|
Name |
Accession |
Description |
Interval |
E-value |
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
1-1055 |
0e+00 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 2021.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 1 MPKRTDIKKIMVIGSGPIIIGQAAEFDYAGTQACLALKEEGYEVVLVNSNPATIMTDKEIADHVYIEPITLEFVSRILRK 80
Cdd:PRK05294 1 MPKRTDIKKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 81 ERPDALLPTLGGQTGLNMAMELSESGILDELNVELLGTKLSAIDQAEDRDLFKQLMEELEQPIPESEIVNTVEQAVAFAK 160
Cdd:PRK05294 81 ERPDAILPTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 161 RIGYPIIVRPAFTLGGTGGGMCDTEEELRQIAENGLKLSPVTQCLIEKSIAGFKEIEYEVMRDSADNAIVVCNMENFDPV 240
Cdd:PRK05294 161 EIGYPVIIRPSFTLGGTGGGIAYNEEELEEIVERGLDLSPVTEVLIEESLLGWKEYEYEVMRDKNDNCIIVCSIENIDPM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 241 GIHTGDSIVFAPSQTLSDYEYQMLRDASLKIIRALKIE-GGCNVQLALDPHSFNYYVIEVNPRVSRSSALASKATGYPIA 319
Cdd:PRK05294 241 GVHTGDSITVAPAQTLTDKEYQMLRDASIAIIREIGVEtGGCNVQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPIA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 320 KLAAKIAVGLTLDEMKNPVTGTTYAEFEPALDYVVSKIPRWPFDKFEKGARELGTQMKATGEVMAIGRNIEESLLKAVRS 399
Cdd:PRK05294 321 KVAAKLAVGYTLDEIKNDITGKTPASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALRS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 400 LEIGAYHNELEELSHVSDLELTKKMVHAQDDRLFYLSEAIRRGYSIEELQSLTKIDLFFLDKLLHIIEIETALESH--VD 477
Cdd:PRK05294 401 LEIGVTGLDEDLFEEESLEELREELKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELKENglPL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 478 NVAVLKEAKQNGFSDRKIAALWGQTEQAIADFRRANQIVPVYKMVDTCAAEFESHTPYFYSTYEVENESNVSKKPSVLVL 557
Cdd:PRK05294 481 DAELLREAKRLGFSDARIAKLLGVTEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYEEECESNPSDRKKVLVL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 558 GSGPIRIGQGVEFDYATVHSVKAIQAAGYEAIIMNSNPETVSTDFSVSDKLYFEPLTLEDVMNVIDLENPIGVIVQFGGQ 637
Cdd:PRK05294 561 GSGPNRIGQGIEFDYCCVHAVLALREAGYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKPKGVIVQFGGQ 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 638 TAINLAEPLTKQGVKILGTTIEDLDRAENRDLFEQALQELAIPQPPGDTATSAEEAVVIADRIGYPVLVRPSYVLGGRAM 717
Cdd:PRK05294 641 TPLKLAKALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPVLVRPSYVLGGRAM 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 718 EIVENQKDLEDYMRHAVKASPEHPVLVDSYLLG-QECEVDAICDGKTVLIPGIMEHIERAGVHSGDSMAVYPPQYLSQEI 796
Cdd:PRK05294 721 EIVYDEEELERYMREAVKVSPDHPVLIDKFLEGaIEVDVDAICDGEDVLIGGIMEHIEEAGVHSGDSACSLPPQTLSEEI 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 797 QATIADYTKKLALGLNCVGMMNIQFVIHENRVYVIEVNPRASRTVPFLSKITGIPMAQVATKAILGEKLTDLGYQDGLYP 876
Cdd:PRK05294 801 IEEIREYTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKIAARVMLGKKLAELGYTKGLIP 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 877 esKQVHVKAPVFSFTKLQKVDTYLGPEMKSTGEVMGSDYYLEKALYKAFEASGLHLPSYGAVLFTIADETKEEALEIAKR 956
Cdd:PRK05294 881 --PYVAVKEAVFPFNKFPGVDPLLGPEMKSTGEVMGIDRTFGEAFAKAQLAAGNRLPTSGTVFLSVRDRDKEEVVELAKR 958
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 957 FSAIGYSLVATEGTADFLAKHQLPVKKVTKISnpEGE-TVLDVIRNGNAQVVINTMDKNrsSANQDGFSIRREAVEHGIP 1035
Cdd:PRK05294 959 LLELGFKILATSGTAKFLREAGIPVELVNKVH--EGRpHIVDLIKNGEIDLVINTPTGR--QAIRDGFSIRRAALEYKVP 1034
|
1050 1060
....*....|....*....|
gi 727116390 1036 LFTSLDTANAILKVLESRAF 1055
Cdd:PRK05294 1035 YITTLAGARAAVKAIEALKF 1054
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
2-1050 |
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: 1674.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 2 PKRTDIKKIMVIGSGPIIIGQAAEFDYAGTQACLALKEEGYEVVLVNSNPATIMTDKEIADHVYIEPITLEFVSRILRKE 81
Cdd:TIGR01369 1 PKRTDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 82 RPDALLPTLGGQTGLNMAMELSESGILDELNVELLGTKLSAIDQAEDRDLFKQLMEELEQPIPESEIVNTVEQAVAFAKR 161
Cdd:TIGR01369 81 RPDAILPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 162 IGYPIIVRPAFTLGGTGGGMCDTEEELRQIAENGLKLSPVTQCLIEKSIAGFKEIEYEVMRDSADNAIVVCNMENFDPVG 241
Cdd:TIGR01369 161 IGYPVIVRPAFTLGGTGGGIAYNREELKEIAERALSASPINQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPMG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 242 IHTGDSIVFAPSQTLSDYEYQMLRDASLKIIRALKIEGGCNVQLALDPHSFNYYVIEVNPRVSRSSALASKATGYPIAKL 321
Cdd:TIGR01369 241 VHTGDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 322 AAKIAVGLTLDEMKNPVTGTTYAEFEPALDYVVSKIPRWPFDKFEKGARELGTQMKATGEVMAIGRNIEESLLKAVRSLE 401
Cdd:TIGR01369 321 AAKLAVGYTLDELKNPVTGTTPASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSLE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 402 IGAYHNELEELSHVSDLELTKKMVHAQDDRLFYLSEAIRRGYSIEELQSLTKIDLFFLDKLLHIIEIETALESHV---DN 478
Cdd:TIGR01369 401 IGATGFDLPDREVEPDEDLWRALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEVKltdLD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 479 VAVLKEAKQNGFSDRKIAALWGQTEQAIADFRRANQIVPVYKMVDTCAAEFESHTPYFYSTYEVE-NESNVSKKPSVLVL 557
Cdd:TIGR01369 481 PELLRRAKKLGFSDAQIARLIGVTEAEVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGErDDVPFTDKKKVLVL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 558 GSGPIRIGQGVEFDYATVHSVKAIQAAGYEAIIMNSNPETVSTDFSVSDKLYFEPLTLEDVMNVIDLENPIGVIVQFGGQ 637
Cdd:TIGR01369 561 GSGPNRIGQGVEFDYCCVHAVLALRELGYETIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEKPEGVIVQFGGQ 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 638 TAINLAEPLTKQGVKILGTTIEDLDRAENRDLFEQALQELAIPQPPGDTATSAEEAVVIADRIGYPVLVRPSYVLGGRAM 717
Cdd:TIGR01369 641 TPLNLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVRPSYVLGGRAM 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 718 EIVENQKDLEDYMRHAVKASPEHPVLVDSYL-LGQECEVDAICDGKTVLIPGIMEHIERAGVHSGDSMAVYPPQYLSQEI 796
Cdd:TIGR01369 721 EIVYNEEELRRYLEEAVAVSPEHPVLIDKYLeDAVEVDVDAVSDGEEVLIPGIMEHIEEAGVHSGDSTCVLPPQTLSAEI 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 797 QATIADYTKKLALGLNCVGMMNIQFVIHENRVYVIEVNPRASRTVPFLSKITGIPMAQVATKAILGEKLTDLGYqdGLYP 876
Cdd:TIGR01369 801 VDRIKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAVRVMLGKKLEELGV--GKEK 878
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 877 ESKQVHVKAPVFSFTKLQKVDTYLGPEMKSTGEVMGSDYYLEKALYKAFEASGLHLPSYGAVLFTIADETKEEALEIAKR 956
Cdd:TIGR01369 879 EPKYVAVKEPVFSFSKLAGVDPVLGPEMKSTGEVMGIGRDLAEAFLKAQLSSGNRIPKKGSVLLSVRDKDKEELLDLARK 958
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 957 FSAIGYSLVATEGTADFLAKHQLPVKKVTKISNpEGETVLDVIRNGNAQVVINTMDKNRSSAnQDGFSIRREAVEHGIPL 1036
Cdd:TIGR01369 959 LAEKGYKLYATEGTAKFLGEAGIKPELVLKVSE-GRPNILDLIKNGEIELVINTTSKGAGTA-TDGYKIRREALDYGVPL 1036
|
1050
....*....|....
gi 727116390 1037 FTSLDTANAILKVL 1050
Cdd:TIGR01369 1037 ITTLNTAEAFAEAL 1050
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
1-1060 |
0e+00 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 1568.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 1 MPKRTDIKKIMVIGSGPIIIGQAAEFDYAGTQACLALKEEGYEVVLVNSNPATIMTDKEIADHVYIEPITLEFVSRILRK 80
Cdd:PRK12815 1 MPKDTDIQKILVIGSGPIVIGQAAEFDYSGTQACLALKEEGYQVVLVNPNPATIMTDPAPADTVYFEPLTVEFVKRIIAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 81 ERPDALLPTLGGQTGLNMAMELSESGILDELNVELLGTKLSAIDQAEDRDLFKQLMEELEQPIPESEIVNTVEQAVAFAK 160
Cdd:PRK12815 81 EKPDALLATLGGQTALNLAVKLHEDGILEQYGVELLGTNIEAIQKGEDRERFRALMKELGEPVPESEIVTSVEEALAFAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 161 RIGYPIIVRPAFTLGGTGGGMCDTEEELRQIAENGLKLSPVTQCLIEKSIAGFKEIEYEVMRDSADNAIVVCNMENFDPV 240
Cdd:PRK12815 161 KIGFPIIVRPAYTLGGTGGGIAENLEELEQLFKQGLQASPIHQCLLEESIAGWKEIEYEVMRDRNGNCITVCNMENIDPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 241 GIHTGDSIVFAPSQTLSDYEYQMLRDASLKIIRALKIEGGCNVQLALDPHSFNYYVIEVNPRVSRSSALASKATGYPIAK 320
Cdd:PRK12815 241 GIHTGDSIVVAPSQTLTDDEYQMLRSASLKIISALGVVGGCNIQFALDPKSKQYYLIEVNPRVSRSSALASKATGYPIAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 321 LAAKIAVGLTLDEMKNPVTGTTYAEFEPALDYVVSKIPRWPFDKFEKGARELGTQMKATGEVMAIGRNIEESLLKAVRSL 400
Cdd:PRK12815 321 IAAKLAVGYTLNELKNPVTGLTYASFEPALDYVVVKFPRWPFDKFGYADRTLGTQMKATGEVMAIGRNFESAFQKALRSL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 401 EIGayHNELE---ELSHVSDLELTKKMVHAQDDRLFYLSEAIRRGYSIEELQSLTKIDLFFLDKLLHIIEIETALESHVD 477
Cdd:PRK12815 401 EIK--RNGLSlpiELSGKSDEELLQDLRHPDDRRLFALLEALRRGITYEEIHELTKIDPFFLQKFEHIVALEKKLAEDGL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 478 NVA--VLKEAKQNGFSDRKIAALWGQTEQAIADFRRANQIVPVYKMVDTCAAEFESHTPYFYSTYEVENESNVSK-KPSV 554
Cdd:PRK12815 479 DLSadLLRKVKEKGFSDALLAELTGVTEEEVRALRKKLGIRPSYKMVDTCAAEFEAKTPYYYSTYFGESEAEPSSeKKKV 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 555 LVLGSGPIRIGQGVEFDYATVHSVKAIQAAGYEAIIMNSNPETVSTDFSVSDKLYFEPLTLEDVMNVIDLENPIGVIVQF 634
Cdd:PRK12815 559 LILGSGPIRIGQGIEFDYSSVHAAFALKKEGYETIMINNNPETVSTDYDTADRLYFEPLTLEDVLNVAEAENIKGVIVQF 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 635 GGQTAINLAEPLTKQGVKILGTTIEDLDRAENRDLFEQALQELAIPQPPGDTATSAEEAVVIADRIGYPVLVRPSYVLGG 714
Cdd:PRK12815 639 GGQTAINLAKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEEEAFAFAKRIGYPVLIRPSYVIGG 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 715 RAMEIVENQKDLEDYMRHAvkASPEHPVLVDSYLLGQECEVDAICDGKTVLIPGIMEHIERAGVHSGDSMAVYPPQYLSQ 794
Cdd:PRK12815 719 QGMAVVYDEPALEAYLAEN--ASQLYPILIDQFIDGKEYEVDAISDGEDVTIPGIIEHIEQAGVHSGDSIAVLPPQSLSE 796
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 795 EIQATIADYTKKLALGLNCVGMMNIQFVIHENRVYVIEVNPRASRTVPFLSKITGIPMAQVATKAILGEKLTDLGYQDGL 874
Cdd:PRK12815 797 EQQEKIRDYAIKIAKKLGFRGIMNIQFVLANDEIYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLGKSLAELGYPNGL 876
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 875 YPESKQVHVKAPVFSFTKLQKVDTYLGPEMKSTGEVMGSDYYLEKALYKAFEASGLHLPSYGAVLFTIADETKEEALEIA 954
Cdd:PRK12815 877 WPGSPFIHVKMPVFSYLKYPGVDNTLGPEMKSTGEVMGIDKDLEEALYKGYEASDLHIPSYGTIFISVRDEDKPEVTKLA 956
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 955 KRFSAIGYSLVATEGTADFLAKHQLPVKKVTKISNPEGeTVLDVIRNGNAQVVINTmdKNRSSANQDGFSIRREAVEHGI 1034
Cdd:PRK12815 957 RRFAQLGFKLLATEGTANWLAEEGITTGVVEKVQEGSP-SLLERIKQHRIVLVVNT--SLSDSASEDAIKIRDEALSTHI 1033
|
1050 1060
....*....|....*....|....*.
gi 727116390 1035 PLFTSLDTANAILKVLESRAFTTEAI 1060
Cdd:PRK12815 1034 PVFTELETAQAFLQVLESLALTTQPI 1059
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
3-1060 |
0e+00 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 1195.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 3 KRTDIKKIMVIGSGPIIIGQAAEFDYAGTQACLALKEEGYEVVLVNSNPATIMTDKEIADHVYIEPITLEFVSRILRKER 82
Cdd:PLN02735 19 KRTDLKKIMILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATIMTDPETADRTYIAPMTPELVEQVIAKER 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 83 PDALLPTLGGQTGLNMAMELSESGILDELNVELLGTKLSAIDQAEDRDLFKQLMEELEQPIPESEIVNTVEQAVAFAKRI 162
Cdd:PLN02735 99 PDALLPTMGGQTALNLAVALAESGILEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPPSGIATTLDECFEIAEDI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 163 G-YPIIVRPAFTLGGTGGGMCDTEEELRQIAENGLKLSPVTQCLIEKSIAGFKEIEYEVMRDSADNAIVVCNMENFDPVG 241
Cdd:PLN02735 179 GeFPLIIRPAFTLGGTGGGIAYNKEEFETICKAGLAASITSQVLVEKSLLGWKEYELEVMRDLADNVVIICSIENIDPMG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 242 IHTGDSIVFAPSQTLSDYEYQMLRDASLKIIRALKIE-GGCNVQLALDPHSFNYYVIEVNPRVSRSSALASKATGYPIAK 320
Cdd:PLN02735 259 VHTGDSITVAPAQTLTDKEYQRLRDYSVAIIREIGVEcGGSNVQFAVNPVDGEVMIIEMNPRVSRSSALASKATGFPIAK 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 321 LAAKIAVGLTLDEMKNPVTGTTYAEFEPALDYVVSKIPRWPFDKFEKGARELGTQMKATGEVMAIGRNIEESLLKAVRSL 400
Cdd:PLN02735 339 MAAKLSVGYTLDQIPNDITLKTPASFEPSIDYVVTKIPRFAFEKFPGSQPILTTQMKSVGEAMALGRTFQESFQKALRSL 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 401 EIG------AYHNELEelshvSDLELTK-KMVHAQDDRLFYLSEAIRRGYSIEELQSLTKIDLFFLDKLLHIIEIETALE 473
Cdd:PLN02735 419 ETGfsgwgcAKVKELD-----WDWEQLKyKLRVPNPDRIHAIYAAMKKGMTVDEIHELTFIDPWFLTQLKELVDVEQFLK 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 474 S-HVDNVAV--LKEAKQNGFSDRKIAALWGQTEQAIADFRRANQIVPVYKMVDTCAAEFESHTPYFYSTYEVENESNVSK 550
Cdd:PLN02735 494 SrSLSELSKddFYEVKRRGFSDKQIAFATKSTEKEVRSKRLSLGVTPSYKRVDTCAAEFEANTPYMYSSYDGECESAPTN 573
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 551 KPSVLVLGSGPIRIGQGVEFDYATVHSVKAIQAAGYEAIIMNSNPETVSTDFSVSDKLYFEPLTLEDVMNVIDLENPIGV 630
Cdd:PLN02735 574 KKKVLILGGGPNRIGQGIEFDYCCCHASFALQDAGYETIMMNSNPETVSTDYDTSDRLYFEPLTVEDVLNVIDLERPDGI 653
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 631 IVQFGGQTAINLAEPLTKQ-------------GVKILGTTIEDLDRAENRDLFEQALQELAIPQPPGDTATSAEEAVVIA 697
Cdd:PLN02735 654 IVQFGGQTPLKLALPIQKYldknpppsasgngNVKIWGTSPDSIDAAEDRERFNAILNELKIEQPKGGIARSEADALAIA 733
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 698 DRIGYPVLVRPSYVLGGRAMEIVENQKDLEDYMRHAVKASPEHPVLVDSYLL-GQECEVDAICDGK-TVLIPGIMEHIER 775
Cdd:PLN02735 734 KRIGYPVVVRPSYVLGGRAMEIVYSDDKLKTYLETAVEVDPERPVLVDKYLSdATEIDVDALADSEgNVVIGGIMEHIEQ 813
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 776 AGVHSGDSMAVYPPQYLSQEIQATIADYTKKLALGLNCVGMMNIQF-VIHENRVYVIEVNPRASRTVPFLSKITGIPMAQ 854
Cdd:PLN02735 814 AGVHSGDSACSLPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYaITPSGEVYIIEANPRASRTVPFVSKAIGHPLAK 893
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 855 VATKAILGEKLTDLGYQDGLYPesKQVHVKAPVFSFTKLQKVDTYLGPEMKSTGEVMGSDYYLEKALYKAFEASGLHLPS 934
Cdd:PLN02735 894 YASLVMSGKSLKDLGFTEEVIP--AHVSVKEAVLPFDKFQGCDVLLGPEMRSTGEVMGIDYEFSKAFAKAQIAAGQRLPL 971
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 935 YGAVLFTIADETKEEALEIAKRFSAIGYSLVATEGTADFLAKHQLPVKKVTKISnpEGET-VLDVIRNGNAQVVINTmdK 1013
Cdd:PLN02735 972 SGTVFISLNDLTKPHLVPIARGFLELGFRIVSTSGTAHFLELAGIPVERVLKLH--EGRPhAGDMLANGQIQLMVIT--S 1047
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|..
gi 727116390 1014 NRSSANQ-DGFSIRREAVEHGIPLFTSLD----TANAIlKVLESRAFTTEAI 1060
Cdd:PLN02735 1048 SGDALDQkDGRQLRRMALAYKVPIITTVAgalaTAQAV-KSLKECPIEMIAL 1098
|
|
| 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: 801.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 13 IGSGPIIIGQAAEFDYAGTQACLALKEEGYEVVLVNSNPATIMTDKEIADHVYIEPITLEFVSRILRKERPDALLPTLGG 92
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 93 QTGLNMAMELSESGILDelNVELLGTKLSAIDQAEDRDLFKQLMEELEQPIPESEIVNTVEQAVAFAKRIGYPIIVRPAF 172
Cdd:COG0458 81 QTALNLAVELEEAGILE--GVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 173 TLGGTGGGMCDTEEELRQIAENGLKLSPVTQCLIEKSIAGFKEIEYEVMRDSADNAIVVCNMENFDPVGIHTGDSIVFAP 252
Cdd:COG0458 159 VLGGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRDGEDNVIIVGIMEHIEPAGVHSGDSICVAP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 253 SQTLSDYEYQMLRDASLKIIRALKIEGGCNVQLALDphSFNYYVIEVNPRVSRSSALASKATGYPIAKLAAKIAVGLTLD 332
Cdd:COG0458 239 PQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVD--DGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 333 EMKNPvtgttyAEFEPALDYVVSKIPRWPFDKFEKGARELGTQMKATGEVMAIGRNIEESLLKAVRSLEIGAYHNELEEL 412
Cdd:COG0458 317 ELGND------TGFEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGTVLLSL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 413 sHVSDLELTKKMVHAQDDRLFYLSEAIRRGYSIEELQSLTKIDLFFLDKLLHIIEIETALESHVDNVAVLKEAKQNGFSD 492
Cdd:COG0458 391 -VADDDKEEALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDEIELEEIILVINTLLGAKSLGDSD 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 727116390 493 RKIAALWGQTEQAIADFRRANQIVPVYKMVDTCAAEFESHTPYFYSTYEVENESNVSKKPSVLVLGS 559
Cdd:COG0458 470 GIIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYYYSTYEYENESEETEEPKVVVIGS 536
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
557-1059 |
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: 720.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 557 LGSGPIRIGQGVEFDYATVHSVKAIQAAGYEAIIMNSNPETVSTDFSVSDKLYFEPLTLEDVMNVIDLENPIGVIVQFGG 636
Cdd:COG0458 1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 637 QTAINLAEPLTK----QGVKILGTTIEDLDRAENRDLFEQALQELAIPQPPGDTATSAEEAVVIADRIGYPVLVRPSYVL 712
Cdd:COG0458 81 QTALNLAVELEEagilEGVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSYVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 713 GGRAMEIVENQKDLEDYMRHAVKASPEHPVLVDSYLLG-QECEVDAICDGK-TVLIPGIMEHIERAGVHSGDSMAVYPPQ 790
Cdd:COG0458 161 GGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGaKEIEVDVVRDGEdNVIIVGIMEHIEPAGVHSGDSICVAPPQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 791 YLSQEIQATIADYTKKLALGLNCVGMMNIQFVIHENRVYVIEVNPRASRTVPFLSKITGIPMAQVATKAILGEKLTDLGY 870
Cdd:COG0458 241 TLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTLDELGN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 871 QDGLYPESKQVHVKAPVFSFTKLQKVDTYLGPEMKSTGEVMGSDYYLEKALYKAFEASGLHLPsyGAVLFT-IADETKEE 949
Cdd:COG0458 321 DTGFEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLP--GTVLLSlVADDDKEE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 950 ALEIAKRFSAIGYSLVATEGTADFLAKHQLPVKKVTKISNpEGETVLDVIRNGNAQVVINTMDKNRSSAnQDGFSIRREA 1029
Cdd:COG0458 399 ALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSE-GRPIIVDEIELEEIILVINTLLGAKSLG-DSDGIIRRAL 476
|
490 500 510
....*....|....*....|....*....|
gi 727116390 1030 VEHGIPLFTSLDTANAILKVLESRAFTTEA 1059
Cdd:COG0458 477 AAKVPYVTTLAAAAAAALAIKAVETEAGEF 506
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
128-332 |
3.49e-95 |
|
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: 300.76 E-value: 3.49e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 128 DRDLFKQLMEELEQPIPESEI--VNTVEQAVAFAKRIGYPIIVRPAFTLGGTGGGMCDTEEELRQIAENGLKLSPVT--- 202
Cdd:pfam02786 1 DKVLFKAAMKEAGVPTVPGTAgpVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAfgn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 203 -QCLIEKSIAGFKEIEYEVMRDSADNAIVVCNMENFDPVgiHTGDSIVFAPSQTLSDYEYQMLRDASLKIIRALKIEGGC 281
Cdd:pfam02786 81 pQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 727116390 282 NVQLALDPHSFNYYVIEVNPRVSRSSALASKATGYPIAKLAAKIAVGLTLD 332
Cdd:pfam02786 159 TVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| CPSase_L_D3 |
smart01096 |
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ... |
420-540 |
6.99e-57 |
|
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: 191.89 E-value: 6.99e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 420 LTKKMVHAQDDRLFYLSEAIRRGYSIEELQSLTKIDLFFLDKLLHIIEIETALESH---VDNVAVLKEAKQNGFSDRKIA 496
Cdd:smart01096 1 LLEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKGgldELDADLLRKAKRLGFSDRQIA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 727116390 497 ALWGQTEQAIADFRRANQIVPVYKMVDTCAAEFESHTPYFYSTY 540
Cdd:smart01096 81 KLLGVTEAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
|
|
| MGS_CPS_II |
cd01424 |
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate ... |
936-1048 |
3.14e-42 |
|
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: 149.55 E-value: 3.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 936 GAVLFTIADETKEEALEIAKRFSAIGYSLVATEGTADFLAKHQLPVKKVTKISnpEGE-TVLDVIRNGNAQVVINTMDKN 1014
Cdd:cd01424 1 GTVFISVADRDKPEAVEIAKRLAELGFKLVATEGTAKYLQEAGIPVEVVNKVS--EGRpNIVDLIKNGEIQLVINTPSGK 78
|
90 100 110
....*....|....*....|....*....|....
gi 727116390 1015 RssANQDGFSIRREAVEHGIPLFTSLDTANAILK 1048
Cdd:cd01424 79 R--AIRDGFSIRRAALEYKVPYFTTLDTARAAVE 110
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
667-865 |
2.66e-34 |
|
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: 130.89 E-value: 2.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 667 RDLFEQALQELAIPQPPG--DTATSAEEAVVIADRIGYPVLVRPSYVLGGRAMEIVENQKDLEDYMRHAVKASPE----H 740
Cdd:pfam02786 2 KVLFKAAMKEAGVPTVPGtaGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAafgnP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 741 PVLVDSYLLG-QECEVDAICDGK-TVLIPGIMEHIERagVHSGDSMAVYPPQYLSQEIQATIADYTKKLALGLNCVGMMN 818
Cdd:pfam02786 82 QVLVEKSLKGpKHIEYQVLRDAHgNCITVCNRECSDQ--RRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGT 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 727116390 819 IQFVIH--ENRVYVIEVNPRASRTVPFLSKITGIPMAQVATKAILGEKL 865
Cdd:pfam02786 160 VEFALDpfSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPL 208
|
|
| CPSase_L_D3 |
pfam02787 |
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate ... |
422-498 |
2.00e-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: 112.08 E-value: 2.00e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 727116390 422 KKMVHAQDDRLFYLSEAIRRGYSIEELQSLTKIDLFFLDKLLHIIEIETALESHVD--NVAVLKEAKQNGFSDRKIAAL 498
Cdd:pfam02787 1 EELRTPTDERLFAIAEALRRGYSVEEIHELTKIDPWFLDKIKNIVELEKELKEAGLdlDAELLREAKRLGFSDRQIAKL 79
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
655-864 |
5.54e-27 |
|
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440208 [Multi-domain] Cd Length: 263 Bit Score: 111.50 E-value: 5.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 655 GTTIEDLDRAENRDLFEQALQELAIPQPPGDTATSAEEAVVIADRIGYPVLVRPSYVLGGRAMEIVENQKDLEDYMRHAV 734
Cdd:COG0439 43 GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEAR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 735 K----ASPEHPVLVDSYLLGQECEVDAICDGKTVLIPGIMEHIeRAGVHSGDSMAVYPPQyLSQEIQATIADYTKKL--A 808
Cdd:COG0439 123 AeakaGSPNGEVLVEEFLEGREYSVEGLVRDGEVVVCSITRKH-QKPPYFVELGHEAPSP-LPEELRAEIGELVARAlrA 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 727116390 809 LGLNCvGMMNIQFVIHEN-RVYVIEVNPRAS--RTVPFLSKITGIPMAQVATKAILGEK 864
Cdd:COG0439 201 LGYRR-GAFHTEFLLTPDgEPYLIEINARLGgeHIPPLTELATGVDLVREQIRLALGEP 258
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
71-329 |
5.25e-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: 108.42 E-value: 5.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 71 LEFVSRILRKERPDALLPtlGGQTGLNMAMELSEsgildELNveLLGTKLSAIDQAEDRDLFKQLMEELEQPIPESEIVN 150
Cdd:COG0439 6 IAAAAELARETGIDAVLS--ESEFAVETAAELAE-----ELG--LPGPSPEAIRAMRDKVLMREALAAAGVPVPGFALVD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 151 TVEQAVAFAKRIGYPIIVRPAftlGGTGG-GM--CDTEEEL----RQIAENGLKLSPVTQCLIEKSIAGfKEIEYEVMrd 223
Cdd:COG0439 77 SPEEALAFAEEIGYPVVVKPA---DGAGSrGVrvVRDEEELeaalAEARAEAKAGSPNGEVLVEEFLEG-REYSVEGL-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 224 SADNAIVVCNM---ENFDPVGIHTGDSivfAPSQtLSDYEYQMLRDASLKIIRALKI-EGGCNVQLALDPHSfNYYVIEV 299
Cdd:COG0439 151 VRDGEVVVCSItrkHQKPPYFVELGHE---APSP-LPEELRAEIGELVARALRALGYrRGAFHTEFLLTPDG-EPYLIEI 225
|
250 260 270
....*....|....*....|....*....|..
gi 727116390 300 NPRVS--RSSALASKATGYPIAKLAAKIAVGL 329
Cdd:COG0439 226 NARLGgeHIPPLTELATGVDLVREQIRLALGE 257
|
|
| MGS |
smart00851 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
949-1038 |
7.00e-24 |
|
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: 96.39 E-value: 7.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 949 EALEIAKRFSAIGYSLVATEGTADFLAKHQLPVkkVTKISNPEGE---TVLDVIRNGNAQVVINTMDKNRSSANQDGFSI 1025
Cdd:smart00851 1 GLVEFAKRLAELGFELLATGGTAKFLREAGLPV--VKTLHPKVHGgipQILDLIKNGEIDLVINTLYPFEAQAHEDGYSI 78
|
90
....*....|...
gi 727116390 1026 RREAVEHGIPLFT 1038
Cdd:smart00851 79 RRAAENIDIPGPT 91
|
|
| MGS |
pfam02142 |
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ... |
949-1038 |
9.03e-23 |
|
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: 93.32 E-value: 9.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 949 EALEIAKRFSAIGYSLVATEGTADFLAKHQLPVKKV---TKISNPEGE-TVLDVIRNGNAQVVINTMDKNRsSANQDGFS 1024
Cdd:pfam02142 1 GLVELAKALVELGFELLATGGTAKFLREAGIPVTEVvekTGEGRPGGRvQIGDLIKNGEIDLVINTLYPFK-ATVHDGYA 79
|
90
....*....|....
gi 727116390 1025 IRREAVEHGIPLFT 1038
Cdd:pfam02142 80 IRRAAENIDIPGPT 93
|
|
| MGS_CPS_I_III |
cd01423 |
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases ... |
937-1038 |
1.61e-17 |
|
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: 79.27 E-value: 1.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 937 AVLFTIADETKEEALEIAKRFSAIGYSLVATEGTADFLAKHQLPVKKVTKISN---PEGETVLDVIRNGNAQVVINTMDK 1013
Cdd:cd01423 2 GILISIGSYSKPELLPTAQKLSKLGYKLYATEGTADFLLENGIPVTPVAWPSEepqNDKPSLRELLAEGKIDLVINLPSN 81
|
90 100
....*....|....*....|....*
gi 727116390 1014 NRSSANQDGFSIRREAVEHGIPLFT 1038
Cdd:cd01423 82 RGKRVLDNDYVMRRAADDFAVPLIT 106
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
36-353 |
5.85e-17 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 84.21 E-value: 5.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 36 ALKEEGYEVVLVNSNPATIMTDKEIADHVYIEP-------ITLEFVSRILRKERPDALLPTlgGQTGLNMameLSEsgIL 108
Cdd:COG3919 23 SLGEAGVRVIVVDRDPLGPAARSRYVDEVVVVPdpgddpeAFVDALLELAERHGPDVLIPT--GDEYVEL---LSR--HR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 109 DEL--NVELLGTKLSAIDQAEDRDLFKQLMEELEQPIPESEIVNTVEQAVAFAKRIGYPIIVRPA--------FTLGGTG 178
Cdd:COG3919 96 DELeeHYRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSADDLDALAEDLGFPVVVKPAdsvgydelSFPGKKK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 179 GGMCDTEEEL----RQIAENGLKlsPVTQCLIEKsiagfkeieyevmrdsADNAIVVCNM---ENFDPVGIHTG-----D 246
Cdd:COG3919 176 VFYVDDREELlallRRIAAAGYE--LIVQEYIPG----------------DDGEMRGLTAyvdRDGEVVATFTGrklrhY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 247 SIVFAPS---QTLSDYEyqmLRDASLKIIRALKIEGGCNVQLALDPHSFNYYVIEVNPRVSRSSALASKAtGYPIAKLAA 323
Cdd:COG3919 238 PPAGGNSaarESVDDPE---LEEAARRLLEALGYHGFANVEFKRDPRDGEYKLIEINPRFWRSLYLATAA-GVNFPYLLY 313
|
330 340 350
....*....|....*....|....*....|..
gi 727116390 324 KIAVGLTLDEMKNPVTGT--TYAEFEPALDYV 353
Cdd:COG3919 314 DDAVGRPLEPVPAYREGVlwRVLPGDLLLRYL 345
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
646-843 |
1.83e-14 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 75.69 E-value: 1.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 646 LTKQGVKILGTTIEDLDRAENRDLFEQALQELAIPQPPGDTATSAE--EAVVIADRIGYPVLVRPSYVLGGRAMEIVENQ 723
Cdd:PRK12767 91 FEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEdfKAALAKGELQFPLFVKPRDGSASIGVFKVNDK 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 724 KDLEDYMRHAVKaspehpVLVDSYLLGQECEVDAICD-GKTVLIPGIMEHIE-RAGvhsGDSMAV---YPPqylsqeiqa 798
Cdd:PRK12767 171 EELEFLLEYVPN------LIIQEFIEGQEYTVDVLCDlNGEVISIVPRKRIEvRAG---ETSKGVtvkDPE--------- 232
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 727116390 799 tIADYTKKLALGLNCVGMMNIQFVIHENRVYVIEVNPRASRTVPF 843
Cdd:PRK12767 233 -LFKLAERLAEALGARGPLNIQCFVTDGEPYLFEINPRFGGGYPL 276
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
83-331 |
3.20e-14 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 76.29 E-value: 3.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 83 PDALLPTLGGQTGLNMAME------------LSESGILDEL----NVELLGTKLSAIDQAEDRDLFKQLMEELEQPI-PE 145
Cdd:PRK07178 53 ADPLAGYLNPRRLVNLAVEtgcdalhpgygfLSENAELAEIcaerGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVtPG 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 146 SE-IVNTVEQAVAFAKRIGYPIIVRPAFTLGGTGGGMCDTEEELRQ-----IAEnGLKLSPVTQCLIEKSIAGFKEIEYE 219
Cdd:PRK07178 133 SEgNLADLDEALAEAERIGYPVMLKATSGGGGRGIRRCNSREELEQnfprvISE-ATKAFGSAEVFLEKCIVNPKHIEVQ 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 220 VMRDSADNAIVV----CNMENfdpvgiHTGDSIVFAPSQTLSDYEYQMLRDASLKIIRALKIEGGCNVQLALDpHSFNYY 295
Cdd:PRK07178 212 ILADSHGNVVHLferdCSIQR------RNQKLIEIAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLD-ADGEVY 284
|
250 260 270
....*....|....*....|....*....|....*.
gi 727116390 296 VIEVNPRVSRSSALASKATGYPIAKLAAKIAVGLTL 331
Cdd:PRK07178 285 FMEMNTRVQVEHTITEEITGIDIVREQIRIASGLPL 320
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
551-875 |
5.08e-12 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 68.80 E-value: 5.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 551 KPSVLVLGSGPIrigqgvefDYATVHSVKAiqaAGYEAIIMNSNPETVS------TDFSVSDKLYFEPLTLEDVMNVIDL 624
Cdd:COG3919 5 RFRVVVLGGDIN--------ALAVARSLGE---AGVRVIVVDRDPLGPAarsryvDEVVVVPDPGDDPEAFVDALLELAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 625 ENPIGVIVQFGGQTAINLAE--PLTKQGVKILGTTIEDLDRAENRDLFEQALQELAIPQPPGDTATSAEEAVVIADRIGY 702
Cdd:COG3919 74 RHGPDVLIPTGDEYVELLSRhrDELEEHYRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSADDLDALAEDLGF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 703 PVLVRPSY--------VLGGRAMEIVENQKDLEDYMRHAVKAspEHPVLV-------DSYLLGQECEVDAicDGKTVLIP 767
Cdd:COG3919 154 PVVVKPADsvgydelsFPGKKKVFYVDDREELLALLRRIAAA--GYELIVqeyipgdDGEMRGLTAYVDR--DGEVVATF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 768 G---IMEHIERAGVHSGdSMAVYPPQylsqeiqatIADYTKKLALGLNCVGMMNIQFVIHE--NRVYVIEVNPRASRTVp 842
Cdd:COG3919 230 TgrkLRHYPPAGGNSAA-RESVDDPE---------LEEAARRLLEALGYHGFANVEFKRDPrdGEYKLIEINPRFWRSL- 298
|
330 340 350
....*....|....*....|....*....|....
gi 727116390 843 FLSKITGIPMAQVATKAILGEKL-TDLGYQDGLY 875
Cdd:COG3919 299 YLATAAGVNFPYLLYDDAVGRPLePVPAYREGVL 332
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
672-853 |
7.21e-12 |
|
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: 67.44 E-value: 7.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 672 QALQELAIPQPPGDTATSAEEAVV--IADRIGYPVLVRPsyVLGG--RAMEIVENQKDLEDYMRHAVKASPEhpVLVDSY 747
Cdd:COG1181 101 RVLAAAGLPTPPYVVLRRGELADLeaIEEELGLPLFVKP--AREGssVGVSKVKNAEELAAALEEAFKYDDK--VLVEEF 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 748 LLGQECEVdAICDGKTVLIPGIMEHIERAGV-------HSGDSMAVYPPQyLSQEIQATIADYTKKLALGLNCVGM---- 816
Cdd:COG1181 177 IDGREVTV-GVLGNGGPRALPPIEIVPENGFydyeakyTDGGTEYICPAR-LPEELEERIQELALKAFRALGCRGYarvd 254
|
170 180 190
....*....|....*....|....*....|....*..
gi 727116390 817 MniqFVIHENRVYVIEVNprasrTVPFLSKITGIPMA 853
Cdd:COG1181 255 F---RLDEDGEPYLLEVN-----TLPGMTPTSLLPKA 283
|
|
| PylC |
COG2232 |
Pyrrolysine biosynthesis ligase PylC and related enzymes, ATP-grasp superfamily [Amino acid ... |
649-863 |
1.43e-11 |
|
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: 67.25 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 649 QGVKILGTTIEDLDRAENRDLFEQALQELAIPQPPgdTATSAEEAvviadriGYPVLVRPSYVLGGRAMEIVENQkdled 728
Cdd:COG2232 95 RRLPLLGNPPEVVRRVKDPLRFFALLDELGIPHPE--TRFEPPPD-------PGPWLVKPIGGAGGWHIRPADSE----- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 729 ymrhavkASPEHPVLVDSYLLGQECEVDAICDGKTVLIPGIMEHIERAG-----VHSGdsmAVYPPQyLSQEIQATIADY 803
Cdd:COG2232 161 -------APPAPGRYFQRYVEGTPASVLFLADGSDARVLGFNRQLIGPAgerpfRYGG---NIGPLA-LPPALAEEMRAI 229
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 804 TKKLALGLNCVGMMNIQFVIHENRVYVIEVNPRASRTVPFLSKITGIPMAQVATKAILGE 863
Cdd:COG2232 230 AEALVAALGLVGLNGVDFILDGDGPYVLEVNPRPQASLDLYEDATGGNLFDAHLRACRGE 289
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
109-328 |
1.54e-11 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 68.09 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 109 DELNVELLGTKLSAIDQAEDRDLFKQLMEELEQP-IPES-EIVNTVEQAVAFAKRIGYPIIVRPAftLGGTGGGM--CDT 184
Cdd:PRK08654 96 EKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPvLPGTeEGIEDIEEAKEIAEEIGYPVIIKAS--AGGGGIGMrvVYS 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 185 EEEL-------RQIAENGLKLSPVtqcLIEKSIAGFKEIEYEVMRDSADNAIvvcnmenfdpvgiHTGDS---------- 247
Cdd:PRK08654 174 EEELedaiestQSIAQSAFGDSTV---FIEKYLEKPRHIEIQILADKHGNVI-------------HLGDRecsiqrrhqk 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 248 -IVFAPSQTLSDYEYQMLRDASLKIIRALKIEGGCNVQLALDphSFNYYVIEVNPRVSRSSALASKATGYPIAKLAAKIA 326
Cdd:PRK08654 238 lIEEAPSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYS--NGNFYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIA 315
|
..
gi 727116390 327 VG 328
Cdd:PRK08654 316 AG 317
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
114-303 |
3.03e-11 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 67.86 E-value: 3.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 114 ELLGTKLSAIDQAEDRDLfkqlmeeleqP-IPESEI-VNTVEQAVAFAKRIGYPIIVRPAftLGGTGGGM--CDTEEELR 189
Cdd:PRK12999 115 RLLGDKVAARNAAIKAGV----------PvIPGSEGpIDDIEEALEFAEEIGYPIMLKAS--AGGGGRGMriVRSEEELE 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 190 QIAENGLKL------SPvtQCLIEKSIAGFKEIEYEVMRDSADNaiVV------CNME-NFDPVgihtgdsIVFAPSQTL 256
Cdd:PRK12999 183 EAFERAKREakaafgND--EVYLEKYVENPRHIEVQILGDKHGN--VVhlyerdCSVQrRHQKV-------VEIAPAPGL 251
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 727116390 257 SDYEYQMLRDASLKIIRALKIEGGCNVQLALDPHSfNYYVIEVNPRV 303
Cdd:PRK12999 252 SEELRERICEAAVKLARAVGYVNAGTVEFLVDADG-NFYFIEVNPRI 297
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
112-328 |
4.12e-11 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 66.31 E-value: 4.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 112 NVELLGTKLSAIDQAEDRDLFKQLMEELEQP-IPESE-IVNTVEQAVAFAKRIGYPIIVRPAFTLGGTGGGMCDTEEELR 189
Cdd:PRK08462 101 NIKFIGPSVEVMALMSDKSKAKEVMKRAGVPvIPGSDgALKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVEDESDLE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 190 QiaengLKLSPVTQCL---------IEKSIAGFKEIEYEVMRDSADNAIVV----CNMENfdpvgiHTGDSIVFAPSQTL 256
Cdd:PRK08462 181 N-----LYLAAESEALsafgdgtmyMEKFINNPRHIEVQILGDKHGNVIHVgerdCSLQR------RHQKLIEESPAVVL 249
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 727116390 257 SDYEYQMLRDASLKIIRALKIEGGCNVQLALDpHSFNYYVIEVNPRVSRSSALASKATGYPIAKLAAKIAVG 328
Cdd:PRK08462 250 DEKTRERLHETAIKAAKAIGYEGAGTFEFLLD-SNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEG 320
|
|
| ATP-grasp_3 |
pfam02655 |
ATP-grasp domain; No functional information or experimental verification of function is known ... |
664-836 |
4.37e-11 |
|
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: 62.40 E-value: 4.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 664 AENRDLFEQALQELAIPQPpgdTATSAEEAVviadRIGYPVLVRPSYVLGGRAMEIVENQKDLEDYMRHavkaspehpVL 743
Cdd:pfam02655 1 ASDKLKTYKALKNAGVPTP---ETLQAEELL----REEKKYVVKPRDGCGGEGVRKVENGREDEAFIEN---------VL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 744 VDSYLLGQECEVDAICDGKTVLI----PGIMEHIERAGVHSGDSMAVypPQYLSQEIQATIADYTKKLAlglNCVGMMNI 819
Cdd:pfam02655 65 VQEFIEGEPLSVSLLSDGEKALPlsvnRQYIDNGGSGFVYAGNVTPS--RTELKEEIIELAEEVVECLP---GLRGYVGV 139
|
170
....*....|....*..
gi 727116390 820 QFVIHENRVYVIEVNPR 836
Cdd:pfam02655 140 DLVLKDNEPYVIEVNPR 156
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
102-303 |
7.61e-11 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 65.59 E-value: 7.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 102 LSESG----ILDELNVELLGTKLSAIDQAEDRDLFKQLMEELEQP-IPESE-IVNTVEQAVAFAKRIGYPIIVRPafTLG 175
Cdd:PRK08591 85 LSENAdfaeICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPvVPGSDgPVDDEEEALAIAKEIGYPVIIKA--TAG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 176 GTGGGM--CDTEEEL-------RQIAE----NGlklspvtQCLIEKSIAGFKEIEYEVMRDSADNAivvcnmenfdpvgI 242
Cdd:PRK08591 163 GGGRGMrvVRTEAELekafsmaRAEAKaafgNP-------GVYMEKYLENPRHIEIQVLADGHGNA-------------I 222
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 727116390 243 HTGD---SI------VF--APSQTLSDYEYQMLRDASLKIIRALKIEGGCNVQLALDpHSFNYYVIEVNPRV 303
Cdd:PRK08591 223 HLGErdcSLqrrhqkVLeeAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYE-KNGEFYFIEMNTRI 293
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
102-332 |
8.24e-11 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 65.50 E-value: 8.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 102 LSESG----ILDELNVELLGTKLSAIDQAEDRDLFKQLMEELEQPI-PESE-IVNTVEQAVAFAKRIGYPIIVRPAFTLG 175
Cdd:PRK05586 85 LSENSkfakMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVvPGSEgEIENEEEALEIAKEIGYPVMVKASAGGG 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 176 GTGGGMCDTEEELRQIAENGLKLSPVT----QCLIEKSIAGFKEIEYEVMRDSADNAIVVCNMEnfdpVGIHTGDSIVF- 250
Cdd:PRK05586 165 GRGIRIVRSEEELIKAFNTAKSEAKAAfgddSMYIEKFIENPKHIEFQILGDNYGNVVHLGERD----CSLQRRNQKVLe 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 251 -APSQTLSDYEYQMLRDASLKIIRALKIEGGCNVQLALDPHSfNYYVIEVNPRVSRSSALASKATGYPIAKLAAKIAVGL 329
Cdd:PRK05586 241 eAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDG-NFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGE 319
|
...
gi 727116390 330 TLD 332
Cdd:PRK05586 320 KLS 322
|
|
| MGS-like |
cd00532 |
MGS-like domain. This domain composes the whole protein of methylglyoxal synthetase, which ... |
938-1046 |
1.10e-10 |
|
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: 59.83 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 938 VLFTIADETKEEALEIAKRFSAIGYSLVATEGTADFLAKHQLPVKKVTKISNPEGETVLDVIRN-GNAQVVINTMDKNRS 1016
Cdd:cd00532 2 VFLSVSDHVKAMLVDLAPKLSSDGFPLFATGGTSRVLADAGIPVRAVSKRHEDGEPTVDAAIAEkGKFDVVINLRDPRRD 81
|
90 100 110
....*....|....*....|....*....|.
gi 727116390 1017 S-ANQDGFSIRREAVEHGIPLFTSLDTANAI 1046
Cdd:cd00532 82 RcTDEDGTALLRLARLYKIPVTTPNATAMFV 112
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
114-303 |
1.35e-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: 65.87 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 114 ELLGTKLSAIDQAEDRDLfkqlmeeleqP-IPESEI-VNTVEQAVAFAKRIGYPIIVRPAftLGGTGGGM--CDTEEELR 189
Cdd:COG1038 114 EMLGDKVAARAAAIEAGV----------PvIPGTEGpVDDLEEALAFAEEIGYPVMLKAA--AGGGGRGMrvVRSEEELE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 190 QIAE-----------NGlklspvtQCLIEKSIAGFKEIEYEVMRDSADNAI---------------VVcnmEnfdpvgih 243
Cdd:COG1038 182 EAFEsarreakaafgDD-------EVFLEKYIERPKHIEVQILGDKHGNIVhlferdcsvqrrhqkVV---E-------- 243
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 244 tgdsivFAPSQTLSDYEYQMLRDASLKIIRALKIEGGCNVQLALDPHSfNYYVIEVNPRV 303
Cdd:COG1038 244 ------IAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVDDDG-NFYFIEVNPRI 296
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
29-313 |
1.60e-09 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 60.67 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 29 AGTQACLALKEE--GYEVVLV---NSNPATIMTDK-----EIADHVYIEpitleFVSRILRKERPDALLPTLGGQTGLnM 98
Cdd:PRK12767 11 RRVQLVKALKKSllKGRVIGAdisELAPALYFADKfyvvpKVTDPNYID-----RLLDICKKEKIDLLIPLIDPELPL-L 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 99 AMELSEsgiLDELNVELLGTKLSAIDQAEDRDLFKQLMEELEQPIPESEIVNTVEQAVA--FAKRIGYPIIVRPAFTLGG 176
Cdd:PRK12767 85 AQNRDR---FEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDFKAalAKGELQFPLFVKPRDGSAS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 177 TGGGMCDTEEELRQIAENGLKLspvtqcLIEKSIAGfKEIEYEVMRDSADNAIVVCNMENFDPVGIHTGDSIVFapsqtl 256
Cdd:PRK12767 162 IGVFKVNDKEELEFLLEYVPNL------IIQEFIEG-QEYTVDVLCDLNGEVISIVPRKRIEVRAGETSKGVTV------ 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 727116390 257 sdyEYQMLRDASLKIIRALKIEGGCNVQLALDPHSfnYYVIEVNPRVSRSSALASKA 313
Cdd:PRK12767 229 ---KDPELFKLAERLAEALGARGPLNIQCFVTDGE--PYLFEINPRFGGGYPLSYMA 280
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
672-842 |
3.69e-09 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 59.35 E-value: 3.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 672 QALQELAIPQPPGDTATSAEEAVVIADRIGYPVLVRPsyVLGGR--AMEIVENQKDLEDYMRHAVKASPEhpVLVDSYLL 749
Cdd:PRK01372 104 LVWQAAGLPTPPWIVLTREEDLLAAIDKLGLPLVVKP--AREGSsvGVSKVKEEDELQAALELAFKYDDE--VLVEKYIK 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 750 GQECEVdAICDGKtVLipGIMEhIERAGV--------HSGDSMAVYPPQyLSQEIQATIADYTKKLALGLNCVGMMNIQF 821
Cdd:PRK01372 180 GRELTV-AVLGGK-AL--PVIE-IVPAGEfydyeakyLAGGTQYICPAG-LPAEIEAELQELALKAYRALGCRGWGRVDF 253
|
170 180
....*....|....*....|..
gi 727116390 822 VIHE-NRVYVIEVNprasrTVP 842
Cdd:PRK01372 254 MLDEdGKPYLLEVN-----TQP 270
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
35-324 |
1.10e-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: 57.64 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 35 LALKEEGYEVVLVNsnpatimtdkeiADHVYIEPITLEFVSRILRKERPDALLPTlggQTGLNMAMELSEsgildelNVE 114
Cdd:COG0189 21 EAAQRRGHEVEVID------------PDDLTLDLGRAPELYRGEDLSEFDAVLPR---IDPPFYGLALLR-------QLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 115 LLGTKL----SAIDQAEDRDLFKQLMEELEQPIPESEIVNTVEQAVAFAKRIGYPIIVRPAFTLGGTGGGMCDTEEELRQ 190
Cdd:COG0189 79 AAGVPVvndpEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDALES 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 191 IAENGLKLSPVT---QCLIEKSiAGFK--------EIEYEVMRDSADNAIVVcNMenfdpvgiHTGDSIVFAPsqtLSDy 259
Cdd:COG0189 159 ILEALTELGSEPvlvQEFIPEE-DGRDirvlvvggEPVAAIRRIPAEGEFRT-NL--------ARGGRAEPVE---LTD- 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 727116390 260 EyqmLRDASLKIIRALKIE-GGcnVQLALDPHsfNYYVIEVNPrvsrSSALA--SKATGYPIAKLAAK 324
Cdd:COG0189 225 E---ERELALRAAPALGLDfAG--VDLIEDDD--GPLVLEVNV----TPGFRglERATGVDIAEAIAD 281
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
672-866 |
2.05e-08 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 57.73 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 672 QALQELAIPQPPG-DTA-TSAEEAVVIADRIGYPVLVRPSYVLGGRAMEIVENQKDLED------------------YMR 731
Cdd:PRK06111 121 RAMQAAGVPVVPGiTTNlEDAEEAIAIARQIGYPVMLKASAGGGGIGMQLVETEQELTKafesnkkraanffgngemYIE 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 732 HAVkASPEH---PVLVDS-----YLLGQECEVDaicdgktvlipgiMEH---IERAgvhsgdsmavyPPQYLSQEIQATI 800
Cdd:PRK06111 201 KYI-EDPRHieiQLLADThgntvYLWERECSVQ-------------RRHqkvIEEA-----------PSPFLDEETRKAM 255
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 727116390 801 ADYTKKLALGLNCVGMMNIQFVIHENR-VYVIEVNPRASRTVPFLSKITGIPMAQVATKAILGEKLT 866
Cdd:PRK06111 256 GERAVQAAKAIGYTNAGTIEFLVDEQKnFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKLS 322
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
113-331 |
2.18e-08 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 57.73 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 113 VELLGTKLSAidqaedrdlfKQLMEELEQPI-P-ESEIVNTVEQAVAFAKRIGYPIIVRPAFtlGGTGGGM--CDTEEEL 188
Cdd:PRK06111 110 IAKMGSKIEA----------RRAMQAAGVPVvPgITTNLEDAEEAIAIARQIGYPVMLKASA--GGGGIGMqlVETEQEL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 189 RQ-IAENGLKLSPV---TQCLIEKSIAGFKEIEYEVMRDSADNAIVV----CNMENFDPVGIHTgdsivfAPSQTLSDYE 260
Cdd:PRK06111 178 TKaFESNKKRAANFfgnGEMYIEKYIEDPRHIEIQLLADTHGNTVYLwereCSVQRRHQKVIEE------APSPFLDEET 251
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 727116390 261 YQMLRDASLKIIRALKIEGGCNVQLALDPHSfNYYVIEVNPRVSRSSALASKATGYPIAKLAAKIAVGLTL 331
Cdd:PRK06111 252 RKAMGERAVQAAKAIGYTNAGTIEFLVDEQK-NFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKL 321
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
99-344 |
2.40e-08 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 57.90 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 99 AMELSESGILdelnveLLGTKLSAIDQAEDRDLFKQLMEELEQPI-PESEIVN--TVEQAVAFAKRIGYPIIVRPAFTLG 175
Cdd:PRK08463 91 AKAVEDAGII------FIGPKSEVIRKMGNKNIARYLMKKNGIPIvPGTEKLNseSMEEIKIFARKIGYPVILKASGGGG 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 176 GTGGGMCDTEEELRQiAENGLKLSPVT-----QCLIEKSIAGFKEIEYEVMRDSADNAIVVCnmENFDPVGIHTGDSIVF 250
Cdd:PRK08463 165 GRGIRVVHKEEDLEN-AFESCKREALAyfnndEVFMEKYVVNPRHIEFQILGDNYGNIIHLC--ERDCSIQRRHQKVIEI 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 251 APSQTLSDYEYQMLRDASLKIIRALKIEGGCNVQLALDPHSfNYYVIEVNPRVSRSSALASKATGYPIAKLAAKIAVGLT 330
Cdd:PRK08463 242 APCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDDYN-RFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAAGEI 320
|
250
....*....|....
gi 727116390 331 LDEMKNPVTGTTYA 344
Cdd:PRK08463 321 LDLEQSDIKPRGFA 334
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
667-863 |
3.73e-08 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 57.55 E-value: 3.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 667 RDLFEQA--LQELAIPQPPGDTATSAEEAVVIADRIGYPVLVRPSYVLGGRAMEIVENQKDLEDYMRHAVKA-SPEhpVL 743
Cdd:PRK02186 106 RDKKRLArtLRDHGIDVPRTHALALRAVALDALDGLTYPVVVKPRMGSGSVGVRLCASVAEAAAHCAALRRAgTRA--AL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 744 VDSYLLGQECEVDAICDGKTVLIPGIM-EHIERAGvHSGDSMAVYPPQyLSQEIQATIADYTKKL--ALGLNcVGMMNIQ 820
Cdd:PRK02186 184 VQAYVEGDEYSVETLTVARGHQVLGITrKHLGPPP-HFVEIGHDFPAP-LSAPQRERIVRTVLRAldAVGYA-FGPAHTE 260
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 727116390 821 FVIHENRVYVIEVNPR-ASRTVP-FLSKITGIPMAQVATKAILGE 863
Cdd:PRK02186 261 LRVRGDTVVIIEINPRlAGGMIPvLLEEAFGVDLLDHVIDLHLGV 305
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
664-752 |
4.74e-08 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 57.09 E-value: 4.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 664 AENRDLFEQALQELAIPQPPGDTATSAEEAVVIADRIGYPVLVRPSYVLGGRAMEI-VENQKDLEDYMRHAVKASPEhpV 742
Cdd:PRK14016 212 ACDKELTKRLLAAAGVPVPEGRVVTSAEDAWEAAEEIGYPVVVKPLDGNHGRGVTVnITTREEIEAAYAVASKESSD--V 289
|
90
....*....|
gi 727116390 743 LVDSYLLGQE 752
Cdd:PRK14016 290 IVERYIPGKD 299
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
32-300 |
5.22e-08 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 55.89 E-value: 5.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 32 QACL-ALKEEGYEVVLVNsnpatimTDKEIADhvyiepitlefvsrILRKERPDALLPTLGGQTGLNMAMelseSGILDE 110
Cdd:PRK01372 26 AAVLaALREAGYDAHPID-------PGEDIAA--------------QLKELGFDRVFNALHGRGGEDGTI----QGLLEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 111 LNVELLGTKL--SAIdqAEDRDLFKQLMEELEQPIPESEIVNTVEQAVAFAKRIGYPIIVRPAftLGGTGGGM--CDTEE 186
Cdd:PRK01372 81 LGIPYTGSGVlaSAL--AMDKLRTKLVWQAAGLPTPPWIVLTREEDLLAAIDKLGLPLVVKPA--REGSSVGVskVKEED 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 187 ELRQIAENGLKLSPvtQCLIEKSIAGfKEIEYEVMRDSADNAI-VVCNMENFDpvgIH----TGDSIVFAPSQtLSDYEY 261
Cdd:PRK01372 157 ELQAALELAFKYDD--EVLVEKYIKG-RELTVAVLGGKALPVIeIVPAGEFYD---YEakylAGGTQYICPAG-LPAEIE 229
|
250 260 270
....*....|....*....|....*....|....*....
gi 727116390 262 QMLRDASLKIIRALKIEGGCNVQLALDPHSfNYYVIEVN 300
Cdd:PRK01372 230 AELQELALKAYRALGCRGWGRVDFMLDEDG-KPYLLEVN 267
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
675-836 |
6.33e-08 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 57.07 E-value: 6.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 675 QELAIPQPPG--DTATSAEEAVVIADRIGYPVLVRPSYVLGGRAMEIVENQKDLEDY----MRHAVKA--SPEhpVLVDS 746
Cdd:PRK12999 128 IKAGVPVIPGseGPIDDIEEALEFAEEIGYPIMLKASAGGGGRGMRIVRSEEELEEAferaKREAKAAfgNDE--VYLEK 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 747 YLLG-QECEVDAICD--GKTVlipgimeH---------------IERAgvhsgdsmavyPPQYLSQEIQATIADYTKKLA 808
Cdd:PRK12999 206 YVENpRHIEVQILGDkhGNVV-------HlyerdcsvqrrhqkvVEIA-----------PAPGLSEELRERICEAAVKLA 267
|
170 180
....*....|....*....|....*....
gi 727116390 809 LGLNCVGMMNIQF-VIHENRVYVIEVNPR 836
Cdd:PRK12999 268 RAVGYVNAGTVEFlVDADGNFYFIEVNPR 296
|
|
| ATP-grasp_4 |
pfam13535 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
700-836 |
7.65e-08 |
|
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: 53.06 E-value: 7.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 700 IGYPVLVRPSYVLGGRAMEIVENQKDL---------------EDYMRHAVKASpehPVLVDSYLLGQECEVDAICD--GK 762
Cdd:pfam13535 1 IPYPCVIKPSVGFFSVGVYKINNREEWkaafaaireeieqwkEMYPEAVVDGG---SFLVEEYIEGEEFAVDAYFDenGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 763 TVLIpGIMEHIERAGVHSGDSMAVYPPQyLSQEIQATIADYTKKL--ALGLNcvgmmniQFVIH-------ENRVYVIEV 833
Cdd:pfam13535 78 PVIL-NILKHDFASSEDVSDRIYVTSAS-IIRETQAAFTEFLKRInaLLGLK-------NFPVHielrvdeDGQIIPIEV 148
|
...
gi 727116390 834 NPR 836
Cdd:pfam13535 149 NPL 151
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
688-836 |
7.81e-08 |
|
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: 56.63 E-value: 7.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 688 TSAEEAVVIADRIGYPVLVRPSYVLGGRAMEIVENQKDLEDY----MRHAVKA--SPEhpVLVDSYLLG-QECEVDAICD 760
Cdd:COG1038 142 DDLEEALAFAEEIGYPVMLKAAAGGGGRGMRVVRSEEELEEAfesaRREAKAAfgDDE--VFLEKYIERpKHIEVQILGD 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 761 --GKTVlipgimeH---------------IERAgvhsgdsmavyPPQYLSQEIQATIADYTKKLA--LGLNCVGmmNIQF 821
Cdd:COG1038 220 khGNIV-------HlferdcsvqrrhqkvVEIA-----------PAPNLDEELREAICEAAVKLAkaVGYVNAG--TVEF 279
|
170
....*....|....*.
gi 727116390 822 -VIHENRVYVIEVNPR 836
Cdd:COG1038 280 lVDDDGNFYFIEVNPR 295
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
642-866 |
7.81e-08 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 56.26 E-value: 7.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 642 LAEPLTKQGVKILGTTIEDLDRAENRDLFEQALQELAIPQPPGDTAT--SAEEAVVIADRIGYPVLVRPSYVLGGRAMEI 719
Cdd:PRK07178 90 LAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNlaDLDEALAEAERIGYPVMLKATSGGGGRGIRR 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 720 VENQKDLE-DYMR---HAVKA--SPEhpVLVDSYLLG-QECEVDAICD--GKTVLIPGIMEHIERagvHSGDSMAVYPPQ 790
Cdd:PRK07178 170 CNSREELEqNFPRvisEATKAfgSAE--VFLEKCIVNpKHIEVQILADshGNVVHLFERDCSIQR---RNQKLIEIAPSP 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 791 YLSQEIQATIADYTKKLAlglNCVGMMN---IQFVI-HENRVYVIEVNPRASRTVPFLSKITGIPMAQVATKAILGEKLT 866
Cdd:PRK07178 245 QLTPEQRAYIGDLAVRAA---KAVGYENagtVEFLLdADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGLPLS 321
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
641-727 |
1.98e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 54.75 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 641 NLAEPLTKQGVKILGTTIEDLDRAENRDLFEQALQELAIPQPPGDTAT--SAEEAVVIADRIGYPVLVRPSYVLGGRAME 718
Cdd:PRK08462 92 NFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGAlkSYEEAKKIAKEIGYPVILKAAAGGGGRGMR 171
|
....*....
gi 727116390 719 IVENQKDLE 727
Cdd:PRK08462 172 VVEDESDLE 180
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
679-836 |
2.87e-07 |
|
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: 51.90 E-value: 2.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 679 IPQPPGDTATSAEEAVVIADRIGYPVLV-RPSYVLGGR----AMEIVENQKDLEDYMRHAVKASPEHPVLVDSYLLGQEC 753
Cdd:pfam01071 15 IPTAEYETFTDPEEAKSYIQEAGFPAIVvKADGLAAGKgvivASSNEEAIKAVDEILEQKKFGEAGETVVIEEFLEGEEV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 754 EVDAICDGKTVLIPGIMEHIERAGvhSGDS------MAVYPP-----QYLSQEIQATIADYT-KKLAL-GLNCVGMMNIQ 820
Cdd:pfam01071 95 SVLAFVDGKTVKPLPPAQDHKRAG--EGDTgpntggMGAYSPapvitPELLERIKETIVEPTvDGLRKeGIPFKGVLYAG 172
|
170
....*....|....*.
gi 727116390 821 FVIHENRVYVIEVNPR 836
Cdd:pfam01071 173 LMLTKDGPKVLEFNCR 188
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
657-865 |
3.08e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 54.33 E-value: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 657 TIEDL-DRAENRDLFEQAlqelAIPQPPG--DTATSAEEAVVIADRIGYPVLVRPSYVLGGRAMEIVENQKDLEDYMRHA 733
Cdd:PRK05586 109 TIELMgNKSNAREIMIKA----GVPVVPGseGEIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEEELIKAFNTA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 734 VKASP--------------EHPVLVDSYLLGQECE-VDAICDGKTVLIPGIMEHIERAgvhsgdsmavyPPQYLSQEIQA 798
Cdd:PRK05586 185 KSEAKaafgddsmyiekfiENPKHIEFQILGDNYGnVVHLGERDCSLQRRNQKVLEEA-----------PSPVMTEELRK 253
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 727116390 799 TIADYTKKLALGLNCVGMMNIQFVIHEN-RVYVIEVNPRASRTVPFLSKITGIPMAQVATKAILGEKL 865
Cdd:PRK05586 254 KMGEIAVKAAKAVNYKNAGTIEFLLDKDgNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEKL 321
|
|
| ATPgrasp_Ter |
pfam15632 |
ATP-grasp in the biosynthetic pathway with Ter operon; This ATP-grasp family is related to ... |
741-867 |
3.97e-07 |
|
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: 49.92 E-value: 3.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 741 PVLVDSYLLGQECEVDAICDGKTVLIPgimehIERAGVHSGDsmavyppQYLSQEiqATIADYTKKLALGLNCVGMMNIQ 820
Cdd:pfam15632 4 PLLVMEYLPGPEYSVDCLAGHGELIAA-----VPRRKGDGGI-------QTLEDD--PELIEAARRLAEAFGLDGLFNVQ 69
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 727116390 821 FVIHENRVYVIEVNPRASRTVPfLSKITGIPMAQVATKAILGEKLTD 867
Cdd:pfam15632 70 FRYDGDGPKLLEINPRMSGGIG-YSCLAGVNLPYLALKLLLGLETPD 115
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
674-853 |
6.55e-07 |
|
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).
Pssm-ID: 429483 [Multi-domain] Cd Length: 204 Bit Score: 51.16 E-value: 6.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 674 LQELAIPQPP-------GDTATSAEEAVVIADRIGYPVLVRPSyVLGGR-AMEIVENQKDLEDYMRHAVKASPEhpVLVD 745
Cdd:pfam07478 2 LKAAGLPVVPfvtftraDWKLNPKEWCAQVEEALGYPVFVKPA-RLGSSvGVSKVESREELQAAIEEAFQYDEK--VLVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 746 SYLLGQECEVdAICDGKTVLIPGIMEHIERAGVH-------SGDSMAVYPPQyLSQEIQATIADYTKKLALGLNCVGMMN 818
Cdd:pfam07478 79 EGIEGREIEC-AVLGNEDPEVSPVGEIVPSGGFYdyeakyiDDSAQIVVPAD-LEEEQEEQIQELALKAYKALGCRGLAR 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 727116390 819 IQ-FVIHENRVYVIEVNprasrTVPFLSKITGIPMA 853
Cdd:pfam07478 157 VDfFLTEDGEIVLNEVN-----TIPGFTSISMFPKL 187
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
642-728 |
8.15e-07 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 53.06 E-value: 8.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 642 LAEPLTKQGVKILGTTIEDLDRAENRDLFEQALQELAIPQPPG--DTATSAEEAVVIADRIGYPVLVRPSYVLGGRAMEI 719
Cdd:PRK08654 91 FAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGteEGIEDIEEAKEIAEEIGYPVIIKASAGGGGIGMRV 170
|
....*....
gi 727116390 720 VENQKDLED 728
Cdd:PRK08654 171 VYSEEELED 179
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
118-170 |
1.01e-06 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 52.85 E-value: 1.01e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 727116390 118 TKLSAIDQAEDRDLFKQLMEELEQPIPESEIVNTVEQAVAFAKRIGYPIIVRP 170
Cdd:PRK14016 204 TSAIAVDIACDKELTKRLLAAAGVPVPEGRVVTSAEDAWEAAEEIGYPVVVKP 256
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
571-835 |
1.16e-06 |
|
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 439959 [Multi-domain] Cd Length: 289 Bit Score: 51.48 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 571 DYATVHSVKAIQAAGYEAIIMNSnpetvstdfsvsDKLYFEPLTLEDVMNVIDLENPIGVIVQFGG-QTAINLAEPLTKQ 649
Cdd:COG0189 13 KDSTKALIEAAQRRGHEVEVIDP------------DDLTLDLGRAPELYRGEDLSEFDAVLPRIDPpFYGLALLRQLEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 650 GVKILGTTiEDLDRAENRDLFEQALQELAIPQPPGDTATSAEEAVVIADRIGYPVLVRPSYVLGGRAMEIVENQKDLEDY 729
Cdd:COG0189 81 GVPVVNDP-EAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDALESI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 730 MRHaVKASPEHPVLVDSYLlGQECEVD---AICDGKTVL-IPGIMEHIE-RAGVHSGDSMAVYPpqyLSQEIQATIADYT 804
Cdd:COG0189 160 LEA-LTELGSEPVLVQEFI-PEEDGRDirvLVVGGEPVAaIRRIPAEGEfRTNLARGGRAEPVE---LTDEERELALRAA 234
|
250 260 270
....*....|....*....|....*....|.
gi 727116390 805 KKLALGLNCVgmmniQFVIHENRVYVIEVNP 835
Cdd:COG0189 235 PALGLDFAGV-----DLIEDDDGPLVLEVNV 260
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
624-853 |
1.25e-06 |
|
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: 51.19 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 624 LENPIGVIVQF-GGQTAINLAEPLTKQGVKILGTTIEdLDRAENRDLFEQALQELAIPQPPGDTATSAEEAVVIADRIGY 702
Cdd:TIGR00768 46 LAELDVVIVRIvSMFRGLAVLRYLESLGVPVINSSDA-ILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEEIGF 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 703 PVLVRPSYVLGGRAMEIVENQKDLEDYMRH-AVKASPEHPVLVDSYL-LGQECEVDAICDGKTVliPGIMEHIE----RA 776
Cdd:TIGR00768 125 PVVLKPVFGSWGRGVSLARDRQAAESLLEHfEQLNGPQNLFLVQEYIkKPGGRDIRVFVVGDEV--VAAIYRITsghwRS 202
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 727116390 777 GVHSGdsmAVYPPQYLSQEIqATIADYTKKlALGLNCVGmmnIQFVIHENRVYVIEVNPrasrTVPF--LSKITGIPMA 853
Cdd:TIGR00768 203 NLARG---GKAEPCSLTEEI-EELAIKAAK-ALGLDVAG---VDLLESEDGLLVNEVNA----NPEFknSVKTTGVNIA 269
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
643-865 |
3.29e-06 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 50.91 E-value: 3.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 643 AEPLTKQGVKILGTTIEDL----DRAENRdlfeQALQELAIPQPPG--DTATSAEEAVVIADRIGYPVLVRPSYVLGGRA 716
Cdd:PRK12833 95 AEAVEAAGLIFVGPDAQTIrtmgDKARAR----RTARRAGVPTVPGsdGVVASLDAALEVAARIGYPLMIKAAAGGGGRG 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 717 MEIVENQKDLEDYM----RHAVKASPEHPVLVDSYLL-GQECEVDAICDGKTVLipgimeHI-ERAGVHSGDSMAVY--- 787
Cdd:PRK12833 171 IRVAHDAAQLAAELplaqREAQAAFGDGGVYLERFIArARHIEVQILGDGERVV------HLfERECSLQRRRQKILeea 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 788 PPQYLSQEIQATIADYTKKLA--LGLNCVGMMNIQFVIHENRVYVIEVNPRASRTVPFLSKITGIPMAQVATKAILGEKL 865
Cdd:PRK12833 245 PSPSLTPAQRDALCASAVRLArqVGYRGAGTLEYLFDDARGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEPL 324
|
|
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
672-727 |
1.09e-05 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 49.03 E-value: 1.09e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 727116390 672 QALQELAIPQPPGDTA--TSAEEAVVIADRIGYPVLVRPSYVLGGRAMEIVENQKDLE 727
Cdd:PRK08591 121 ATMKKAGVPVVPGSDGpvDDEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELE 178
|
|
| PurD |
COG0151 |
Phosphoribosylamine-glycine ligase [Nucleotide transport and metabolism]; ... |
679-836 |
1.64e-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: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 679 IPQPPGDTATSAEEAVVIADRIGYPVLVRPSYVLGGR----AMEIVENQKDLEDYMRHAVKASPEHPVLVDSYLLGQECE 754
Cdd:COG0151 115 IPTAAYRVFTDLEEALAYLEEQGAPIVVKADGLAAGKgvvvAETLEEALAAVDDMLADGKFGDAGARVVIEEFLEGEEAS 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 755 VDAICDGKTVLI-PGIMEHiERAGvhSGDS------MAVY--PPQY---LSQEIQATIADYTKKlAL---GLNCVGMMNI 819
Cdd:COG0151 195 LFALTDGKTVLPlPTAQDH-KRAG--DGDTgpntggMGAYspAPVVteeLLEKIMEEIIEPTVA-GMaaeGIPYRGVLYA 270
|
170
....*....|....*..
gi 727116390 820 QFVIHENRVYVIEVNPR 836
Cdd:COG0151 271 GLMITADGPKVLEFNVR 287
|
|
| PatZN |
COG1042 |
Acyl-CoA synthetase (NDP forming) [Energy production and conversion]; |
655-704 |
2.04e-05 |
|
Acyl-CoA synthetase (NDP forming) [Energy production and conversion];
Pssm-ID: 440664 [Multi-domain] Cd Length: 708 Bit Score: 48.58 E-value: 2.04e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 727116390 655 GTTIEDLDRAENRDLFEQALQE-------------LA---IPQPPGDTATSAEEAVVIADRIGYPV 704
Cdd:COG1042 462 ASEDFDPDRERARAIIEAALAEgrgvlteaeakalLAaygIPVVPTRLARSAEEAVAAAEEIGYPV 527
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
62-325 |
1.58e-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: 44.64 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 62 DHVYIEPITLEFVSRILRKERPDALLPTlggqtGLNMAMELSESGILDELNVELLGTKlSAIDQAEDRDLFKQLMEELEQ 141
Cdd:TIGR00768 28 KVVTPPAINLTFNEGPRALAELDVVIVR-----IVSMFRGLAVLRYLESLGVPVINSS-DAILNAGDKFLSHQLLAKAGI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 142 PIPESEIVNTVEQAVAFAKRIGYPIIVRPAFTLGGTGGGMCDTEEELRQIAE-----NGLKLSPVTQCLIEKSiaGFKEI 216
Cdd:TIGR00768 102 PLPRTGLAGSPEEALKLIEEIGFPVVLKPVFGSWGRGVSLARDRQAAESLLEhfeqlNGPQNLFLVQEYIKKP--GGRDI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 217 EYEVMRDSADNAIVVCNMENFDpVGIHTGDSivfAPSQTLSDYEyqmlRDASLKIIRALKIEgGCNVQLALDPHSFnyYV 296
Cdd:TIGR00768 180 RVFVVGDEVVAAIYRITSGHWR-SNLARGGK---AEPCSLTEEI----EELAIKAAKALGLD-VAGVDLLESEDGL--LV 248
|
250 260 270
....*....|....*....|....*....|
gi 727116390 297 IEVNPRVSRSSalASKATGYPIA-KLAAKI 325
Cdd:TIGR00768 249 NEVNANPEFKN--SVKTTGVNIAgKLLDYI 276
|
|
| PRK14569 |
PRK14569 |
D-alanyl-alanine synthetase A; Provisional |
616-845 |
2.39e-04 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173033 [Multi-domain] Cd Length: 296 Bit Score: 44.28 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 616 EDVMNVIDLeNPIGVIVQFGGQTAIN--LAEPLTKQGVKILGTTIEDLDRAENRDLFEQALQELAIPQPPGDTATsaeEA 693
Cdd:PRK14569 47 ELVAKLLEL-KPDKCFVALHGEDGENgrVSALLEMLEIKHTSSSMKSSVITMDKMISKEILMHHRMPTPMAKFLT---DK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 694 VVIADRIGYPVLVRPSYvlGGRAMEIVEnQKDLEDyMRHAVKASPEH-PVLVDSYLLGQECEVDAICDG--KTVLIPGIM 770
Cdd:PRK14569 123 LVAEDEISFPVAVKPSS--GGSSIATFK-VKSIQE-LKHAYEEASKYgEVMIEQWVTGKEITVAIVNDEvySSVWIEPQN 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 727116390 771 EHIERAGVHSGDSMaVYPPQYLSQEIQATIADYTKKLALGLNCVGMMNIQFvIHENR--VYVIEVNPRASRTVPFLS 845
Cdd:PRK14569 199 EFYDYESKYSGKSI-YHSPSGLCEQKELEVRQLAKKAYDLLGCSGHARVDF-IYDDRgnFYIMEINSSPGMTDNSLS 273
|
|
| SucC |
COG0045 |
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA ... |
133-208 |
4.42e-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: 4.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 133 KQLMEELEQPIPESEIVNTVEQAVAFAKRIGYPIIV---------RpaftlgGTGGG--MCDTEEELRQIAEN--GLKLS 199
Cdd:COG0045 9 KELLAKYGVPVPRGIVATTPEEAVAAAEELGGPPVVvkaqvhaggR------GKAGGvkLAKSPEEAREAAEEilGMTLV 82
|
90
....*....|....*...
gi 727116390 200 ---------PVTQCLIEK 208
Cdd:COG0045 83 thqtgpkgkPVNKVLVEE 100
|
|
| PRK14572 |
PRK14572 |
D-alanyl-alanine synthetase A; Provisional |
642-860 |
7.12e-04 |
|
D-alanyl-alanine synthetase A; Provisional
Pssm-ID: 173036 [Multi-domain] Cd Length: 347 Bit Score: 42.97 E-value: 7.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 642 LAEPLTKQGVkiLGTTIEdLDRAENRDLFEQALQELA--IPQPPGDTATSAEEAVVIADRIGYPVLVRPsyVLGGRAMEI 719
Cdd:PRK14572 113 LGIPYTGSGV--LASALA-MDKTRANQIFLQSGQKVApfFELEKLKYLNSPRKTLLKLESLGFPQFLKP--VEGGSSVST 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 720 --VENQKDLEDYMrhAVKASPEHPVLVDSYLLGQECEVDAI---CDGK--------TVLIPGIMEHIERAGVHSGDSMAV 786
Cdd:PRK14572 188 ykITNAEQLMTLL--ALIFESDSKVMSQSFLSGTEVSCGVLeryRGGKrnpialpaTEIVPGGEFFDFESKYKQGGSEEI 265
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 727116390 787 YPPQyLSQEIQATIADYTKKLALGLNCVGMMNIQFVIHENRVYVIEVN--PRASRT--VPFLSKITGIPMAQVATKAI 860
Cdd:PRK14572 266 TPAR-ISDQEMKRVQELAIRAHESLGCKGYSRTDFIIVDGEPHILETNtlPGMTETslIPQQAKAAGINMEEVFTDLI 342
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
161-301 |
1.48e-03 |
|
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).
Pssm-ID: 429483 [Multi-domain] Cd Length: 204 Bit Score: 41.15 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 161 RIGYPIIVRPAftLGGTGGGM--CDTEEELRQIAENGLKLSPVTqcLIEKSIAGfKEIEYEVMRDSADNAI----VVCNM 234
Cdd:pfam07478 34 ALGYPVFVKPA--RLGSSVGVskVESREELQAAIEEAFQYDEKV--LVEEGIEG-REIECAVLGNEDPEVSpvgeIVPSG 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 727116390 235 ENFDpvgIHT----GDSIVFAPSQtLSDYEYQMLRDASLKIIRALKIEGGCNVQLALDPhSFNYYVIEVNP 301
Cdd:pfam07478 109 GFYD---YEAkyidDSAQIVVPAD-LEEEQEEQIQELALKAYKALGCRGLARVDFFLTE-DGEIVLNEVNT 174
|
|
| ATP-grasp_5 |
pfam13549 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
679-704 |
1.76e-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: 40.92 E-value: 1.76e-03
10 20
....*....|....*....|....*.
gi 727116390 679 IPQPPGDTATSAEEAVVIADRIGYPV 704
Cdd:pfam13549 24 IPVVPTRLARSPEEAVAAAEEIGYPV 49
|
|
| purT |
PRK09288 |
formate-dependent phosphoribosylglycinamide formyltransferase; |
662-836 |
3.23e-03 |
|
formate-dependent phosphoribosylglycinamide formyltransferase;
Pssm-ID: 236454 [Multi-domain] Cd Length: 395 Bit Score: 41.28 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 662 DRAENRDLfeqALQELAIPQPPGDTATSAEEAVVIADRIGYPVLVRPsyVLG--GRAMEIVENQKDLE---DY-MRHAVK 735
Cdd:PRK09288 113 NREGIRRL---AAEELGLPTSPYRFADSLEELRAAVEEIGYPCVVKP--VMSssGKGQSVVRSPEDIEkawEYaQEGGRG 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 736 ASPEhpVLVDSYLlgqecEVD------AIC--DGKTVLIPGImEHIEragvHSGDSMAVYPPQYLSQEIQATIADYTKKL 807
Cdd:PRK09288 188 GAGR--VIVEEFI-----DFDyeitllTVRavDGGTHFCAPI-GHRQ----EDGDYRESWQPQPMSPAALEEAQEIAKKV 255
|
170 180
....*....|....*....|....*....
gi 727116390 808 ALGLNCVGMMNIQFVIHENRVYVIEVNPR 836
Cdd:PRK09288 256 TDALGGRGLFGVELFVKGDEVYFSEVSPR 284
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
649-836 |
4.08e-03 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 40.91 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 649 QGVKILGTTiedLDRaenrdLFE-QALQELAIPQPPGDTATSAEEAVVIADRIGYPVLVRpSYVLG--GRAMEIVENQKD 725
Cdd:PRK06019 90 PGPDALAIA---QDR-----LTEkQFLDKLGIPVAPFAVVDSAEDLEAALADLGLPAVLK-TRRGGydGKGQWVIRSAED 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 726 LEDymrhAVKASPEHPVLVDSYL-LgqECEVDAIC----DGKTVLIPgIMEHIERAGV-HsgdsmAVYPPQYLSQEIQAT 799
Cdd:PRK06019 161 LEA----AWALLGSVPCILEEFVpF--EREVSVIVargrDGEVVFYP-LVENVHRNGIlR-----TSIAPARISAELQAQ 228
|
170 180 190
....*....|....*....|....*....|....*...
gi 727116390 800 IADYTKKLALGLNCVGMMNIQ-FVIHENRVYVIEVNPR 836
Cdd:PRK06019 229 AEEIASRIAEELDYVGVLAVEfFVTGDGELLVNEIAPR 266
|
|
| ATPgrasp_Ter |
pfam15632 |
ATP-grasp in the biosynthetic pathway with Ter operon; This ATP-grasp family is related to ... |
266-347 |
4.44e-03 |
|
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: 38.36 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 266 DASLKIIRALKIEGGCNVQLALDPHsfNYYVIEVNPRVsrSSALA-SKATGYPIAKLAAKIAVGLTLDEMKNPVTGTTYA 344
Cdd:pfam15632 51 EAARRLAEAFGLDGLFNVQFRYDGD--GPKLLEINPRM--SGGIGySCLAGVNLPYLALKLLLGLETPDPVEPRLGLRVR 126
|
...
gi 727116390 345 EFE 347
Cdd:pfam15632 127 EIE 129
|
|
| purH |
PRK00881 |
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; ... |
951-991 |
7.61e-03 |
|
bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; Provisional
Pssm-ID: 234854 Cd Length: 513 Bit Score: 40.07 E-value: 7.61e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 727116390 951 LEIAKRFSAIGYSLVATEGTADFLAKHQLPVKKVTKISN-PE 991
Cdd:PRK00881 18 VEFAKALVELGVEILSTGGTAKLLAEAGIPVTEVSDVTGfPE 59
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
650-728 |
9.24e-03 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 39.80 E-value: 9.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 650 GVKILGTTIEDLDRAENRDLFEQALQELAIPQPPGD---TATSAEEAVVIADRIGYPVLVRPSYVLGGRAMEIVENQKDL 726
Cdd:PRK08463 98 GIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTeklNSESMEEIKIFARKIGYPVILKASGGGGGRGIRVVHKEEDL 177
|
..
gi 727116390 727 ED 728
Cdd:PRK08463 178 EN 179
|
|
| sucC |
PRK00696 |
ADP-forming succinate--CoA ligase subunit beta; |
133-208 |
9.48e-03 |
|
ADP-forming succinate--CoA ligase subunit beta;
Pssm-ID: 234813 [Multi-domain] Cd Length: 388 Bit Score: 39.69 E-value: 9.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727116390 133 KQLMEELEQPIPESEIVNTVEQAVAFAKRI-GYPIIVRPAFTLGGTG--GG--MCDTEEELRQIAEN--GLKLS------ 199
Cdd:PRK00696 9 KELFAKYGVPVPRGIVATTPEEAVEAAEELgGGVWVVKAQVHAGGRGkaGGvkLAKSPEEAREFAKQilGMTLVthqtgp 88
|
90
....*....|..
gi 727116390 200 ---PVTQCLIEK 208
Cdd:PRK00696 89 kgqPVNKVLVEE 100
|
|
| |
