146 SE-IVNTVEEAVAFAATIGYPVIVRPAFTLGGTGGGMCANEEEL-----REIAEnGLKLSPVTQCLIERSIAGFKEIEYE 219
Cdd:PRK07178 133 SEgNLADLDEALAEAERIGYPVMLKATSGGGGRGIRRCNSREELeqnfpRVISE-ATKAFGSAEVFLEKCIVNPKHIEVQ 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 220 VMRDSADNALVV----CNMENfdpvgiHTGDSIVFAPAQTMSDYENQMLRDASLSIIRALKIEGGCNVQLALDpHSFKYY 295
Cdd:PRK07178 212 ILADSHGNVVHLferdCSIQR------RNQKLIEIAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLD-ADGEVY 284
|
250 260 270
....*....|....*....|....*....|....*.
gi 447049177 296 VIEVNPRVSRSSALASKATGYPIAKLAAKIAVGLTL 331
Cdd:PRK07178 285 FMEMNTRVQVEHTITEEITGIDIVREQIRIASGLPL 320
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
114-303 |
3.41e-11 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 67.86 E-value: 3.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 114 ELLGTKLSAIDQAEdrdlfkqlmeELNQP-IPESEI-VNTVEEAVAFAATIGYPVIVRPAftLGGTGGGM--CANEEELR 189
Cdd:PRK12999 115 RLLGDKVAARNAAI----------KAGVPvIPGSEGpIDDIEEALEFAEEIGYPIMLKAS--AGGGGRGMriVRSEEELE 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 190 EIAENGLKL------SPvtQCLIERSIAGFKEIEYEVMRDSADNalVV------CNME-NFDPVgihtgdsIVFAPAQTM 256
Cdd:PRK12999 183 EAFERAKREakaafgND--EVYLEKYVENPRHIEVQILGDKHGN--VVhlyerdCSVQrRHQKV-------VEIAPAPGL 251
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 447049177 257 SDYENQMLRDASLSIIRALKIEGGCNVQLALDPHSfKYYVIEVNPRV 303
Cdd:PRK12999 252 SEELRERICEAAVKLARAVGYVNAGTVEFLVDADG-NFYFIEVNPRI 297
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
642-836 |
5.67e-11 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 67.09 E-value: 5.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 642 LAEPLAKAGVTILGTQVADLDRAEDRDLFEQALKELDIPQPPG--QTATNEEEAALAARKIGFPVLVRPSYVLGGRAMEI 719
Cdd:PRK12999 95 FARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGseGPIDDIEEALEFAEEIGYPIMLKASAGGGGRGMRI 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 720 VENEEDLR----SYMRTAVKASPDHPVLVDSYIVG-QECEVDAISDGE-NVLipgimeH---------------IERAgv 778
Cdd:PRK12999 175 VRSEEELEeafeRAKREAKAAFGNDEVYLEKYVENpRHIEVQILGDKHgNVV------HlyerdcsvqrrhqkvVEIA-- 246
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447049177 779 hsgdsmavyPPQTLSQKVQETIADYTKRLA--IGLNCLGmmNIQF-VIKDEKVYVIEVNPR 836
Cdd:PRK12999 247 ---------PAPGLSEELRERICEAAVKLAraVGYVNAG--TVEFlVDADGNFYFIEVNPR 296
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
61-313 |
6.96e-11 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 64.91 E-value: 6.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 61 ADKVYIEP-IT----LEFVTRILRKERPDALLPTLGGQTGLnmameLSKN-GILDELGVELLGTKLSAIDQAEDRDLFKQ 134
Cdd:PRK12767 43 ADKFYVVPkVTdpnyIDRLLDICKKEKIDLLIPLIDPELPL-----LAQNrDRFEEIGVKVLVSSKEVIEICNDKWLTYE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 135 LMEELNQPIPESEIVNTVE--EAVAFAATIGYPVIVRPAFTLGGTGGGMCANEEELREIAENGLKLspvtqcLIERSIAG 212
Cdd:PRK12767 118 FLKENGIPTPKSYLPESLEdfKAALAKGELQFPLFVKPRDGSASIGVFKVNDKEELEFLLEYVPNL------IIQEFIEG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 213 fKEIEYEVMRDSADNALVVCNMENFDPVGIHTGDSIVFapaqtmsdyENQMLRDASLSIIRALKIEGGCNVQLALDPHsf 292
Cdd:PRK12767 192 -QEYTVDVLCDLNGEVISIVPRKRIEVRAGETSKGVTV---------KDPELFKLAERLAEALGARGPLNIQCFVTDG-- 259
|
250 260
....*....|....*....|.
gi 447049177 293 KYYVIEVNPRVSRSSALASKA 313
Cdd:PRK12767 260 EPYLFEINPRFGGGYPLSYMA 280
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
674-835 |
8.75e-11 |
|
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: 62.72 E-value: 8.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 674 LKELDIPQPPGQTATNE-------EEAALAARKIGFPVLVRPSyVLGGR-AMEIVENEEDLRSYMRTAVKAspDHPVLVD 745
Cdd:pfam07478 2 LKAAGLPVVPFVTFTRAdwklnpkEWCAQVEEALGYPVFVKPA-RLGSSvGVSKVESREELQAAIEEAFQY--DEKVLVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 746 SYIVGQECEVdAISDGENVLIPGIMEHIERAGVH-------SGDSMAVYPPQtLSQKVQETIADYTKRLAIGLNCLGMMN 818
Cdd:pfam07478 79 EGIEGREIEC-AVLGNEDPEVSPVGEIVPSGGFYdyeakyiDDSAQIVVPAD-LEEEQEEQIQELALKAYKALGCRGLAR 156
|
170
....*....|....*...
gi 447049177 819 IQ-FVIKDEKVYVIEVNP 835
Cdd:pfam07478 157 VDfFLTEDGEIVLNEVNT 174
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
667-862 |
2.77e-10 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 64.48 E-value: 2.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 667 RDLFEQA--LKELDIPQPPGQTATNEEEAALAARKIGFPVLVRPSYVLGGRAMEIVENEEDLRSYMRTAVKA-SPDhpVL 743
Cdd:PRK02186 106 RDKKRLArtLRDHGIDVPRTHALALRAVALDALDGLTYPVVVKPRMGSGSVGVRLCASVAEAAAHCAALRRAgTRA--AL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 744 VDSYIVGQECEVDAISDGENVLIPGIM-EHIERAGvHSGDSMAVYPPQtLSQKVQETIADYTKRL--AIGLNcLGMMNIQ 820
Cdd:PRK02186 184 VQAYVEGDEYSVETLTVARGHQVLGITrKHLGPPP-HFVEIGHDFPAP-LSAPQRERIVRTVLRAldAVGYA-FGPAHTE 260
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 447049177 821 FVIKDEKVYVIEVNPR-ASRTVP-FLSKVTNIPMAQVATKLILG 862
Cdd:PRK02186 261 LRVRGDTVVIIEINPRlAGGMIPvLLEEAFGVDLLDHVIDLHLG 304
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
37-336 |
6.20e-10 |
|
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: 61.66 E-value: 6.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 37 LKEEGYEVVLVNSNPATIMTDkeiadkvyiepitlefvtriLRKERPDALLPTLGGQTGLNMAMElsknGILDELGVELL 116
Cdd:COG1181 28 LDKAGYDVVPIGIDVEDLPAA--------------------LKELKPDVVFPALHGRGGEDGTIQ----GLLELLGIPYT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 117 GT--KLSAIdqAEDRDLFKQLMEELNQPIPESEIVNTVEEAV--AFAATIGYPVIVRPAFtlGGTGGGM--CANEEELRE 190
Cdd:COG1181 84 GSgvLASAL--AMDKALTKRVLAAAGLPTPPYVVLRRGELADleAIEEELGLPLFVKPAR--EGSSVGVskVKNAEELAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 191 IAENGLKLSPvtQCLIERSIAGfKEIEYEVMRDSADNALVVcnMEnFDPVGI--------HTGDSIVFAPAQtMSDYENQ 262
Cdd:COG1181 160 ALEEAFKYDD--KVLVEEFIDG-REVTVGVLGNGGPRALPP--IE-IVPENGfydyeakyTDGGTEYICPAR-LPEELEE 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447049177 263 MLRDASLSIIRALKIEGGCNVQLALDPHSfKYYVIEVN--PRVSRSSalaskatGYPiaKLAAkiAVGLTLDEVIN 336
Cdd:COG1181 233 RIQELALKAFRALGCRGYARVDFRLDEDG-EPYLLEVNtlPGMTPTS-------LLP--KAAA--AAGISYEELIE 296
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
102-303 |
7.27e-10 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 62.51 E-value: 7.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 102 LSKNG----ILDELGVELLGTKLSAIDQAEDRDLFKQLMEELNQP-IPESE-IVNTVEEAVAFAATIGYPVIVRPafTLG 175
Cdd:PRK08591 85 LSENAdfaeICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPvVPGSDgPVDDEEEALAIAKEIGYPVIIKA--TAG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 176 GTGGGM--CANEEELreiaENGLKLspvTQ-----------CLIERSIAGFKEIEYEVMRDSADNAlvvcnmenfdpvgI 242
Cdd:PRK08591 163 GGGRGMrvVRTEAEL----EKAFSM---ARaeakaafgnpgVYMEKYLENPRHIEIQVLADGHGNA-------------I 222
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447049177 243 HTGD---SI------VF--APAQTMSDYENQMLRDASLSIIRALKIEGGCNVQLALDpHSFKYYVIEVNPRV 303
Cdd:PRK08591 223 HLGErdcSLqrrhqkVLeeAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYE-KNGEFYFIEMNTRI 293
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
642-836 |
8.06e-10 |
|
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: 63.17 E-value: 8.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 642 LAEPLAKAGVTILGTQVADLDRAEDRDLFEQALKELDIPQPPGQTA--TNEEEAALAARKIGFPVLVRPSYVLGGRAMEI 719
Cdd:COG1038 94 FARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGpvDDLEEALAFAEEIGYPVMLKAAAGGGGRGMRV 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 720 VENEEDLR----SYMRTAVKASPDHPVLVDSYIVG-QECEVDAISDGE-NVLipgimeH---------------IERAgv 778
Cdd:COG1038 174 VRSEEELEeafeSARREAKAAFGDDEVFLEKYIERpKHIEVQILGDKHgNIV------HlferdcsvqrrhqkvVEIA-- 245
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447049177 779 hsgdsmavyPPQTLSQKVQETIADYTKRLA--IGLNCLGmmNIQF-VIKDEKVYVIEVNPR 836
Cdd:COG1038 246 ---------PAPNLDEELREAICEAAVKLAkaVGYVNAG--TVEFlVDDDGNFYFIEVNPR 295
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
664-752 |
2.40e-09 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 61.33 E-value: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 664 AEDRDLFEQALKELDIPQPPGQTATNEEEAALAARKIGFPVLVRPSYVLGGRAMEI-VENEEDLRSYMRTAVKASPDhpV 742
Cdd:PRK14016 212 ACDKELTKRLLAAAGVPVPEGRVVTSAEDAWEAAEEIGYPVVVKPLDGNHGRGVTVnITTREEIEAAYAVASKESSD--V 289
|
90
....*....|
gi 447049177 743 LVDSYIVGQE 752
Cdd:PRK14016 290 IVERYIPGKD 299
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
114-303 |
2.51e-09 |
|
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: 61.63 E-value: 2.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 114 ELLGTKLSAIDQAEdrdlfkqlmeELNQP-IPESEI-VNTVEEAVAFAATIGYPVIVRPAftLGGTGGGM--CANEEELR 189
Cdd:COG1038 114 EMLGDKVAARAAAI----------EAGVPvIPGTEGpVDDLEEALAFAEEIGYPVMLKAA--AGGGGRGMrvVRSEEELE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 190 EIAE-----------NGlklspvtQCLIERSIAGFKEIEYEVMRDSADNalVV------CnmenfdpvgihtgdSI---- 248
Cdd:COG1038 182 EAFEsarreakaafgDD-------EVFLEKYIERPKHIEVQILGDKHGN--IVhlferdC--------------SVqrrh 238
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 447049177 249 --V--FAPAQTMSDYENQMLRDASLSIIRALKIEGGCNVQLALDPHSfKYYVIEVNPRV 303
Cdd:COG1038 239 qkVveIAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVDDDG-NFYFIEVNPRI 296
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
112-328 |
9.97e-09 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 58.99 E-value: 9.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 112 GVELLGTKLSAIDQAEDRDLFKQLMEELNQP-IPESE-IVNTVEEAVAFAATIGYPVIVRPAftLGGTGGGMCANEEElr 189
Cdd:PRK08462 101 NIKFIGPSVEVMALMSDKSKAKEVMKRAGVPvIPGSDgALKSYEEAKKIAKEIGYPVILKAA--AGGGGRGMRVVEDE-- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 190 EIAENgLKLSPVTQCL---------IERSIAGFKEIEYEVMRDSADNALVV----CNMENfdpvgiHTGDSIVFAPAQTM 256
Cdd:PRK08462 177 SDLEN-LYLAAESEALsafgdgtmyMEKFINNPRHIEVQILGDKHGNVIHVgerdCSLQR------RHQKLIEESPAVVL 249
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447049177 257 SDYENQMLRDASLSIIRALKIEGGCNVQLALDpHSFKYYVIEVNPRVSRSSALASKATGYPIAKLAAKIAVG 328
Cdd:PRK08462 250 DEKTRERLHETAIKAAKAIGYEGAGTFEFLLD-SNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEG 320
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
642-836 |
1.47e-08 |
|
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid transport and metabolism];
Pssm-ID: 441833 [Multi-domain] Cd Length: 370 Bit Score: 58.01 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 642 LAEPLAkAGVTILGTQVADLDRAEDRDLFEQALKELDIPQPPgqTATNEEEAAlaarkigFPVLVRPSYVLGGRAMEIVE 721
Cdd:COG2232 89 LLERLA-RRLPLLGNPPEVVRRVKDPLRFFALLDELGIPHPE--TRFEPPPDP-------GPWLVKPIGGAGGWHIRPAD 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 722 NEedlrsymrtavkASPDHPVLVDSYIVGQECEVDAISDGENVLIPGIMEHIERAgvhSGDSMAVYP----PQTLSQKVQ 797
Cdd:COG2232 159 SE------------APPAPGRYFQRYVEGTPASVLFLADGSDARVLGFNRQLIGP---AGERPFRYGgnigPLALPPALA 223
|
170 180 190
....*....|....*....|....*....|....*....
gi 447049177 798 ETIADYTKRLAIGLNCLGMMNIQFVIKDEKVYVIEVNPR 836
Cdd:COG2232 224 EEMRAIAEALVAALGLVGLNGVDFILDGDGPYVLEVNPR 262
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
666-842 |
1.50e-08 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 57.43 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 666 DRDLFEQALKELDIPQPPGQTATNEEEAALAARKIGFPVLVRPsyVLGGR--AMEIVENEEDLRSYMRTAVKASPDhpVL 743
Cdd:PRK01372 98 DKLRTKLVWQAAGLPTPPWIVLTREEDLLAAIDKLGLPLVVKP--AREGSsvGVSKVKEEDELQAALELAFKYDDE--VL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 744 VDSYIVGQECEVdAISDGEnVLipGIMEhIERAGV--------HSGDSMAVYPPQtLSQKVQETIADYTKRLAIGLNCLG 815
Cdd:PRK01372 174 VEKYIKGRELTV-AVLGGK-AL--PVIE-IVPAGEfydyeakyLAGGTQYICPAG-LPAEIEAELQELALKAYRALGCRG 247
|
170 180
....*....|....*....|....*...
gi 447049177 816 MMNIQFVIKDE-KVYVIEVNprasrTVP 842
Cdd:PRK01372 248 WGRVDFMLDEDgKPYLLEVN-----TQP 270
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
674-836 |
1.73e-08 |
|
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide synthetase catalyzes the second step in the de novo biosynthesis of purine. The reaction catalyzed by Phosphoribosylglycinamide synthetase is the ATP- dependent addition of 5-phosphoribosylamine to glycine to form 5'phosphoribosylglycinamide. This domain is related to the ATP-grasp domain of biotin carboxylase/carbamoyl phosphate synthetase (see pfam02786).
Pssm-ID: 395851 [Multi-domain] Cd Length: 194 Bit Score: 55.75 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 674 LKELDIPQPPGQTATNEEEAALAARKIGFPVLV-RPSYVLGGRAMEIVENEED----LRSYMRTAVKASPDHPVLVDSYI 748
Cdd:pfam01071 10 MKRYGIPTAEYETFTDPEEAKSYIQEAGFPAIVvKADGLAAGKGVIVASSNEEaikaVDEILEQKKFGEAGETVVIEEFL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 749 VGQECEVDAISDGENVLIPGIMEHIERAGvhSGDS------MAVYPP-----QTLSQKVQETIADYT-KRLAI-GLNCLG 815
Cdd:pfam01071 90 EGEEVSVLAFVDGKTVKPLPPAQDHKRAG--EGDTgpntggMGAYSPapvitPELLERIKETIVEPTvDGLRKeGIPFKG 167
|
170 180
....*....|....*....|.
gi 447049177 816 MMNIQFVIKDEKVYVIEVNPR 836
Cdd:pfam01071 168 VLYAGLMLTKDGPKVLEFNCR 188
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
662-866 |
1.85e-08 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 58.18 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 662 DRAEDRDLFEQAlkelDIPQPPG--QTATNEEEAALAARKIGFPVLVRPSYVLGGRAMEIVENEEDLRSYMRTAVKASP- 738
Cdd:PRK05586 115 NKSNAREIMIKA----GVPVVPGseGEIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEEELIKAFNTAKSEAKa 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 739 ---DHPVLVDSYIVG-QECEVDAISDG-ENVLIPGIME-HIERagvHSGDSMAVYPPQTLSQKVQETIADYTKRLAIGLN 812
Cdd:PRK05586 191 afgDDSMYIEKFIENpKHIEFQILGDNyGNVVHLGERDcSLQR---RNQKVLEEAPSPVMTEELRKKMGEIAVKAAKAVN 267
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 447049177 813 CLGMMNIQFVI-KDEKVYVIEVNPRASRTVPFLSKVTNIPMAQVATKLILGQKLE 866
Cdd:PRK05586 268 YKNAGTIEFLLdKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEKLS 322
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
642-727 |
4.31e-08 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 56.96 E-value: 4.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 642 LAEPLAKAGVTILGTQVADLDRAEDRDLFEQALKELDIPQPPGQTAT--NEEEAALAARKIGFPVLVRPSYVLGGRAMEI 719
Cdd:PRK06111 91 FAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNleDAEEAIAIARQIGYPVMLKASAGGGGIGMQL 170
|
....*...
gi 447049177 720 VENEEDLR 727
Cdd:PRK06111 171 VETEQELT 178
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
102-332 |
4.73e-08 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 56.64 E-value: 4.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 102 LSKNG----ILDELGVELLGTKLSAIDQAEDRDLFKQLMEELNQPI-PESE-IVNTVEEAVAFAATIGYPVIVRPAFTLG 175
Cdd:PRK05586 85 LSENSkfakMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVvPGSEgEIENEEEALEIAKEIGYPVMVKASAGGG 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 176 GTGGGMCANEEELREIAENGLKLSPVT----QCLIERSIAGFKEIEYEVMRDSADNALVVCNMEnfdpVGIHTGDSIVF- 250
Cdd:PRK05586 165 GRGIRIVRSEEELIKAFNTAKSEAKAAfgddSMYIEKFIENPKHIEFQILGDNYGNVVHLGERD----CSLQRRNQKVLe 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 251 -APAQTMSDYENQMLRDASLSIIRALKIEGGCNVQLALDPHSfKYYVIEVNPRVSRSSALASKATGYPIAKLAAKIAVGL 329
Cdd:PRK05586 241 eAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDG-NFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGE 319
|
...
gi 447049177 330 TLD 332
Cdd:PRK05586 320 KLS 322
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
571-835 |
5.11e-08 |
|
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: 55.72 E-value: 5.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 571 DYATVHSVKAIQAAGYEAIIMNSnpetvstdfsvsDKLYFEPLTFEDVMNVIDLEQPKGVIVQFGG-QTAINLAEPLAKA 649
Cdd:COG0189 13 KDSTKALIEAAQRRGHEVEVIDP------------DDLTLDLGRAPELYRGEDLSEFDAVLPRIDPpFYGLALLRQLEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 650 GVTILGTQVAdLDRAEDRDLFEQALKELDIPQPPGQTATNEEEAALAARKIGFPVLVRPSYVLGGRAMEIVENEEDLRSY 729
Cdd:COG0189 81 GVPVVNDPEA-IRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDALESI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 730 MRTaVKASPDHPVLVDSYIV---GQECEVDAIsDGEnvLIPGIM----EHIERAGVHSGDSMAvypPQTLSQKVQETIAD 802
Cdd:COG0189 160 LEA-LTELGSEPVLVQEFIPeedGRDIRVLVV-GGE--PVAAIRripaEGEFRTNLARGGRAE---PVELTDEERELALR 232
|
250 260 270
....*....|....*....|....*....|...
gi 447049177 803 YTKRLAIGLNClgmmnIQFVIKDEKVYVIEVNP 835
Cdd:COG0189 233 AAPALGLDFAG-----VDLIEDDDGPLVLEVNV 260
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
642-748 |
1.40e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 55.37 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 642 LAEPLAKAGVTILGTQVADLDRAEDRDLFEQALKELDIPQPPG--QTATNEEEAALAARKIGFPVLVRPSYVLGGRAMEI 719
Cdd:PRK08654 91 FAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGteEGIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRV 170
|
90 100 110
....*....|....*....|....*....|...
gi 447049177 720 VENEEDL----RSYMRTAVKASPDHPVLVDSYI 748
Cdd:PRK08654 171 VYSEEELedaiESTQSIAQSAFGDSTVFIEKYL 203
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
113-229 |
1.60e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 55.03 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 113 VELLGTKLSAidqaedrdlfKQLMEELNQPI-P-ESEIVNTVEEAVAFAATIGYPVIVRPAFTLGGTGGGMCANEEELRE 190
Cdd:PRK06111 110 IAKMGSKIEA----------RRAMQAAGVPVvPgITTNLEDAEEAIAIARQIGYPVMLKASAGGGGIGMQLVETEQELTK 179
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 447049177 191 -IAENGLKLSPV---TQCLIERSIAGFKEIEYEVMRDSADNAL 229
Cdd:PRK06111 180 aFESNKKRAANFfgnGEMYIEKYIEDPRHIEIQLLADTHGNTV 222
|
|
| purT |
PRK09288 |
formate-dependent phosphoribosylglycinamide formyltransferase; |
616-836 |
1.78e-07 |
|
formate-dependent phosphoribosylglycinamide formyltransferase;
Pssm-ID: 236454 [Multi-domain] Cd Length: 395 Bit Score: 54.76 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 616 EDVMNVIDLEQPKGVI--VQfggqtAIN---LAEpLAKAGVTIL----GTQVAdLDRAEDRDLfeqALKELDIPQPPGQT 686
Cdd:PRK09288 65 DALRAVIEREKPDYIVpeIE-----AIAtdaLVE-LEKEGFNVVptarATRLT-MNREGIRRL---AAEELGLPTSPYRF 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 687 ATNEEEAALAARKIGFPVLVRPsyVLG--GRAMEIVENEEDLRSYMRTAVKASP-DHP-VLVDSYIvgqecEVD------ 756
Cdd:PRK09288 135 ADSLEELRAAVEEIGYPCVVKP--VMSssGKGQSVVRSPEDIEKAWEYAQEGGRgGAGrVIVEEFI-----DFDyeitll 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 757 AIS--DGENVLIPGImEHIEragvHSGDSMAVYPPQTLSQKVQETIADYTKRLAIGLNCLGMMNIQFVIKDEKVYVIEVN 834
Cdd:PRK09288 208 TVRavDGGTHFCAPI-GHRQ----EDGDYRESWQPQPMSPAALEEAQEIAKKVTDALGGRGLFGVELFVKGDEVYFSEVS 282
|
..
gi 447049177 835 PR 836
Cdd:PRK09288 283 PR 284
|
|
| MGS-like |
cd00532 |
MGS-like domain. This domain composes the whole protein of methylglyoxal synthetase, which ... |
938-1043 |
2.58e-07 |
|
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: 50.20 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 938 VVFTIADDAKEEALDLARRFQNIGYGILATEGTAAFFASHGLQSQPVGKI--GDDDKDIPSFVRKGRIQAIINTV--GTK 1013
Cdd:cd00532 2 VFLSVSDHVKAMLVDLAPKLSSDGFPLFATGGTSRVLADAGIPVRAVSKRheDGEPTVDAAIAEKGKFDVVINLRdpRRD 81
|
90 100 110
....*....|....*....|....*....|
gi 447049177 1014 RTADEDGEQIRRSAIEHGVPLFTAIDTANA 1043
Cdd:cd00532 82 RCTDEDGTALLRLARLYKIPVTTPNATAMF 111
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
109-332 |
2.69e-07 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 54.43 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 109 DELGVELLGTKLSAIDQAEDRDLFKQLMEELNQPI-PESEIVN--TVEEAVAFAATIGYPVIVRPAFTLGGTGGGMCANE 185
Cdd:PRK08463 95 EDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIvPGTEKLNseSMEEIKIFARKIGYPVILKASGGGGGRGIRVVHKE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 186 EELrEIAENGLKLSPVT-----QCLIERSIAGFKEIEYEVMRDSADNALVVCnmENFDPVGIHTGDSIVFAPAQTMSDYE 260
Cdd:PRK08463 175 EDL-ENAFESCKREALAyfnndEVFMEKYVVNPRHIEFQILGDNYGNIIHLC--ERDCSIQRRHQKVIEIAPCPSISDNL 251
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447049177 261 NQMLRDASLSIIRALKIEGGCNVQLALDPHSfKYYVIEVNPRVSRSSALASKATGYPIAKLAAKIAVGLTLD 332
Cdd:PRK08463 252 RKTMGVTAVAAAKAVGYTNAGTIEFLLDDYN-RFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGEILD 322
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
32-300 |
3.49e-07 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 53.19 E-value: 3.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 32 QACL-SLKEEGYEVVLVNsnpatimTDKEIADKvyiepitlefvtriLRKERPDALLPTLGGQTGLNMAMElsknGILDE 110
Cdd:PRK01372 26 AAVLaALREAGYDAHPID-------PGEDIAAQ--------------LKELGFDRVFNALHGRGGEDGTIQ----GLLEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 111 LGVELLGTKL--SAIdqAEDRDLFKQLMEELNQPIPESEIVNTVEEAVAFAATIGYPVIVRPAftLGGTGGGM--CANEE 186
Cdd:PRK01372 81 LGIPYTGSGVlaSAL--AMDKLRTKLVWQAAGLPTPPWIVLTREEDLLAAIDKLGLPLVVKPA--REGSSVGVskVKEED 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 187 ELREIAENGLKLSPvtQCLIERSIAGfKEIEYEVMRDSadnALVVCNMEnfdPVGI--------HTGDSIVFAPAQtMSD 258
Cdd:PRK01372 157 ELQAALELAFKYDD--EVLVEKYIKG-RELTVAVLGGK---ALPVIEIV---PAGEfydyeakyLAGGTQYICPAG-LPA 226
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 447049177 259 YENQMLRDASLSIIRALKIEGGCNVQLALDPHSfKYYVIEVN 300
Cdd:PRK01372 227 EIEAELQELALKAYRALGCRGWGRVDFMLDEDG-KPYLLEVN 267
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
118-170 |
3.66e-07 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 54.39 E-value: 3.66e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 447049177 118 TKLSAIDQAEDRDLFKQLMEELNQPIPESEIVNTVEEAVAFAATIGYPVIVRP 170
Cdd:PRK14016 204 TSAIAVDIACDKELTKRLLAAAGVPVPEGRVVTSAEDAWEAAEEIGYPVVVKP 256
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
643-733 |
3.84e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 53.65 E-value: 3.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 643 AEPLAKAGVTILGTQVADLDRAEDRDLFEQALKELDIPQPPGQTA--TNEEEAALAARKIGFPVLVRPSYVLGGRAMEIV 720
Cdd:PRK08591 92 AEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGpvDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVV 171
|
90
....*....|...
gi 447049177 721 ENEEDLRSYMRTA 733
Cdd:PRK08591 172 RTEAELEKAFSMA 184
|
|
| ATP-grasp_4 |
pfam13535 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
700-836 |
4.30e-07 |
|
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 316093 [Multi-domain] Cd Length: 160 Bit Score: 50.74 E-value: 4.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 700 IGFPVLVRPSYVLGGRAMEIVENEED-------LRSYMRTAVKASPDHPV-----LVDSYIVGQECEVDAI--SDGENVL 765
Cdd:pfam13535 1 IPYPCVIKPSVGFFSVGVYKINNREEwkaafaaIREEIEQWKEMYPEAVVdggsfLVEEYIEGEEFAVDAYfdENGEPVI 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447049177 766 IpGIMEHIERAGVHSGDSMAVYPPQtLSQKVQETIADYTKRL--AIGLNcLGMMNIQFVIKDE-KVYVIEVNPR 836
Cdd:pfam13535 81 L-NILKHDFASSEDVSDRIYVTSAS-IIRETQAAFTEFLKRInaLLGLK-NFPVHIELRVDEDgQIIPIEVNPL 151
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
641-865 |
8.04e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 52.82 E-value: 8.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 641 NLAEPLAKAGVTILGTQVADLDRAEDRDLFEQALKELDIPQPPGQTAT--NEEEAALAARKIGFPVLVRPSYVLGGRAME 718
Cdd:PRK08462 92 NFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGAlkSYEEAKKIAKEIGYPVILKAAAGGGGRGMR 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 719 IVENEEDL-RSYMRT---AVKASPDHPVLVDSYIVG-QECEVDAISDGE-NVLipgimeHIERAGV-----HSG---DSM 784
Cdd:PRK08462 172 VVEDESDLeNLYLAAeseALSAFGDGTMYMEKFINNpRHIEVQILGDKHgNVI------HVGERDCslqrrHQKlieESP 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 785 AVYPPQTLSQKVQETIADYTKrlAIGLNCLGmmNIQFVI-KDEKVYVIEVNPRASRTVPFLSKVTNIPMAQVATKLILGQ 863
Cdd:PRK08462 246 AVVLDEKTRERLHETAIKAAK--AIGYEGAG--TFEFLLdSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGE 321
|
..
gi 447049177 864 KL 865
Cdd:PRK08462 322 EL 323
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
37-193 |
9.22e-07 |
|
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: 51.87 E-value: 9.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 37 LKEEGYEVVLVNsnpatimtdkeiADKVYIEPITLEFVTRILRKERPDALLPTlggQTGLNMAMELSKNgildelgVELL 116
Cdd:COG0189 23 AQRRGHEVEVID------------PDDLTLDLGRAPELYRGEDLSEFDAVLPR---IDPPFYGLALLRQ-------LEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 117 GTKL----SAIDQAEDRDLFKQLMEELNQPIPESEIVNTVEEAVAFAATIGYPVIVRPAFTLGGTGGGMCANEEELREIA 192
Cdd:COG0189 81 GVPVvndpEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDALESIL 160
|
.
gi 447049177 193 E 193
Cdd:COG0189 161 E 161
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
643-865 |
1.43e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 52.06 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 643 AEPLAKAGVTILGTQVADLDRAEDRDLFEQALKELDIPQPPGQTA--TNEEEAALAARKIGFPVLVRPSYVLGGRAMEIV 720
Cdd:PRK12833 95 AEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGvvASLDAALEVAARIGYPLMIKAAAGGGGRGIRVA 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 721 ENEEDLRSYM----RTAVKASPDHPVLVDSYIV-GQECEVDAISDGENVLipgimeHI-ERAGVHSGDSMAVY---PPQT 791
Cdd:PRK12833 175 HDAAQLAAELplaqREAQAAFGDGGVYLERFIArARHIEVQILGDGERVV------HLfERECSLQRRRQKILeeaPSPS 248
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447049177 792 LSQKVQETIADYTKRLAIGLNCLGMMNIQFVIKDEK--VYVIEVNPRASRTVPFLSKVTNIPMAQVATKLILGQKL 865
Cdd:PRK12833 249 LTPAQRDALCASAVRLARQVGYRGAGTLEYLFDDARgeFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEPL 324
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
642-865 |
2.26e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 51.26 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 642 LAEPLAKAGVTILGTQVADLDRAEDRDLFEQALKELDIPQPPGQTATNE--EEAALAARKIGFPVLVRPSYVLGGRAMEI 719
Cdd:PRK07178 90 LAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLAdlDEALAEAERIGYPVMLKATSGGGGRGIRR 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 720 VENEEDLRS-YMRT---AVKASPDHPVLVDSYIVG-QECEVDAISDGENVLIpGIMEH---IERagvHSGDSMAVYPPQT 791
Cdd:PRK07178 170 CNSREELEQnFPRViseATKAFGSAEVFLEKCIVNpKHIEVQILADSHGNVV-HLFERdcsIQR---RNQKLIEIAPSPQ 245
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447049177 792 LSQKVQETIADYTKRLAIGLNCLGMMNIQFVI-KDEKVYVIEVNPRASRTVPFLSKVTNIPMAQVATKLILGQKL 865
Cdd:PRK07178 246 LTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLdADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLPL 320
|
|
| PRK07206 |
PRK07206 |
hypothetical protein; Provisional |
579-815 |
2.55e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 180883 [Multi-domain] Cd Length: 416 Bit Score: 51.18 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 579 KAIQAAGYEAI-IMNSN--PETVSTDFSVSDklYFEPLTFEDVMNVID-LEQ--PKGVIVqfGGQTAINLAEPLAKagvt 652
Cdd:PRK07206 19 PAFKKRGIEPIaVTSSCllDPYYYASFDTSD--FIEVIINGDIDDLVEfLRKlgPEAIIA--GAESGVELADRLAE---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 653 ILGTQVA-DLDRAEDR-DLFE--QALKELDIPqPPGQTATNEEEAALA----ARKIGFPVLVRPSYVLGGRAMEIVENEE 724
Cdd:PRK07206 91 ILTPQYSnDPALSSARrNKAEmiNALAEAGLP-AARQINTADWEEAEAwlreNGLIDRPVVIKPLESAGSDGVFICPAKG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 725 DLRSYMRTAVK-----ASPDHPVLVDSYIVGQECEVDAIS-DGENVLIPGIMEHieraGVHSGDSMAVYPPQTL---SQK 795
Cdd:PRK07206 170 DWKHAFNAILGkanklGLVNETVLVQEYLIGTEYVVNFVSlDGNHLVTEIVRYH----KTSLNSGSTVYDYDEFldySEP 245
|
250 260
....*....|....*....|
gi 447049177 796 VQETIADYTKRLaigLNCLG 815
Cdd:PRK07206 246 EYQELVDYTKQA---LDALG 262
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
1-332 |
7.38e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 49.75 E-value: 7.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 1 MPKRtdIQKIMVIGSGPI---IIGQAAEFDYAGTQACLSLKEEgyevvlvnSNPATiMTDKEI------ADKVYIEPitl 71
Cdd:PRK12833 1 MPSR--IRKVLVANRGEIavrIIRAARELGMRTVAACSDADRD--------SLAAR-MADEAVhigpshAAKSYLNP--- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 72 EFVTRILRKERPDALLPTLGGqtglnmameLSKNGILDE----LGVELLGTKLSAIDQAEDRDLFKQLMEELNQP-IPES 146
Cdd:PRK12833 67 AAILAAARQCGADAIHPGYGF---------LSENAAFAEaveaAGLIFVGPDAQTIRTMGDKARARRTARRAGVPtVPGS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 147 E-IVNTVEEAVAFAATIGYPVIVRPAFTLGGTGGGMCANEEELREIAenglklsPVTQ-----------CLIERSIAGFK 214
Cdd:PRK12833 138 DgVVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQLAAEL-------PLAQreaqaafgdggVYLERFIARAR 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 215 EIEYEVMRDSADnalVVCNMENfdPVGIHTGDSIVF--APAQTMSDYENQMLRDASLSIIRALKIEGGCNVQLALDPHSF 292
Cdd:PRK12833 211 HIEVQILGDGER---VVHLFER--ECSLQRRRQKILeeAPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDDARG 285
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 447049177 293 KYYVIEVNPRVSRSSALASKATGYPIAKLAAKIAVGLTLD 332
Cdd:PRK12833 286 EFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEPLR 325
|
|
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
674-836 |
1.53e-05 |
|
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; Phosphoribosylamine-glycine ligase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439921 [Multi-domain] Cd Length: 422 Bit Score: 48.47 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 674 LKELDIPQPPGQTATNEEEAALAARKIGFPVLVRPSYVLGGR----AMEIVENEEDLRSYMRTAVKASPDHPVLVDSYIV 749
Cdd:COG0151 110 MARYGIPTAAYRVFTDLEEALAYLEEQGAPIVVKADGLAAGKgvvvAETLEEALAAVDDMLADGKFGDAGARVVIEEFLE 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 750 GQECEVDAISDGENVLI-PGIMEHiERAGvhSGDS------MAVYPP-----QTLSQKVQETIADYTKR--LAIGLNCLG 815
Cdd:COG0151 190 GEEASLFALTDGKTVLPlPTAQDH-KRAG--DGDTgpntggMGAYSPapvvtEELLEKIMEEIIEPTVAgmAAEGIPYRG 266
|
170 180
....*....|....*....|.
gi 447049177 816 MMNIQFVIKDEKVYVIEVNPR 836
Cdd:COG0151 267 VLYAGLMITADGPKVLEFNVR 287
|
|
| ATPgrasp_Ter |
pfam15632 |
ATP-grasp in the biosynthetic pathway with Ter operon; This ATP-grasp family is related to ... |
741-867 |
3.68e-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: 44.53 E-value: 3.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 741 PVLVDSYIVGQECEVDAISDGENVLIPgimehIERAGVHSGDsmavyppQTLSQkvQETIADYTKRLAIGLNCLGMMNIQ 820
Cdd:pfam15632 4 PLLVMEYLPGPEYSVDCLAGHGELIAA-----VPRRKGDGGI-------QTLED--DPELIEAARRLAEAFGLDGLFNVQ 69
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 447049177 821 FVIKDEKVYVIEVNPRASRTVPfLSKVTNIPMAQVATKLILGQKLEE 867
Cdd:pfam15632 70 FRYDGDGPKLLEINPRMSGGIG-YSCLAGVNLPYLALKLLLGLETPD 115
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
643-728 |
3.90e-05 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 47.50 E-value: 3.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 643 AEPLAKAGVTILGTQVADLDRAEDRDLFEQALKELDIPQPPGQTATNE---EEAALAARKIGFPVLVRPSYVLGGRAMEI 719
Cdd:PRK08463 91 AKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTEKLNSesmEEIKIFARKIGYPVILKASGGGGGRGIRV 170
|
....*....
gi 447049177 720 VENEEDLRS 728
Cdd:PRK08463 171 VHKEEDLEN 179
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
62-325 |
4.25e-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: 46.57 E-value: 4.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 62 DKVYIEPITLEFVTRILRKERPDALLPTlggqtGLNMAMELSKNGILDELGVELLGTKlSAIDQAEDRDLFKQLMEELNQ 141
Cdd:TIGR00768 28 KVVTPPAINLTFNEGPRALAELDVVIVR-----IVSMFRGLAVLRYLESLGVPVINSS-DAILNAGDKFLSHQLLAKAGI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 142 PIPESEIVNTVEEAVAFAATIGYPVIVRPAFTLGGTGGGMCANEEELREIAE-----NGLKLSPVTQCLIERSiaGFKEI 216
Cdd:TIGR00768 102 PLPRTGLAGSPEEALKLIEEIGFPVVLKPVFGSWGRGVSLARDRQAAESLLEhfeqlNGPQNLFLVQEYIKKP--GGRDI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 217 EYEVMRDSADNALVVCNMENFdpvgihtgDSIVFAPAQTMSDYENQMLRDASLSIIRALKIEgGCNVQLALDPHSFKyyV 296
Cdd:TIGR00768 180 RVFVVGDEVVAAIYRITSGHW--------RSNLARGGKAEPCSLTEEIEELAIKAAKALGLD-VAGVDLLESEDGLL--V 248
|
250 260 270
....*....|....*....|....*....|
gi 447049177 297 IEVNPRVSRSSalASKATGYPIA-KLAAKI 325
Cdd:TIGR00768 249 NEVNANPEFKN--SVKTTGVNIAgKLLDYI 276
|
|
| PLN02257 |
PLN02257 |
phosphoribosylamine--glycine ligase |
642-800 |
7.04e-05 |
|
phosphoribosylamine--glycine ligase
Pssm-ID: 177899 [Multi-domain] Cd Length: 434 Bit Score: 46.66 E-value: 7.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 642 LAEPLAKAGVTILG--TQVADLDRAedRDLFEQALKELDIPQPPGQTATNEEEAALAARKIGFPVLVRPSYVLGGR---- 715
Cdd:PLN02257 78 LADDLVKAGIPTFGpsAEAAALEGS--KNFMKDLCDKYKIPTAKYETFTDPAAAKKYIKEQGAPIVVKADGLAAGKgvvv 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 716 AMEIVENEEDLRSYMRTAVKASPDHPVLVDSYIVGQECEVDAISDGENVL-IPGIMEHiERAGvhSGDS------MAVYP 788
Cdd:PLN02257 156 AMTLEEAYEAVDSMLVKGAFGSAGSEVVVEEFLDGEEASFFALVDGENAIpLESAQDH-KRVG--DGDTgpntggMGAYS 232
|
170
....*....|....*..
gi 447049177 789 P-----QTLSQKVQETI 800
Cdd:PLN02257 233 PapvltPELESKVMETI 249
|
|
| PatZN |
COG1042 |
Acyl-CoA synthetase (NDP forming) [Energy production and conversion]; |
660-704 |
1.05e-04 |
|
Acyl-CoA synthetase (NDP forming) [Energy production and conversion];
Pssm-ID: 440664 [Multi-domain] Cd Length: 708 Bit Score: 46.27 E-value: 1.05e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447049177 660 DLDRAEDRDLFEQALKE----LD------------IPQPPGQTATNEEEAALAARKIGFPV 704
Cdd:COG1042 467 DPDRERARAIIEAALAEgrgvLTeaeakallaaygIPVVPTRLARSAEEAVAAAEEIGYPV 527
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
121-279 |
1.09e-04 |
|
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439797 [Multi-domain] Cd Length: 353 Bit Score: 45.84 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 121 SAIDQAEDRDLFKQLMEELNQPIPESEIVNTVEEAVAFAATIGYPVIVRPAfTLG--GTGGGMCANEEELREIAEnglKL 198
Cdd:COG0026 82 EALEIAQDRLLEKAFLAELGIPVAPFAAVDSLEDLEAAIAELGLPAVLKTR-RGGydGKGQVVIKSAADLEAAWA---AL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 199 SPVtQCLIErsiaGFKEIEYE----VMRdSADNALVVcnmenFDPV-GIHTgDSI---VFAPAQTMSDYENQMlRDASLS 270
Cdd:COG0026 158 GGG-PCILE----EFVPFERElsviVAR-SPDGEVAT-----YPVVeNVHR-NGIldeSIAPARISEALAAEA-EEIAKR 224
|
....*....
gi 447049177 271 IIRALKIEG 279
Cdd:COG0026 225 IAEALDYVG 233
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
611-860 |
1.10e-04 |
|
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: 45.42 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 611 EPLTFEDVMNVidLEQPKGVIVQF-GGQTAINLAEPLAKAGVTILGTQVAdLDRAEDRDLFEQALKELDIPQPPGQTATN 689
Cdd:TIGR00768 35 INLTFNEGPRA--LAELDVVIVRIvSMFRGLAVLRYLESLGVPVINSSDA-ILNAGDKFLSHQLLAKAGIPLPRTGLAGS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 690 EEEAALAARKIGFPVLVRPSYVLGGRAMEIVENEEDLRSYMRT-AVKASPDHPVLVDSYI-VGQECEVDAISDGENVliP 767
Cdd:TIGR00768 112 PEEALKLIEEIGFPVVLKPVFGSWGRGVSLARDRQAAESLLEHfEQLNGPQNLFLVQEYIkKPGGRDIRVFVVGDEV--V 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 768 GIMEHIE----RAGVHSGdsmAVYPPQTLSQKVQEtIADYTKRlAIGLNCLGmmnIQFVIKDEKVYVIEVNPrasrTVPF 843
Cdd:TIGR00768 190 AAIYRITsghwRSNLARG---GKAEPCSLTEEIEE-LAIKAAK-ALGLDVAG---VDLLESEDGLLVNEVNA----NPEF 257
|
250
....*....|....*....
gi 447049177 844 --LSKVTNIpmaQVATKLI 860
Cdd:TIGR00768 258 knSVKTTGV---NIAGKLL 273
|
|
| PRK14572 |
PRK14572 |
D-alanyl-alanine synthetase A; Provisional |
650-860 |
1.97e-04 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173036 [Multi-domain] Cd Length: 347 Bit Score: 44.90 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 650 GVTILGTQVADLDRAEDRDLFEQALKELDIPQPP------GQTATNEEEAALAARKIGFPVLVRPsyVLGGRAMEI--VE 721
Cdd:PRK14572 114 GIPYTGSGVLASALAMDKTRANQIFLQSGQKVAPffelekLKYLNSPRKTLLKLESLGFPQFLKP--VEGGSSVSTykIT 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 722 NEEDLRSYMrtAVKASPDHPVLVDSYIVGQECEVDAIS---DGENVLIPGIMEHIeRAGVHSGDSMAVYP--------PQ 790
Cdd:PRK14572 192 NAEQLMTLL--ALIFESDSKVMSQSFLSGTEVSCGVLEryrGGKRNPIALPATEI-VPGGEFFDFESKYKqggseeitPA 268
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447049177 791 TLSQKVQETIADYTKRLAIGLNCLGMMNIQFVIKDEKVYVIEVN--PRASRT--VPFLSKVTNIPMAQVATKLI 860
Cdd:PRK14572 269 RISDQEMKRVQELAIRAHESLGCKGYSRTDFIIVDGEPHILETNtlPGMTETslIPQQAKAAGINMEEVFTDLI 342
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
661-836 |
2.64e-04 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 44.37 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 661 LDRAEDRdLFE-QALKELDIPQPPGQTATNEEEAALAARKIGFPVLVRpSYVLG--GRAMEIVENEEDLRSymrtAVKAS 737
Cdd:PRK06019 95 LAIAQDR-LTEkQFLDKLGIPVAPFAVVDSAEDLEAALADLGLPAVLK-TRRGGydGKGQWVIRSAEDLEA----AWALL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 738 PDHPVLVDSYiVGQECEVDAI----SDGENVLIPgIMEHIERAGV-HsgdsmAVYPPQTLSQKVQETIADYTKRLAIGLN 812
Cdd:PRK06019 169 GSVPCILEEF-VPFEREVSVIvargRDGEVVFYP-LVENVHRNGIlR-----TSIAPARISAELQAQAEEIASRIAEELD 241
|
170 180
....*....|....*....|....*
gi 447049177 813 CLGMMNIQ-FVIKDEKVYVIEVNPR 836
Cdd:PRK06019 242 YVGVLAVEfFVTGDGELLVNEIAPR 266
|
|
| SucC |
COG0045 |
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA ... |
133-207 |
3.87e-04 |
|
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA synthetase, beta subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 439815 [Multi-domain] Cd Length: 388 Bit Score: 43.89 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 133 KQLMEELNQPIPESEIVNTVEEAVAFAATIGYPVIV---------RpaftlgGTGGG--MCANEEELREIAEN--GLKLS 199
Cdd:COG0045 9 KELLAKYGVPVPRGIVATTPEEAVAAAEELGGPPVVvkaqvhaggR------GKAGGvkLAKSPEEAREAAEEilGMTLV 82
|
90
....*....|....*..
gi 447049177 200 ---------PVTQCLIE 207
Cdd:COG0045 83 thqtgpkgkPVNKVLVE 99
|
|
| PRK14569 |
PRK14569 |
D-alanyl-alanine synthetase A; Provisional |
666-845 |
6.36e-04 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173033 [Multi-domain] Cd Length: 296 Bit Score: 43.13 E-value: 6.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 666 DRDLFEQALKELDIPQPPGQTATNEeeaALAARKIGFPVLVRPSYVLGGRAMEIVENEEDLRSYMRTAVKASpdhPVLVD 745
Cdd:PRK14569 98 DKMISKEILMHHRMPTPMAKFLTDK---LVAEDEISFPVAVKPSSGGSSIATFKVKSIQELKHAYEEASKYG---EVMIE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 746 SYIVGQECEVDAISDG--ENVLIPGIMEHIERAGVHSGDSMaVYPPQTLSQKVQETIADYTKRLAIGLNCLGMMNIQFVI 823
Cdd:PRK14569 172 QWVTGKEITVAIVNDEvySSVWIEPQNEFYDYESKYSGKSI-YHSPSGLCEQKELEVRQLAKKAYDLLGCSGHARVDFIY 250
|
170 180
....*....|....*....|...
gi 447049177 824 KDE-KVYVIEVNPRASRTVPFLS 845
Cdd:PRK14569 251 DDRgNFYIMEINSSPGMTDNSLS 273
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
150-301 |
7.29e-04 |
|
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: 41.92 E-value: 7.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 150 NTVEEAVAFAATIGYPVIVRPAftLGGTGGGM--CANEEELREIAENGLKLSPVTqcLIERSIAGfKEIEYEVMRDSADN 227
Cdd:pfam07478 23 NPKEWCAQVEEALGYPVFVKPA--RLGSSVGVskVESREELQAAIEEAFQYDEKV--LVEEGIEG-REIECAVLGNEDPE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 228 AL----VVCNMENFDpvgIHT----GDSIVFAPAQtMSDYENQMLRDASLSIIRALKIEGGCNVQLALDPhSFKYYVIEV 299
Cdd:pfam07478 98 VSpvgeIVPSGGFYD---YEAkyidDSAQIVVPAD-LEEEQEEQIQELALKAYKALGCRGLARVDFFLTE-DGEIVLNEV 172
|
..
gi 447049177 300 NP 301
Cdd:pfam07478 173 NT 174
|
|
| PatZN |
COG1042 |
Acyl-CoA synthetase (NDP forming) [Energy production and conversion]; |
133-166 |
7.29e-04 |
|
Acyl-CoA synthetase (NDP forming) [Energy production and conversion];
Pssm-ID: 440664 [Multi-domain] Cd Length: 708 Bit Score: 43.57 E-value: 7.29e-04
10 20 30
....*....|....*....|....*....|....
gi 447049177 133 KQLMEELNQPIPESEIVNTVEEAVAFAATIGYPV 166
Cdd:COG1042 494 KALLAAYGIPVVPTRLARSAEEAVAAAEEIGYPV 527
|
|
| sucC |
PRK00696 |
ADP-forming succinate--CoA ligase subunit beta; |
133-207 |
9.70e-04 |
|
ADP-forming succinate--CoA ligase subunit beta;
Pssm-ID: 234813 [Multi-domain] Cd Length: 388 Bit Score: 42.77 E-value: 9.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 133 KQLMEELNQPIPESEIVNTVEEAVAFAATI-GYPVIVRPAFTLGGTG--GG--MCANEEELREIAEN--GLKLS------ 199
Cdd:PRK00696 9 KELFAKYGVPVPRGIVATTPEEAVEAAEELgGGVWVVKAQVHAGGRGkaGGvkLAKSPEEAREFAKQilGMTLVthqtgp 88
|
90
....*....|.
gi 447049177 200 ---PVTQCLIE 207
Cdd:PRK00696 89 kgqPVNKVLVE 99
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
142-304 |
3.25e-03 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 41.37 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 142 PIPESEIVNTVEEAVAFAATIGYPVIVRPAFTLGGTGGGMCANEEELREIAeNGLKLSPVTQCLIERSIAGfKEIEYEVM 221
Cdd:PRK02186 121 DVPRTHALALRAVALDALDGLTYPVVVKPRMGSGSVGVRLCASVAEAAAHC-AALRRAGTRAALVQAYVEG-DEYSVETL 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 222 RDSADNALVVCnmenfdpVGIHTGDSIVF--------APAQTMSdyeNQMLRDASLSIIRALKIE-GGCNVQLALdpHSF 292
Cdd:PRK02186 199 TVARGHQVLGI-------TRKHLGPPPHFveighdfpAPLSAPQ---RERIVRTVLRALDAVGYAfGPAHTELRV--RGD 266
|
170
....*....|..
gi 447049177 293 KYYVIEVNPRVS 304
Cdd:PRK02186 267 TVVIIEINPRLA 278
|
|
| PRK06849 |
PRK06849 |
hypothetical protein; Provisional |
668-837 |
4.07e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235876 [Multi-domain] Cd Length: 389 Bit Score: 40.80 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 668 DLFEQAlKELDIPQPPGQTATNEEEA-ALAARKIGFPVLVRPSYVLGGRAMEIVENEEDLRSYMrtavkASPDHPVLVDS 746
Cdd:PRK06849 119 EFAEQA-RSLGLSVPKTYLITDPEAIrNFMFKTPHTPYVLKPIYSRFVRRVDLLPKEAALKELP-----ISKDNPWVMQE 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447049177 747 YIVGQE-CEVDAISDGEnVLIPGIMEHIERAGVHSGDSMA-VYPPQtlsqkvqetIADYTKRLAIGLNCLGMMNIQFvIK 824
Cdd:PRK06849 193 FIQGKEyCSYSIVRSGE-LRAHSCYKPEYCAGSGAQIAFQpINHPR---------IEEFVTHFVKELNYTGQISFDF-IE 261
|
170
....*....|....*
gi 447049177 825 DE--KVYVIEVNPRA 837
Cdd:PRK06849 262 TEngDAYPIECNPRT 276
|
|
| ATP-grasp_5 |
pfam13549 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
133-166 |
6.26e-03 |
|
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 463918 [Multi-domain] Cd Length: 221 Bit Score: 39.38 E-value: 6.26e-03
10 20 30
....*....|....*....|....*....|....
gi 447049177 133 KQLMEELNQPIPESEIVNTVEEAVAFAATIGYPV 166
Cdd:pfam13549 16 KALLAAYGIPVVPTRLARSPEEAVAAAEEIGYPV 49
|
|
| ATP-grasp_2 |
pfam08442 |
ATP-grasp domain; |
133-194 |
6.80e-03 |
|
ATP-grasp domain;
Pssm-ID: 400651 [Multi-domain] Cd Length: 202 Bit Score: 39.17 E-value: 6.80e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447049177 133 KQLMEELNQPIPESEIVNTVEEAVAFAATIGYPVIVRPAFTL-GGTG--GG--MCANEEELREIAEN 194
Cdd:pfam08442 8 KEIFAKYGIPVPRGEVATSPEEAEEIAKKLGGKVYVVKAQVLaGGRGkaGGvkLAKSPEEAKEVAKE 74
|
|
| |
