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Conserved domains on  [gi|651883668|ref|WP_026643379|]
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MULTISPECIES: carbamoyl-phosphate synthase large subunit [Bifidobacterium]

Protein Classification

carbamoyl phosphate synthase large subunit( domain architecture ID 11480555)

carbamoyl phosphate synthase large subunit is a component of the two-subunit enzyme that catalyzes the reaction of bicarbonate, glutamine, and two molecules of MgATP, to produce carbamoyl phosphate, an intermediate in the biosynthesis of arginine and pyrimidine nucleotides

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
carB PRK05294
carbamoyl-phosphate synthase large subunit;
1-1115 0e+00

carbamoyl-phosphate synthase large subunit;


:

Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 1830.87  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668    1 MPKRNDIKSVMVIGSGPIVIGQAAEFDYSGTQACRVLREEGIRVILVNSNPATIMTDPEMADATYIEPIATPILERIIAK 80
Cdd:PRK05294    1 MPKRTDIKKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   81 ERPDALLPTLGGQTALNAAVALGEAGVLKKYNVELIGASLEAIDRGEDRESFKEVVEAAGAESARSDIAHTLEEVDAIAE 160
Cdd:PRK05294   81 ERPDAILPTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVAE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  161 RFGFPLVVRPSFTMGGLGSGIAHNTEELHRIAGAGIHYSPTDEVLIEEGIEGWKEYELELMRDRNDNVVVVCPIENVDPV 240
Cdd:PRK05294  161 EIGYPVIIRPSFTLGGTGGGIAYNEEELEEIVERGLDLSPVTEVLIEESLLGWKEYEYEVMRDKNDNCIIVCSIENIDPM 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  241 GVHTGDSITVAPVFTLTDREYQKLRDIGIAIIRGVGVDTGGCNIQFAMHPATGRIIVIEMNPRVSRSSALASKATGFPIA 320
Cdd:PRK05294  241 GVHTGDSITVAPAQTLTDKEYQMLRDASIAIIREIGVETGGCNVQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPIA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  321 KIATKLALGYTLDEIQNDITKSTPASFEPTIDYVVTKVPRFAFEKFPGADPTLTTSMKSVGEAMALAGNFQESLGKAMRS 400
Cdd:PRK05294  321 KVAAKLAVGYTLDEIKNDITGKTPASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALRS 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  401 IDKRDMGFswSGEKPGEQEVAELLEAMKVPTEHRYLQIMRAIWGGATEEQIFASTKIDPWFVKQFMLINDTAMQVRD-AE 479
Cdd:PRK05294  401 LEIGVTGL--DEDLFEEESLEELREELKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELKEnGL 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  480 TLSPRLLKKAKLAGLSDLQIARLRGLgdaGENTVRELRWNYGLHPVYKTVDTCAAEFDAVTPYYYSCYADESELRKRDRE 559
Cdd:PRK05294  479 PLDAELLREAKRLGFSDARIAKLLGV---TEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYEEECESNPSDRK 555
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  560 AVIILGSGPNRIGQGIEFDYTCVHAVQELgKDC--DTIMVNCNPETVSTDYDMSDRLYFEPLTFEDVIEIYEAEKKmgpi 637
Cdd:PRK05294  556 KVLVLGSGPNRIGQGIEFDYCCVHAVLAL-REAgyETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKP---- 630
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  638 KGVIVQLGGQTPLSLAARLKAAGVPILGTTPESIDLAENRELFGEVLRAEKLNAPRFGTALSLEEALDAAHSIGYPVLVR 717
Cdd:PRK05294  631 KGVIVQFGGQTPLKLAKALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPVLVR 710
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  718 PSYVLGGRGMEIVYDDAQLEKYVNRALNeakadtvVSGRlpSPLLIDKFLQDAIEIDVDALFDGDELYIGGIMEHIEEAG 797
Cdd:PRK05294  711 PSYVLGGRAMEIVYDEEELERYMREAVK-------VSPD--HPVLIDKFLEGAIEVDVDAICDGEDVLIGGIMEHIEEAG 781
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  798 VHSGDAACTLPPSTLSDDQIRRLREATYAIAKGCGVCGLINVQYAFMANTLYVIEANPRASRTVPFASKATGVALAKAAA 877
Cdd:PRK05294  782 VHSGDSACSLPPQTLSEEIIEEIREYTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKIAA 861
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  878 RIMAGETIAQQRANGLLLPHGdggdvrlgqqVAIKESVLPFKRFRtpvgkTVDILLGPEMRSTGEVMGFDRDFPHAFAKS 957
Cdd:PRK05294  862 RVMLGKKLAELGYTKGLIPPY----------VAVKEAVFPFNKFP-----GVDPLLGPEMKSTGEVMGIDRTFGEAFAKA 926
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  958 QLSAYEgGLPTSGNVFISVNDTDKRQLPLFAVRLVELGFQIWATEGTASVLRRYGIESKIVDKItarvdsdpdapvqidk 1037
Cdd:PRK05294  927 QLAAGN-RLPTSGTVFLSVRDRDKEEVVELAKRLLELGFKILATSGTAKFLREAGIPVELVNKV---------------- 989
                        1050      1060      1070      1080      1090      1100      1110
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 651883668 1038 AEGSvgKNVVELIEEGTIDLILNTPNSRGSRSDGYSIRAAAIAADVPQFTTMTEFSAVLLAIEAVKANDYQVMSIQEH 1115
Cdd:PRK05294  990 HEGR--PHIVDLIKNGEIDLVINTPTGRQAIRDGFSIRRAALEYKVPYITTLAGARAAVKAIEALKFGELEVRSLQEY 1065
 
Name Accession Description Interval E-value
carB PRK05294
carbamoyl-phosphate synthase large subunit;
1-1115 0e+00

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 1830.87  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668    1 MPKRNDIKSVMVIGSGPIVIGQAAEFDYSGTQACRVLREEGIRVILVNSNPATIMTDPEMADATYIEPIATPILERIIAK 80
Cdd:PRK05294    1 MPKRTDIKKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   81 ERPDALLPTLGGQTALNAAVALGEAGVLKKYNVELIGASLEAIDRGEDRESFKEVVEAAGAESARSDIAHTLEEVDAIAE 160
Cdd:PRK05294   81 ERPDAILPTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVAE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  161 RFGFPLVVRPSFTMGGLGSGIAHNTEELHRIAGAGIHYSPTDEVLIEEGIEGWKEYELELMRDRNDNVVVVCPIENVDPV 240
Cdd:PRK05294  161 EIGYPVIIRPSFTLGGTGGGIAYNEEELEEIVERGLDLSPVTEVLIEESLLGWKEYEYEVMRDKNDNCIIVCSIENIDPM 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  241 GVHTGDSITVAPVFTLTDREYQKLRDIGIAIIRGVGVDTGGCNIQFAMHPATGRIIVIEMNPRVSRSSALASKATGFPIA 320
Cdd:PRK05294  241 GVHTGDSITVAPAQTLTDKEYQMLRDASIAIIREIGVETGGCNVQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPIA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  321 KIATKLALGYTLDEIQNDITKSTPASFEPTIDYVVTKVPRFAFEKFPGADPTLTTSMKSVGEAMALAGNFQESLGKAMRS 400
Cdd:PRK05294  321 KVAAKLAVGYTLDEIKNDITGKTPASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALRS 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  401 IDKRDMGFswSGEKPGEQEVAELLEAMKVPTEHRYLQIMRAIWGGATEEQIFASTKIDPWFVKQFMLINDTAMQVRD-AE 479
Cdd:PRK05294  401 LEIGVTGL--DEDLFEEESLEELREELKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELKEnGL 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  480 TLSPRLLKKAKLAGLSDLQIARLRGLgdaGENTVRELRWNYGLHPVYKTVDTCAAEFDAVTPYYYSCYADESELRKRDRE 559
Cdd:PRK05294  479 PLDAELLREAKRLGFSDARIAKLLGV---TEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYEEECESNPSDRK 555
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  560 AVIILGSGPNRIGQGIEFDYTCVHAVQELgKDC--DTIMVNCNPETVSTDYDMSDRLYFEPLTFEDVIEIYEAEKKmgpi 637
Cdd:PRK05294  556 KVLVLGSGPNRIGQGIEFDYCCVHAVLAL-REAgyETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKP---- 630
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  638 KGVIVQLGGQTPLSLAARLKAAGVPILGTTPESIDLAENRELFGEVLRAEKLNAPRFGTALSLEEALDAAHSIGYPVLVR 717
Cdd:PRK05294  631 KGVIVQFGGQTPLKLAKALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPVLVR 710
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  718 PSYVLGGRGMEIVYDDAQLEKYVNRALNeakadtvVSGRlpSPLLIDKFLQDAIEIDVDALFDGDELYIGGIMEHIEEAG 797
Cdd:PRK05294  711 PSYVLGGRAMEIVYDEEELERYMREAVK-------VSPD--HPVLIDKFLEGAIEVDVDAICDGEDVLIGGIMEHIEEAG 781
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  798 VHSGDAACTLPPSTLSDDQIRRLREATYAIAKGCGVCGLINVQYAFMANTLYVIEANPRASRTVPFASKATGVALAKAAA 877
Cdd:PRK05294  782 VHSGDSACSLPPQTLSEEIIEEIREYTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKIAA 861
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  878 RIMAGETIAQQRANGLLLPHGdggdvrlgqqVAIKESVLPFKRFRtpvgkTVDILLGPEMRSTGEVMGFDRDFPHAFAKS 957
Cdd:PRK05294  862 RVMLGKKLAELGYTKGLIPPY----------VAVKEAVFPFNKFP-----GVDPLLGPEMKSTGEVMGIDRTFGEAFAKA 926
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  958 QLSAYEgGLPTSGNVFISVNDTDKRQLPLFAVRLVELGFQIWATEGTASVLRRYGIESKIVDKItarvdsdpdapvqidk 1037
Cdd:PRK05294  927 QLAAGN-RLPTSGTVFLSVRDRDKEEVVELAKRLLELGFKILATSGTAKFLREAGIPVELVNKV---------------- 989
                        1050      1060      1070      1080      1090      1100      1110
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 651883668 1038 AEGSvgKNVVELIEEGTIDLILNTPNSRGSRSDGYSIRAAAIAADVPQFTTMTEFSAVLLAIEAVKANDYQVMSIQEH 1115
Cdd:PRK05294  990 HEGR--PHIVDLIKNGEIDLVINTPTGRQAIRDGFSIRRAALEYKVPYITTLAGARAAVKAIEALKFGELEVRSLQEY 1065
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
2-1099 0e+00

carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273581 [Multi-domain]  Cd Length: 1050  Bit Score: 1444.81  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668     2 PKRNDIKSVMVIGSGPIVIGQAAEFDYSGTQACRVLREEGIRVILVNSNPATIMTDPEMADATYIEPIATPILERIIAKE 81
Cdd:TIGR01369    1 PKRTDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668    82 RPDALLPTLGGQTALNAAVALGEAGVLKKYNVELIGASLEAIDRGEDRESFKEVVEAAGAESARSDIAHTLEEVDAIAER 161
Cdd:TIGR01369   81 RPDAILPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKE 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   162 FGFPLVVRPSFTMGGLGSGIAHNTEELHRIAGAGIHYSPTDEVLIEEGIEGWKEYELELMRDRNDNVVVVCPIENVDPVG 241
Cdd:TIGR01369  161 IGYPVIVRPAFTLGGTGGGIAYNREELKEIAERALSASPINQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPMG 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   242 VHTGDSITVAPVFTLTDREYQKLRDIGIAIIRGVGVDtGGCNIQFAMHPATGRIIVIEMNPRVSRSSALASKATGFPIAK 321
Cdd:TIGR01369  241 VHTGDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIE-GGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAK 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   322 IATKLALGYTLDEIQNDITKSTPASFEPTIDYVVTKVPRFAFEKFPGADPTLTTSMKSVGEAMALAGNFQESLGKAMRSI 401
Cdd:TIGR01369  320 VAAKLAVGYTLDELKNPVTGTTPASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSL 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   402 DKRDMGFSWSGEKPGEQEvaELLEAMKVPTEHRYLQIMRAIWGGATEEQIFASTKIDPWFVKQFMLINDTAMQVRD--AE 479
Cdd:TIGR01369  400 EIGATGFDLPDREVEPDE--DLWRALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEvkLT 477
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   480 TLSPRLLKKAKLAGLSDLQIARLRGLGDAgenTVRELRWNYGLHPVYKTVDTCAAEFDAVTPYYYSCYADES-ELRKRDR 558
Cdd:TIGR01369  478 DLDPELLRRAKKLGFSDAQIARLIGVTEA---EVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERdDVPFTDK 554
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   559 EAVIILGSGPNRIGQGIEFDYTCVHAVQELGKDCD-TIMVNCNPETVSTDYDMSDRLYFEPLTFEDVIEIYEAEKkmgpI 637
Cdd:TIGR01369  555 KKVLVLGSGPNRIGQGVEFDYCCVHAVLALRELGYeTIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEK----P 630
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   638 KGVIVQLGGQTPLSLAARLKAAGVPILGTTPESIDLAENRELFGEVLRAEKLNAPRFGTALSLEEALDAAHSIGYPVLVR 717
Cdd:TIGR01369  631 EGVIVQFGGQTPLNLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVR 710
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   718 PSYVLGGRGMEIVYDDAQLEKYVNRALNeakadtvVSGrlPSPLLIDKFLQDAIEIDVDALFDGDELYIGGIMEHIEEAG 797
Cdd:TIGR01369  711 PSYVLGGRAMEIVYNEEELRRYLEEAVA-------VSP--EHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEEAG 781
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   798 VHSGDAACTLPPSTLSDDQIRRLREATYAIAKGCGVCGLINVQYAFMANTLYVIEANPRASRTVPFASKATGVALAKAAA 877
Cdd:TIGR01369  782 VHSGDSTCVLPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAV 861
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   878 RIMAGETIAQQranGLLLPHGDGGdvrlgqqVAIKESVLPFKRFRtpvgkTVDILLGPEMRSTGEVMGFDRDFPHAFAKS 957
Cdd:TIGR01369  862 RVMLGKKLEEL---GVGKEKEPKY-------VAVKEPVFSFSKLA-----GVDPVLGPEMKSTGEVMGIGRDLAEAFLKA 926
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   958 QLSAYEgGLPTSGNVFISVNDTDKRQLPLFAVRLVELGFQIWATEGTASVLRRYGIESKIVDKITARvdsdpdapvqidk 1037
Cdd:TIGR01369  927 QLSSGN-RIPKKGSVLLSVRDKDKEELLDLARKLAEKGYKLYATEGTAKFLGEAGIKPELVLKVSEG------------- 992
                         1050      1060      1070      1080      1090      1100
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 651883668  1038 aegsvGKNVVELIEEGTIDLILNTP-NSRGSRSDGYSIRAAAIAADVPQFTTMTEFSAVLLAI 1099
Cdd:TIGR01369  993 -----RPNILDLIKNGEIELVINTTsKGAGTATDGYKIRREALDYGVPLITTLNTAEAFAEAL 1050
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
13-566 0e+00

Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440226 [Multi-domain]  Cd Length: 536  Bit Score: 699.32  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   13 IGSGPIVIGQAAEFDYSGTQACRVLREEGIRVILVNSNPATIMTDPEMADATYIEPIATPILERIIAKERPDALLPTLGG 92
Cdd:COG0458     1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   93 QTALNAAVALGEAGVLKkyNVELIGASLEAIDRGEDRESFKEVVEAAGAESARSDIAHTLEEVDAIAERFGFPLVVRPSF 172
Cdd:COG0458    81 QTALNLAVELEEAGILE--GVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  173 TMGGLGSGIAHNTEELHRIAGAGIHYSPTDEVLIEEGIEGWKEYELELMRDRNDNVVVVCPIENVDPVGVHTGDSITVAP 252
Cdd:COG0458   159 VLGGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRDGEDNVIIVGIMEHIEPAGVHSGDSICVAP 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  253 VFTLTDREYQKLRDIGIAIIRGVGVDtGGCNIQFAMHpaTGRIIVIEMNPRVSRSSALASKATGFPIAKIATKLALGYTL 332
Cdd:COG0458   239 PQTLSDKEYQRLRDATLKIARALGVV-GLCNIQFAVD--DGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTL 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  333 DEIQNDiTKstpasFEPTIDYVVTKVPRFAFEKFPGADPTLTTSMKSVGEAMALAGNFQESLGKAMRSIDKRDMGFSWSG 412
Cdd:COG0458   316 DELGND-TG-----FEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGTVLLS 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  413 EKPGEQEVAELLEAmkvPTEHRYLQIMRAIWGGATEEQIFASTKIDPWFVKQFMLINDTAMQVRDaETLSPRLLKKAKLA 492
Cdd:COG0458   390 LVADDDKEEALLLA---RRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDEIELEE-IILVINTLLGAKSL 465
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 651883668  493 GLSDLQIARLRglgDAGENTVRELRWNYGLHPVYKTVDTCAAEFDAVTPYYYSCYADESELRKRDREAVIILGS 566
Cdd:COG0458   466 GDSDGIIRRAL---AAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYYYSTYEYENESEETEEPKVVVIGS 536
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
128-333 1.04e-71

Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.


Pssm-ID: 397079 [Multi-domain]  Cd Length: 209  Bit Score: 237.59  E-value: 1.04e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   128 DRESFKEVVEAAGAESARSDIA--HTLEEVDAIAERFGFPLVVRPSFTMGGLGSGIAHNTEELHRIAGAGIHYSPT---- 201
Cdd:pfam02786    1 DKVLFKAAMKEAGVPTVPGTAGpvETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAafgn 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   202 DEVLIEEGIEGWKEYELELMRDRNDNVVVVCPIENVDPVgvHTGDSITVAPVFTLTDREYQKLRDIGIAIIRGVGVdTGG 281
Cdd:pfam02786   81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGY-VGA 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 651883668   282 CNIQFAMHPATGRIIVIEMNPRVSRSSALASKATGFPIAKIATKLALGYTLD 333
Cdd:pfam02786  158 GTVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
CPSase_L_D3 smart01096
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ...
423-547 1.54e-43

Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain.


Pssm-ID: 198164 [Multi-domain]  Cd Length: 124  Bit Score: 154.14  E-value: 1.54e-43
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668    423 LLEAMKVPTEHRYLQIMRAIWGGATEEQIFASTKIDPWFVKQFMLINDTAMQVRD--AETLSPRLLKKAKLAGLSDLQIA 500
Cdd:smart01096    1 LLEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKggLDELDADLLRKAKRLGFSDRQIA 80
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*..
gi 651883668    501 RLRGLGdagENTVRELRWNYGLHPVYKTVDTCAAEFDAVTPYYYSCY 547
Cdd:smart01096   81 KLLGVT---EAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
MGS_CPS_II cd01424
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate ...
970-1096 2.34e-36

Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate synthetase (CSP). CSP, a CarA and CarB heterodimer, catalyzes the production of carbamoyl phosphate which is subsequently employed in the metabolic pathways responsible for the synthesis of pyrimidine nucleotides or arginine. The MGS-like domain is the C-terminal domain of CarB and appears to play a regulatory role in CPS function by binding allosteric effector molecules, including UMP and ornithine.


Pssm-ID: 238712 [Multi-domain]  Cd Length: 110  Bit Score: 132.99  E-value: 2.34e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  970 GNVFISVNDTDKRQLPLFAVRLVELGFQIWATEGTASVLRRYGIESKIVDKItarvdsdpdapvqidkAEGSvgKNVVEL 1049
Cdd:cd01424     1 GTVFISVADRDKPEAVEIAKRLAELGFKLVATEGTAKYLQEAGIPVEVVNKV----------------SEGR--PNIVDL 62
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 651883668 1050 IEEGTIDLILNTPNSRGSRSDGYSIRAAAIAADVPQFTTMTEFSAVL 1096
Cdd:cd01424    63 IKNGEIQLVINTPSGKRAIRDGFSIRRAALEYKVPYFTTLDTARAAV 109
 
Name Accession Description Interval E-value
carB PRK05294
carbamoyl-phosphate synthase large subunit;
1-1115 0e+00

carbamoyl-phosphate synthase large subunit;


Pssm-ID: 235393 [Multi-domain]  Cd Length: 1066  Bit Score: 1830.87  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668    1 MPKRNDIKSVMVIGSGPIVIGQAAEFDYSGTQACRVLREEGIRVILVNSNPATIMTDPEMADATYIEPIATPILERIIAK 80
Cdd:PRK05294    1 MPKRTDIKKILIIGSGPIVIGQACEFDYSGTQACKALREEGYRVVLVNSNPATIMTDPEMADATYIEPITPEFVEKIIEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   81 ERPDALLPTLGGQTALNAAVALGEAGVLKKYNVELIGASLEAIDRGEDRESFKEVVEAAGAESARSDIAHTLEEVDAIAE 160
Cdd:PRK05294   81 ERPDAILPTMGGQTALNLAVELAESGVLEKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLPVPRSGIAHSMEEALEVAE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  161 RFGFPLVVRPSFTMGGLGSGIAHNTEELHRIAGAGIHYSPTDEVLIEEGIEGWKEYELELMRDRNDNVVVVCPIENVDPV 240
Cdd:PRK05294  161 EIGYPVIIRPSFTLGGTGGGIAYNEEELEEIVERGLDLSPVTEVLIEESLLGWKEYEYEVMRDKNDNCIIVCSIENIDPM 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  241 GVHTGDSITVAPVFTLTDREYQKLRDIGIAIIRGVGVDTGGCNIQFAMHPATGRIIVIEMNPRVSRSSALASKATGFPIA 320
Cdd:PRK05294  241 GVHTGDSITVAPAQTLTDKEYQMLRDASIAIIREIGVETGGCNVQFALNPKDGRYIVIEMNPRVSRSSALASKATGYPIA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  321 KIATKLALGYTLDEIQNDITKSTPASFEPTIDYVVTKVPRFAFEKFPGADPTLTTSMKSVGEAMALAGNFQESLGKAMRS 400
Cdd:PRK05294  321 KVAAKLAVGYTLDEIKNDITGKTPASFEPSLDYVVTKIPRFAFEKFPGADRRLGTQMKSVGEVMAIGRTFEESLQKALRS 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  401 IDKRDMGFswSGEKPGEQEVAELLEAMKVPTEHRYLQIMRAIWGGATEEQIFASTKIDPWFVKQFMLINDTAMQVRD-AE 479
Cdd:PRK05294  401 LEIGVTGL--DEDLFEEESLEELREELKEPTPERLFYIAEAFRRGASVEEIHELTKIDPWFLEQIEEIVELEEELKEnGL 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  480 TLSPRLLKKAKLAGLSDLQIARLRGLgdaGENTVRELRWNYGLHPVYKTVDTCAAEFDAVTPYYYSCYADESELRKRDRE 559
Cdd:PRK05294  479 PLDAELLREAKRLGFSDARIAKLLGV---TEDEVRKLRKALGIHPVYKRVDTCAAEFEADTPYYYSTYEEECESNPSDRK 555
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  560 AVIILGSGPNRIGQGIEFDYTCVHAVQELgKDC--DTIMVNCNPETVSTDYDMSDRLYFEPLTFEDVIEIYEAEKKmgpi 637
Cdd:PRK05294  556 KVLVLGSGPNRIGQGIEFDYCCVHAVLAL-REAgyETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIIEKEKP---- 630
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  638 KGVIVQLGGQTPLSLAARLKAAGVPILGTTPESIDLAENRELFGEVLRAEKLNAPRFGTALSLEEALDAAHSIGYPVLVR 717
Cdd:PRK05294  631 KGVIVQFGGQTPLKLAKALEAAGVPILGTSPDAIDLAEDRERFSKLLEKLGIPQPPNGTATSVEEALEVAEEIGYPVLVR 710
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  718 PSYVLGGRGMEIVYDDAQLEKYVNRALNeakadtvVSGRlpSPLLIDKFLQDAIEIDVDALFDGDELYIGGIMEHIEEAG 797
Cdd:PRK05294  711 PSYVLGGRAMEIVYDEEELERYMREAVK-------VSPD--HPVLIDKFLEGAIEVDVDAICDGEDVLIGGIMEHIEEAG 781
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  798 VHSGDAACTLPPSTLSDDQIRRLREATYAIAKGCGVCGLINVQYAFMANTLYVIEANPRASRTVPFASKATGVALAKAAA 877
Cdd:PRK05294  782 VHSGDSACSLPPQTLSEEIIEEIREYTKKLALELNVVGLMNVQFAVKDDEVYVIEVNPRASRTVPFVSKATGVPLAKIAA 861
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  878 RIMAGETIAQQRANGLLLPHGdggdvrlgqqVAIKESVLPFKRFRtpvgkTVDILLGPEMRSTGEVMGFDRDFPHAFAKS 957
Cdd:PRK05294  862 RVMLGKKLAELGYTKGLIPPY----------VAVKEAVFPFNKFP-----GVDPLLGPEMKSTGEVMGIDRTFGEAFAKA 926
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  958 QLSAYEgGLPTSGNVFISVNDTDKRQLPLFAVRLVELGFQIWATEGTASVLRRYGIESKIVDKItarvdsdpdapvqidk 1037
Cdd:PRK05294  927 QLAAGN-RLPTSGTVFLSVRDRDKEEVVELAKRLLELGFKILATSGTAKFLREAGIPVELVNKV---------------- 989
                        1050      1060      1070      1080      1090      1100      1110
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 651883668 1038 AEGSvgKNVVELIEEGTIDLILNTPNSRGSRSDGYSIRAAAIAADVPQFTTMTEFSAVLLAIEAVKANDYQVMSIQEH 1115
Cdd:PRK05294  990 HEGR--PHIVDLIKNGEIDLVINTPTGRQAIRDGFSIRRAALEYKVPYITTLAGARAAVKAIEALKFGELEVRSLQEY 1065
CPSaseII_lrg TIGR01369
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ...
2-1099 0e+00

carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]


Pssm-ID: 273581 [Multi-domain]  Cd Length: 1050  Bit Score: 1444.81  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668     2 PKRNDIKSVMVIGSGPIVIGQAAEFDYSGTQACRVLREEGIRVILVNSNPATIMTDPEMADATYIEPIATPILERIIAKE 81
Cdd:TIGR01369    1 PKRTDIKKILVIGSGPIVIGQAAEFDYSGSQACKALKEEGYRVILVNSNPATIMTDPEMADKVYIEPLTPEAVEKIIEKE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668    82 RPDALLPTLGGQTALNAAVALGEAGVLKKYNVELIGASLEAIDRGEDRESFKEVVEAAGAESARSDIAHTLEEVDAIAER 161
Cdd:TIGR01369   81 RPDAILPTFGGQTALNLAVELEESGVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEPVPESEIAHSVEEALAAAKE 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   162 FGFPLVVRPSFTMGGLGSGIAHNTEELHRIAGAGIHYSPTDEVLIEEGIEGWKEYELELMRDRNDNVVVVCPIENVDPVG 241
Cdd:TIGR01369  161 IGYPVIVRPAFTLGGTGGGIAYNREELKEIAERALSASPINQVLVEKSLAGWKEIEYEVMRDSNDNCITVCNMENFDPMG 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   242 VHTGDSITVAPVFTLTDREYQKLRDIGIAIIRGVGVDtGGCNIQFAMHPATGRIIVIEMNPRVSRSSALASKATGFPIAK 321
Cdd:TIGR01369  241 VHTGDSIVVAPSQTLTDKEYQMLRDASIKIIRELGIE-GGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAK 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   322 IATKLALGYTLDEIQNDITKSTPASFEPTIDYVVTKVPRFAFEKFPGADPTLTTSMKSVGEAMALAGNFQESLGKAMRSI 401
Cdd:TIGR01369  320 VAAKLAVGYTLDELKNPVTGTTPASFEPSLDYVVVKIPRWDFDKFAGVDRKLGTQMKSVGEVMAIGRTFEEALQKALRSL 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   402 DKRDMGFSWSGEKPGEQEvaELLEAMKVPTEHRYLQIMRAIWGGATEEQIFASTKIDPWFVKQFMLINDTAMQVRD--AE 479
Cdd:TIGR01369  400 EIGATGFDLPDREVEPDE--DLWRALKKPTDRRIFAIAEALRRGVSVDEIHELTKIDRWFLHKIKNIVDLEEELEEvkLT 477
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   480 TLSPRLLKKAKLAGLSDLQIARLRGLGDAgenTVRELRWNYGLHPVYKTVDTCAAEFDAVTPYYYSCYADES-ELRKRDR 558
Cdd:TIGR01369  478 DLDPELLRRAKKLGFSDAQIARLIGVTEA---EVRKLRKELGIMPVYKRVDTCAAEFEAQTPYLYSTYEGERdDVPFTDK 554
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   559 EAVIILGSGPNRIGQGIEFDYTCVHAVQELGKDCD-TIMVNCNPETVSTDYDMSDRLYFEPLTFEDVIEIYEAEKkmgpI 637
Cdd:TIGR01369  555 KKVLVLGSGPNRIGQGVEFDYCCVHAVLALRELGYeTIMINYNPETVSTDYDTSDRLYFEPLTFEDVMNIIELEK----P 630
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   638 KGVIVQLGGQTPLSLAARLKAAGVPILGTTPESIDLAENRELFGEVLRAEKLNAPRFGTALSLEEALDAAHSIGYPVLVR 717
Cdd:TIGR01369  631 EGVIVQFGGQTPLNLAKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKWKTATSVEEAVEFASEIGYPVLVR 710
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   718 PSYVLGGRGMEIVYDDAQLEKYVNRALNeakadtvVSGrlPSPLLIDKFLQDAIEIDVDALFDGDELYIGGIMEHIEEAG 797
Cdd:TIGR01369  711 PSYVLGGRAMEIVYNEEELRRYLEEAVA-------VSP--EHPVLIDKYLEDAVEVDVDAVSDGEEVLIPGIMEHIEEAG 781
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   798 VHSGDAACTLPPSTLSDDQIRRLREATYAIAKGCGVCGLINVQYAFMANTLYVIEANPRASRTVPFASKATGVALAKAAA 877
Cdd:TIGR01369  782 VHSGDSTCVLPPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDGEVYVIEVNPRASRTVPFVSKATGVPLAKLAV 861
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   878 RIMAGETIAQQranGLLLPHGDGGdvrlgqqVAIKESVLPFKRFRtpvgkTVDILLGPEMRSTGEVMGFDRDFPHAFAKS 957
Cdd:TIGR01369  862 RVMLGKKLEEL---GVGKEKEPKY-------VAVKEPVFSFSKLA-----GVDPVLGPEMKSTGEVMGIGRDLAEAFLKA 926
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   958 QLSAYEgGLPTSGNVFISVNDTDKRQLPLFAVRLVELGFQIWATEGTASVLRRYGIESKIVDKITARvdsdpdapvqidk 1037
Cdd:TIGR01369  927 QLSSGN-RIPKKGSVLLSVRDKDKEELLDLARKLAEKGYKLYATEGTAKFLGEAGIKPELVLKVSEG------------- 992
                         1050      1060      1070      1080      1090      1100
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 651883668  1038 aegsvGKNVVELIEEGTIDLILNTP-NSRGSRSDGYSIRAAAIAADVPQFTTMTEFSAVLLAI 1099
Cdd:TIGR01369  993 -----RPNILDLIKNGEIELVINTTsKGAGTATDGYKIRREALDYGVPLITTLNTAEAFAEAL 1050
carB PRK12815
carbamoyl phosphate synthase large subunit; Reviewed
1-1118 0e+00

carbamoyl phosphate synthase large subunit; Reviewed


Pssm-ID: 237215 [Multi-domain]  Cd Length: 1068  Bit Score: 1371.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668    1 MPKRNDIKSVMVIGSGPIVIGQAAEFDYSGTQACRVLREEGIRVILVNSNPATIMTDPEMADATYIEPIATPILERIIAK 80
Cdd:PRK12815    1 MPKDTDIQKILVIGSGPIVIGQAAEFDYSGTQACLALKEEGYQVVLVNPNPATIMTDPAPADTVYFEPLTVEFVKRIIAR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   81 ERPDALLPTLGGQTALNAAVALGEAGVLKKYNVELIGASLEAIDRGEDRESFKEVVEAAGAESARSDIAHTLEEVDAIAE 160
Cdd:PRK12815   81 EKPDALLATLGGQTALNLAVKLHEDGILEQYGVELLGTNIEAIQKGEDRERFRALMKELGEPVPESEIVTSVEEALAFAE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  161 RFGFPLVVRPSFTMGGLGSGIAHNTEELHRIAGAGIHYSPTDEVLIEEGIEGWKEYELELMRDRNDNVVVVCPIENVDPV 240
Cdd:PRK12815  161 KIGFPIIVRPAYTLGGTGGGIAENLEELEQLFKQGLQASPIHQCLLEESIAGWKEIEYEVMRDRNGNCITVCNMENIDPV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  241 GVHTGDSITVAPVFTLTDREYQKLRDIGIAIIRGVGVdTGGCNIQFAMHPATGRIIVIEMNPRVSRSSALASKATGFPIA 320
Cdd:PRK12815  241 GIHTGDSIVVAPSQTLTDDEYQMLRSASLKIISALGV-VGGCNIQFALDPKSKQYYLIEVNPRVSRSSALASKATGYPIA 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  321 KIATKLALGYTLDEIQNDITKSTPASFEPTIDYVVTKVPRFAFEKFPGADPTLTTSMKSVGEAMALAGNFQESLGKAMRS 400
Cdd:PRK12815  320 KIAAKLAVGYTLNELKNPVTGLTYASFEPALDYVVVKFPRWPFDKFGYADRTLGTQMKATGEVMAIGRNFESAFQKALRS 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  401 IDKRDMGFSwSGEKPGEQEVAELLEAMKVPTEHRYLQIMRAIWGGATEEQIFASTKIDPWFVKQFMLINDTAMQVR-DAE 479
Cdd:PRK12815  400 LEIKRNGLS-LPIELSGKSDEELLQDLRHPDDRRLFALLEALRRGITYEEIHELTKIDPFFLQKFEHIVALEKKLAeDGL 478
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  480 TLSPRLLKKAKLAGLSDLQIARLRGLgdaGENTVRELRWNYGLHPVYKTVDTCAAEFDAVTPYYYSCYADESELRK-RDR 558
Cdd:PRK12815  479 DLSADLLRKVKEKGFSDALLAELTGV---TEEEVRALRKKLGIRPSYKMVDTCAAEFEAKTPYYYSTYFGESEAEPsSEK 555
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  559 EAVIILGSGPNRIGQGIEFDYTCVHAVQELGK-DCDTIMVNCNPETVSTDYDMSDRLYFEPLTFEDVIEIYEAEKkmgpI 637
Cdd:PRK12815  556 KKVLILGSGPIRIGQGIEFDYSSVHAAFALKKeGYETIMINNNPETVSTDYDTADRLYFEPLTLEDVLNVAEAEN----I 631
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  638 KGVIVQLGGQTPLSLAARLKAAGVPILGTTPESIDLAENRELFGEVLRAEKLNAPRFGTALSLEEALDAAHSIGYPVLVR 717
Cdd:PRK12815  632 KGVIVQFGGQTAINLAKGLEEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPGLTATDEEEAFAFAKRIGYPVLIR 711
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  718 PSYVLGGRGMEIVYDDAQLEKYvnraLNEAKAdtvvsgrLPSPLLIDKFLqDAIEIDVDALFDGDELYIGGIMEHIEEAG 797
Cdd:PRK12815  712 PSYVIGGQGMAVVYDEPALEAY----LAENAS-------QLYPILIDQFI-DGKEYEVDAISDGEDVTIPGIIEHIEQAG 779
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  798 VHSGDAACTLPPSTLSDDQIRRLREATYAIAKGCGVCGLINVQYAFMANTLYVIEANPRASRTVPFASKATGVALAKAAA 877
Cdd:PRK12815  780 VHSGDSIAVLPPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVLANDEIYVLEVNPRASRTVPFVSKATGVPLAKLAT 859
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  878 RIMAGETIAQQRANGLLLPHGDggdvrlgqQVAIKESVLPFKRFRtpvgkTVDILLGPEMRSTGEVMGFDRDFPHAFAKS 957
Cdd:PRK12815  860 KVLLGKSLAELGYPNGLWPGSP--------FIHVKMPVFSYLKYP-----GVDNTLGPEMKSTGEVMGIDKDLEEALYKG 926
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  958 QlSAYEGGLPTSGNVFISVNDTDKRQLPLFAVRLVELGFQIWATEGTASVLRRYGIESKIVDKITarvdsdpdapvqidk 1037
Cdd:PRK12815  927 Y-EASDLHIPSYGTIFISVRDEDKPEVTKLARRFAQLGFKLLATEGTANWLAEEGITTGVVEKVQ--------------- 990
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 1038 aEGSvgKNVVELIEEGTIDLILNTPNSRGSRSDGYSIRAAAIAADVPQFTTMTEFSAVLLAIEAVKANDYQVMSIQEHAR 1117
Cdd:PRK12815  991 -EGS--PSLLERIKQHRIVLVVNTSLSDSASEDAIKIRDEALSTHIPVFTELETAQAFLQVLESLALTTQPIQELQEKHK 1067

                  .
gi 651883668 1118 E 1118
Cdd:PRK12815 1068 Q 1068
PLN02735 PLN02735
carbamoyl-phosphate synthase
3-1114 0e+00

carbamoyl-phosphate synthase


Pssm-ID: 215391 [Multi-domain]  Cd Length: 1102  Bit Score: 1269.70  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668    3 KRNDIKSVMVIGSGPIVIGQAAEFDYSGTQACRVLREEGIRVILVNSNPATIMTDPEMADATYIEPIATPILERIIAKER 82
Cdd:PLN02735   19 KRTDLKKIMILGAGPIVIGQACEFDYSGTQACKALKEEGYEVVLINSNPATIMTDPETADRTYIAPMTPELVEQVIAKER 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   83 PDALLPTLGGQTALNAAVALGEAGVLKKYNVELIGASLEAIDRGEDRESFKEVVEAAGAESARSDIAHTLEEVDAIAERF 162
Cdd:PLN02735   99 PDALLPTMGGQTALNLAVALAESGILEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPPSGIATTLDECFEIAEDI 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  163 G-FPLVVRPSFTMGGLGSGIAHNTEELHRIAGAGIHYSPTDEVLIEEGIEGWKEYELELMRDRNDNVVVVCPIENVDPVG 241
Cdd:PLN02735  179 GeFPLIIRPAFTLGGTGGGIAYNKEEFETICKAGLAASITSQVLVEKSLLGWKEYELEVMRDLADNVVIICSIENIDPMG 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  242 VHTGDSITVAPVFTLTDREYQKLRDIGIAIIRGVGVDTGGCNIQFAMHPATGRIIVIEMNPRVSRSSALASKATGFPIAK 321
Cdd:PLN02735  259 VHTGDSITVAPAQTLTDKEYQRLRDYSVAIIREIGVECGGSNVQFAVNPVDGEVMIIEMNPRVSRSSALASKATGFPIAK 338
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  322 IATKLALGYTLDEIQNDITKSTPASFEPTIDYVVTKVPRFAFEKFPGADPTLTTSMKSVGEAMALAGNFQESLGKAMRSI 401
Cdd:PLN02735  339 MAAKLSVGYTLDQIPNDITLKTPASFEPSIDYVVTKIPRFAFEKFPGSQPILTTQMKSVGEAMALGRTFQESFQKALRSL 418
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  402 dkrDMGFS-WSGEKPGEQE--VAELLEAMKVPTEHRYLQIMRAIWGGATEEQIFASTKIDPWFVKQFMLINDTA--MQVR 476
Cdd:PLN02735  419 ---ETGFSgWGCAKVKELDwdWEQLKYKLRVPNPDRIHAIYAAMKKGMTVDEIHELTFIDPWFLTQLKELVDVEqfLKSR 495
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  477 DAETLSPRLLKKAKLAGLSDLQIARLRGlgdAGENTVRELRWNYGLHPVYKTVDTCAAEFDAVTPYYYSCYADESELRKR 556
Cdd:PLN02735  496 SLSELSKDDFYEVKRRGFSDKQIAFATK---STEKEVRSKRLSLGVTPSYKRVDTCAAEFEANTPYMYSSYDGECESAPT 572
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  557 DREAVIILGSGPNRIGQGIEFDYTCVHAVQELGK-DCDTIMVNCNPETVSTDYDMSDRLYFEPLTFEDVIEIYEAEKKmg 635
Cdd:PLN02735  573 NKKKVLILGGGPNRIGQGIEFDYCCCHASFALQDaGYETIMMNSNPETVSTDYDTSDRLYFEPLTVEDVLNVIDLERP-- 650
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  636 piKGVIVQLGGQTPLSLAARLK----------AAG---VPILGTTPESIDLAENRELFGEVLRAEKLNAPRFGTALSLEE 702
Cdd:PLN02735  651 --DGIIVQFGGQTPLKLALPIQkyldknpppsASGngnVKIWGTSPDSIDAAEDRERFNAILNELKIEQPKGGIARSEAD 728
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  703 ALDAAHSIGYPVLVRPSYVLGGRGMEIVYDDAQLEKYVNRALNeakadtVVSGRlpsPLLIDKFLQDAIEIDVDALFDGD 782
Cdd:PLN02735  729 ALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDKLKTYLETAVE------VDPER---PVLVDKYLSDATEIDVDALADSE 799
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  783 -ELYIGGIMEHIEEAGVHSGDAACTLPPSTLSDDQIRRLREATYAIAKGCGVCGLINVQYAF-MANTLYVIEANPRASRT 860
Cdd:PLN02735  800 gNVVIGGIMEHIEQAGVHSGDSACSLPTQTIPSSCLATIRDWTTKLAKRLNVCGLMNCQYAItPSGEVYIIEANPRASRT 879
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  861 VPFASKATGVALAKAAARIMAGETIAQQRANGLLLPhgdggdvrlgQQVAIKESVLPFKRFrtpvgKTVDILLGPEMRST 940
Cdd:PLN02735  880 VPFVSKAIGHPLAKYASLVMSGKSLKDLGFTEEVIP----------AHVSVKEAVLPFDKF-----QGCDVLLGPEMRST 944
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  941 GEVMGFDRDFPHAFAKSQLSAYEgGLPTSGNVFISVNDTDKRQLPLFAVRLVELGFQIWATEGTASVLRRYGIESKIVDK 1020
Cdd:PLN02735  945 GEVMGIDYEFSKAFAKAQIAAGQ-RLPLSGTVFISLNDLTKPHLVPIARGFLELGFRIVSTSGTAHFLELAGIPVERVLK 1023
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 1021 ItarvdsdpdapvqidkAEGSvgKNVVELIEEGTIDLILNTPNSRG-SRSDGYSIRAAAIAADVPQFTTMTEFSAVLLAI 1099
Cdd:PLN02735 1024 L----------------HEGR--PHAGDMLANGQIQLMVITSSGDAlDQKDGRQLRRMALAYKVPIITTVAGALATAQAV 1085
                        1130
                  ....*....|....*
gi 651883668 1100 EAVKANDYQVMSIQE 1114
Cdd:PLN02735 1086 KSLKECPIEMIALQD 1100
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
13-566 0e+00

Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440226 [Multi-domain]  Cd Length: 536  Bit Score: 699.32  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   13 IGSGPIVIGQAAEFDYSGTQACRVLREEGIRVILVNSNPATIMTDPEMADATYIEPIATPILERIIAKERPDALLPTLGG 92
Cdd:COG0458     1 IGSGPIRIGQGIEFDYSGVQACKALREEGYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEKPDGVIVQFGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   93 QTALNAAVALGEAGVLKkyNVELIGASLEAIDRGEDRESFKEVVEAAGAESARSDIAHTLEEVDAIAERFGFPLVVRPSF 172
Cdd:COG0458    81 QTALNLAVELEEAGILE--GVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRPSY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  173 TMGGLGSGIAHNTEELHRIAGAGIHYSPTDEVLIEEGIEGWKEYELELMRDRNDNVVVVCPIENVDPVGVHTGDSITVAP 252
Cdd:COG0458   159 VLGGRGMGIVYNEEELEEYLERALKVSPDHPVLIDESLLGAKEIEVDVVRDGEDNVIIVGIMEHIEPAGVHSGDSICVAP 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  253 VFTLTDREYQKLRDIGIAIIRGVGVDtGGCNIQFAMHpaTGRIIVIEMNPRVSRSSALASKATGFPIAKIATKLALGYTL 332
Cdd:COG0458   239 PQTLSDKEYQRLRDATLKIARALGVV-GLCNIQFAVD--DGRVYVIEVNPRASRSSPFASKATGYPIAKIAAKLALGYTL 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  333 DEIQNDiTKstpasFEPTIDYVVTKVPRFAFEKFPGADPTLTTSMKSVGEAMALAGNFQESLGKAMRSIDKRDMGFSWSG 412
Cdd:COG0458   316 DELGND-TG-----FEPTLDYVVVKEPVFPFEKFPGVDPVLGPEMKSTGEVMGIGRTFEEALQKALRSLEIGLPGTVLLS 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  413 EKPGEQEVAELLEAmkvPTEHRYLQIMRAIWGGATEEQIFASTKIDPWFVKQFMLINDTAMQVRDaETLSPRLLKKAKLA 492
Cdd:COG0458   390 LVADDDKEEALLLA---RRLARLGFLIEATRGTAEVLEEAGITVIDVFKLSEGRPIIVDEIELEE-IILVINTLLGAKSL 465
                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 651883668  493 GLSDLQIARLRglgDAGENTVRELRWNYGLHPVYKTVDTCAAEFDAVTPYYYSCYADESELRKRDREAVIILGS 566
Cdd:COG0458   466 GDSDGIIRRAL---AAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYYYSTYEYENESEETEEPKVVVIGS 536
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
564-1116 0e+00

Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440226 [Multi-domain]  Cd Length: 536  Bit Score: 653.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  564 LGSGPNRIGQGIEFDYTCVHAVQELGKD-CDTIMVNCNPETVSTDYDMSDRLYFEPLTFEDVIEIYEAEKkmgpIKGVIV 642
Cdd:COG0458     1 IGSGPIRIGQGIEFDYSGVQACKALREEgYEVILVNSNPETVSTDYDTADRLYFEPLTVEDVLDIIEKEK----PDGVIV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  643 QLGGQTPLSLAARLKAA----GVPILGTTPESIDLAENRELFGEVLRAEKLNAPRFGTALSLEEALDAAHSIGYPVLVRP 718
Cdd:COG0458    77 QFGGQTALNLAVELEEAgileGVKILGTSPDAIDLAEDRELFKELLDKLGIPQPKSGTATSVEEALAIAEEIGYPVIVRP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  719 SYVLGGRGMEIVYDDAQLEKYVNRALNeakadtvVSGRlpSPLLIDKFLQDAIEIDVDALFDG-DELYIGGIMEHIEEAG 797
Cdd:COG0458   157 SYVLGGRGMGIVYNEEELEEYLERALK-------VSPD--HPVLIDESLLGAKEIEVDVVRDGeDNVIIVGIMEHIEPAG 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  798 VHSGDAACTLPPSTLSDDQIRRLREATYAIAKGCGVCGLINVQYAFMANTLYVIEANPRASRTVPFASKATGVALAKAAA 877
Cdd:COG0458   228 VHSGDSICVAPPQTLSDKEYQRLRDATLKIARALGVVGLCNIQFAVDDGRVYVIEVNPRASRSSPFASKATGYPIAKIAA 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  878 RIMAGETIAQQRANGLLLPHGDggdvrlgqQVAIKESVLPFKRFrtpvgKTVDILLGPEMRSTGEVMGFDRDFPHAFAKS 957
Cdd:COG0458   308 KLALGYTLDELGNDTGFEPTLD--------YVVVKEPVFPFEKF-----PGVDPVLGPEMKSTGEVMGIGRTFEEALQKA 374
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  958 QLSAyEGGLPtsGNVFIS-VNDTDKRQLPLFAVRLVELGFQIWATEGTASVLRRYGIESKIVDKITarvdsdpdapvqid 1036
Cdd:COG0458   375 LRSL-EIGLP--GTVLLSlVADDDKEEALLLARRLARLGFLIEATRGTAEVLEEAGITVIDVFKLS-------------- 437
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668 1037 kaEGSvgKNVVELIEEGTIDLILNTPNSRGSRSDGYSIRAAAIAADVPQFTTMTEFSAVLLAIEAVKANDYQVMSIQEHA 1116
Cdd:COG0458   438 --EGR--PIIVDEIELEEIILVINTLLGAKSLGDSDGIIRRALAAKVPYVTTLAAAAAAALAIKAVETEAGEFEEATAYY 513
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
128-333 1.04e-71

Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.


Pssm-ID: 397079 [Multi-domain]  Cd Length: 209  Bit Score: 237.59  E-value: 1.04e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   128 DRESFKEVVEAAGAESARSDIA--HTLEEVDAIAERFGFPLVVRPSFTMGGLGSGIAHNTEELHRIAGAGIHYSPT---- 201
Cdd:pfam02786    1 DKVLFKAAMKEAGVPTVPGTAGpvETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAafgn 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   202 DEVLIEEGIEGWKEYELELMRDRNDNVVVVCPIENVDPVgvHTGDSITVAPVFTLTDREYQKLRDIGIAIIRGVGVdTGG 281
Cdd:pfam02786   81 PQVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQR--RTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGY-VGA 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 651883668   282 CNIQFAMHPATGRIIVIEMNPRVSRSSALASKATGFPIAKIATKLALGYTLD 333
Cdd:pfam02786  158 GTVEFALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
CPSase_L_D3 smart01096
Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate ...
423-547 1.54e-43

Carbamoyl-phosphate synthetase large chain, oligomerisation domain; Carbamoyl-phosphate synthase catalyses the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain.


Pssm-ID: 198164 [Multi-domain]  Cd Length: 124  Bit Score: 154.14  E-value: 1.54e-43
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668    423 LLEAMKVPTEHRYLQIMRAIWGGATEEQIFASTKIDPWFVKQFMLINDTAMQVRD--AETLSPRLLKKAKLAGLSDLQIA 500
Cdd:smart01096    1 LLEELRTPTDERLFYIAEALRRGYSVDEIHELTKIDPWFLEKIKEIVELEKELKKggLDELDADLLRKAKRLGFSDRQIA 80
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*..
gi 651883668    501 RLRGLGdagENTVRELRWNYGLHPVYKTVDTCAAEFDAVTPYYYSCY 547
Cdd:smart01096   81 KLLGVT---EAEVRALRKELGIRPVYKRVDTCAAEFPANTPYYYSTY 124
CPSase_L_D2 pfam02786
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
695-885 2.90e-37

Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.


Pssm-ID: 397079 [Multi-domain]  Cd Length: 209  Bit Score: 139.36  E-value: 2.90e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   695 GTALSLEEALDAAHSIGYPVLVRPSYVLGGRGMEIVYDDAQLEKYVNRALNEAKADTVVSGrlpspLLIDKFLQDAIEID 774
Cdd:pfam02786   22 GPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGNPQ-----VLVEKSLKGPKHIE 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   775 VDALFDG-DELYIGGIMEHIEEagVHSGDAACTLPPSTLSDDQIRRLREATYAIAKGCGVCGLINVQYAF--MANTLYVI 851
Cdd:pfam02786   97 YQVLRDAhGNCITVCNRECSDQ--RRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVEFALdpFSGEYYFI 174
                          170       180       190
                   ....*....|....*....|....*....|....
gi 651883668   852 EANPRASRTVPFASKATGVALAKAAARIMAGETI 885
Cdd:pfam02786  175 EMNTRLQVEHALAEKATGYDLAKEAAKIALGYPL 208
MGS_CPS_II cd01424
Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate ...
970-1096 2.34e-36

Methylglyoxal synthase-like domain from type II glutamine-dependent carbamoyl phosphate synthetase (CSP). CSP, a CarA and CarB heterodimer, catalyzes the production of carbamoyl phosphate which is subsequently employed in the metabolic pathways responsible for the synthesis of pyrimidine nucleotides or arginine. The MGS-like domain is the C-terminal domain of CarB and appears to play a regulatory role in CPS function by binding allosteric effector molecules, including UMP and ornithine.


Pssm-ID: 238712 [Multi-domain]  Cd Length: 110  Bit Score: 132.99  E-value: 2.34e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  970 GNVFISVNDTDKRQLPLFAVRLVELGFQIWATEGTASVLRRYGIESKIVDKItarvdsdpdapvqidkAEGSvgKNVVEL 1049
Cdd:cd01424     1 GTVFISVADRDKPEAVEIAKRLAELGFKLVATEGTAKYLQEAGIPVEVVNKV----------------SEGR--PNIVDL 62
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 651883668 1050 IEEGTIDLILNTPNSRGSRSDGYSIRAAAIAADVPQFTTMTEFSAVL 1096
Cdd:cd01424    63 IKNGEIQLVINTPSGKRAIRDGFSIRRAALEYKVPYFTTLDTARAAV 109
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
74-329 6.38e-27

Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440208 [Multi-domain]  Cd Length: 263  Bit Score: 111.12  E-value: 6.38e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   74 LERIIAKERPDALLptlggqtALNAAVALGEAGVLKKYNveLIGASLEAIDRGEDRESFKEVVEAAGAESARSDIAHTLE 153
Cdd:COG0439     9 AAELARETGIDAVL-------SESEFAVETAAELAEELG--LPGPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSPE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  154 EVDAIAERFGFPLVVRPSFTMGGLGSGIAHNTEEL----HRIAGAGIHYSPTDEVLIEEGIEGwKEYELE-LMRDRNdnv 228
Cdd:COG0439    80 EALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELeaalAEARAEAKAGSPNGEVLVEEFLEG-REYSVEgLVRDGE--- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  229 VVVCPI---ENVDPVGVHTGDsitVAPVFtLTDREYQKLRDIGIAIIRGVGVDTGGCNIQFAMHPAtGRIIVIEMNPRVS 305
Cdd:COG0439   156 VVVCSItrkHQKPPYFVELGH---EAPSP-LPEELRAEIGELVARALRALGYRRGAFHTEFLLTPD-GEPYLIEINARLG 230
                         250       260
                  ....*....|....*....|....*.
gi 651883668  306 --RSSALASKATGFPIAKIATKLALG 329
Cdd:COG0439   231 geHIPPLTELATGVDLVREQIRLALG 256
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
622-883 1.45e-26

Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440208 [Multi-domain]  Cd Length: 263  Bit Score: 110.35  E-value: 1.45e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  622 EDVIEIYEAEKKMGPIKGVIVqlGGQTPLSLAARL-KAAGVPilGTTPESIDLAENRELFGEVLRAEKLNAPRFGTALSL 700
Cdd:COG0439     3 DAIIAAAAELARETGIDAVLS--ESEFAVETAAELaEELGLP--GPSPEAIRAMRDKVLMREALAAAGVPVPGFALVDSP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  701 EEALDAAHSIGYPVLVRPSYVLGGRGMEIVYDDAQLEKYVNRALNEAKAdtvvsGRLPSPLLIDKFLqDAIEIDVDALFD 780
Cdd:COG0439    79 EEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKA-----GSPNGEVLVEEFL-EGREYSVEGLVR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  781 GDELYIGGIMEHIEEA--GVHSGDAActlpPSTLSDDQIRRLREATYAIAKGCGV-CGLINVQYAFMAN-TLYVIEANPR 856
Cdd:COG0439   153 DGEVVVCSITRKHQKPpyFVELGHEA----PSPLPEELRAEIGELVARALRALGYrRGAFHTEFLLTPDgEPYLIEINAR 228
                         250       260
                  ....*....|....*....|....*....
gi 651883668  857 AS--RTVPFASKATGVALAKAAARIMAGE 883
Cdd:COG0439   229 LGgeHIPPLTELATGVDLVREQIRLALGE 257
CPSase_L_D3 pfam02787
Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate ...
425-502 7.21e-20

Carbamoyl-phosphate synthetase large chain, oligomerization domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain.


Pssm-ID: 460695  Cd Length: 79  Bit Score: 84.74  E-value: 7.21e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 651883668   425 EAMKVPTEHRYLQIMRAIWGGATEEQIFASTKIDPWFVKQFMLINDTAMQVRDA-ETLSPRLLKKAKLAGLSDLQIARL 502
Cdd:pfam02787    1 EELRTPTDERLFAIAEALRRGYSVEEIHELTKIDPWFLDKIKNIVELEKELKEAgLDLDAELLREAKRLGFSDRQIAKL 79
COG3919 COG3919
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
17-329 4.39e-19

Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];


Pssm-ID: 443124 [Multi-domain]  Cd Length: 382  Bit Score: 90.76  E-value: 4.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   17 PIVIGqaaeFDYSGTQACRVLREEGIRVILVNSNPATIMT------------DPEMADATYIEpiatpILERIIAKERPD 84
Cdd:COG3919     8 VVVLG----GDINALAVARSLGEAGVRVIVVDRDPLGPAArsryvdevvvvpDPGDDPEAFVD-----ALLELAERHGPD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   85 ALLPTlgGQTALNAAVALGEAgvLKKYnVELIGASLEAIDRGEDRESFKEVVEAAGAESARSDIAHTLEEVDAIAERFGF 164
Cdd:COG3919    79 VLIPT--GDEYVELLSRHRDE--LEEH-YRLPYPDADLLDRLLDKERFYELAEELGVPVPKTVVLDSADDLDALAEDLGF 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  165 PLVVRPS--------FTMGGLGSGIAHNTEEL----HRIAGAGIhysptdEVLIEEGIEGWKEYE--LELMRDRNDNVVV 230
Cdd:COG3919   154 PVVVKPAdsvgydelSFPGKKKVFYVDDREELlallRRIAAAGY------ELIVQEYIPGDDGEMrgLTAYVDRDGEVVA 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  231 VCpienvdpVG-VHTGDSITV-APVFTLTdREYQKLRDIGIAIIRGVGVdTGGCNIQFAMHPATGRIIVIEMNPRVSRSS 308
Cdd:COG3919   228 TF-------TGrKLRHYPPAGgNSAARES-VDDPELEEAARRLLEALGY-HGFANVEFKRDPRDGEYKLIEINPRFWRSL 298
                         330       340
                  ....*....|....*....|.
gi 651883668  309 ALASKAtGFPIAKIATKLALG 329
Cdd:COG3919   299 YLATAA-GVNFPYLLYDDAVG 318
MGS pfam02142
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ...
987-1087 7.81e-18

MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the domain is also found in Carbamoyl phosphate synthetase (CPS) where it forms a regulatory domain that binds to the allosteric effector ornithine. This family also includes inosicase. The known structures in this family show a common phosphate binding site.


Pssm-ID: 460462 [Multi-domain]  Cd Length: 93  Bit Score: 79.46  E-value: 7.81e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   987 FAVRLVELGFQIWATEGTASVLRRYGIESKIVDKITArvDSDPDAPVQIdkaegsvgknvVELIEEGTIDLILNTPNS-R 1065
Cdd:pfam02142    5 LAKALVELGFELLATGGTAKFLREAGIPVTEVVEKTG--EGRPGGRVQI-----------GDLIKNGEIDLVINTLYPfK 71
                           90       100
                   ....*....|....*....|..
gi 651883668  1066 GSRSDGYSIRAAAIAADVPQFT 1087
Cdd:pfam02142   72 ATVHDGYAIRRAAENIDIPGPT 93
MGS smart00851
MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the ...
987-1087 4.51e-17

MGS-like domain; This domain composes the whole protein of methylglyoxal synthetase and the domain is also found in Carbamoyl phosphate synthetase (CPS) where it forms a regulatory domain that binds to the allosteric effector ornithine. This family also includes inosicase. The known structures in this family show a common phosphate binding site.


Pssm-ID: 214855 [Multi-domain]  Cd Length: 91  Bit Score: 77.13  E-value: 4.51e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668    987 FAVRLVELGFQIWATEGTASVLRRYGIE--SKIVDKITarvdsdpdapvqidkaEGSvgKNVVELIEEGTIDLILNT--P 1062
Cdd:smart00851    5 FAKRLAELGFELLATGGTAKFLREAGLPvvKTLHPKVH----------------GGI--PQILDLIKNGEIDLVINTlyP 66
                            90       100
                    ....*....|....*....|....*
gi 651883668   1063 NSRGSRSDGYSIRAAAIAADVPQFT 1087
Cdd:smart00851   67 FEAQAHEDGYSIRRAAENIDIPGPT 91
PRK12833 PRK12833
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
653-883 6.24e-17

acetyl-CoA carboxylase biotin carboxylase subunit; Provisional


Pssm-ID: 183781 [Multi-domain]  Cd Length: 467  Bit Score: 85.19  E-value: 6.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  653 AARLKAAGVPILGTTPESI----DLAENRELfgevlrAEKLNAPRF----GTALSLEEALDAAHSIGYPVLVRPSYVLGG 724
Cdd:PRK12833   95 AEAVEAAGLIFVGPDAQTIrtmgDKARARRT------ARRAGVPTVpgsdGVVASLDAALEVAARIGYPLMIKAAAGGGG 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  725 RGMEIVYDDAQLEKYVNRALNEAKADTVVSGrlpspLLIDKFLQDAIEIDVDALFDGdelyiggimehieEAGVHSGDAA 804
Cdd:PRK12833  169 RGIRVAHDAAQLAAELPLAQREAQAAFGDGG-----VYLERFIARARHIEVQILGDG-------------ERVVHLFERE 230
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  805 CTL-----------PPSTLSDDQIRRLREATYAIAKGCGVCGLINVQYAFMANT--LYVIEANPRASRTVPFASKATGVA 871
Cdd:PRK12833  231 CSLqrrrqkileeaPSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDDARgeFYFIEMNTRIQVEHPVTEAITGID 310
                         250
                  ....*....|..
gi 651883668  872 LAKAAARIMAGE 883
Cdd:PRK12833  311 LVQEMLRIADGE 322
MGS_CPS_I_III cd01423
Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases ...
971-1100 1.32e-13

Methylglyoxal synthase-like domain found in pyr1 and URA1-like carbamoyl phosphate synthetases (CPS), including ammonia-dependent CPS Type I, and glutamine-dependent CPS Type III. These are multidomain proteins, in which MGS is the C-terminal domain.


Pssm-ID: 238711 [Multi-domain]  Cd Length: 116  Bit Score: 68.10  E-value: 1.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  971 NVFISVNDTDKRQLPLFAVRLVELGFQIWATEGTASVLRRYGIESKIVDKITArvDSDPDAPVQidkaegsvgknvVELI 1050
Cdd:cd01423     2 GILISIGSYSKPELLPTAQKLSKLGYKLYATEGTADFLLENGIPVTPVAWPSE--EPQNDKPSL------------RELL 67
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 651883668 1051 EEGTIDLILNTPNSRGSR--SDGYSIRAAAIAADVPQFttmTEFSAVLLAIE 1100
Cdd:cd01423    68 AEGKIDLVINLPSNRGKRvlDNDYVMRRAADDFAVPLI---TNPKCAKLFIE 116
PRK06111 PRK06111
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
635-888 1.52e-13

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 180406 [Multi-domain]  Cd Length: 450  Bit Score: 74.29  E-value: 1.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  635 GPIKGVIVQLGGQtplsLAAR--LKAAGVPILGTTPESIDlaenrelfgevlraeklnaprfgtalSLEEALDAAHSIGY 712
Cdd:PRK06111  104 GPSADIIAKMGSK----IEARraMQAAGVPVVPGITTNLE--------------------------DAEEAIAIARQIGY 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  713 PVLVRPSYVLGGRGMEIVYDDAQLEKYVnrALNEAKADTVVSGrlpSPLLIDKFLQDA--IEIDVDALFDGDELYIG--- 787
Cdd:PRK06111  154 PVMLKASAGGGGIGMQLVETEQELTKAF--ESNKKRAANFFGN---GEMYIEKYIEDPrhIEIQLLADTHGNTVYLWere 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  788 -GIMEH----IEEAgvhsgdaactlpPSTLSDDQIR-RLREATYAIAKGCGVCGLINVQYAF-MANTLYVIEANPRASRT 860
Cdd:PRK06111  229 cSVQRRhqkvIEEA------------PSPFLDEETRkAMGERAVQAAKAIGYTNAGTIEFLVdEQKNFYFLEMNTRLQVE 296
                         250       260       270
                  ....*....|....*....|....*....|
gi 651883668  861 VPFASKATGVALAKAAARIMAGE--TIAQQ 888
Cdd:PRK06111  297 HPVTEEITGIDLVEQQLRIAAGEklSFTQD 326
PRK12767 PRK12767
carbamoyl phosphate synthase-like protein; Provisional
60-314 3.13e-13

carbamoyl phosphate synthase-like protein; Provisional


Pssm-ID: 237195 [Multi-domain]  Cd Length: 326  Bit Score: 72.22  E-value: 3.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   60 MADATYIEPIAT-----PILERIIAKERPDALLPTLGGQTALNAAvalgEAGVLKKYNVELIGASLEAIDRGEDRESFKE 134
Cdd:PRK12767   42 FADKFYVVPKVTdpnyiDRLLDICKKEKIDLLIPLIDPELPLLAQ----NRDRFEEIGVKVLVSSKEVIEICNDKWLTYE 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  135 VVEAAGAESARSDIAHTLEEVDAI--AERFGFPLVVRPSFTMGGLGSGIAHNTEELHRIagagIHYSPtdEVLIEEGIEG 212
Cdd:PRK12767  118 FLKENGIPTPKSYLPESLEDFKAAlaKGELQFPLFVKPRDGSASIGVFKVNDKEELEFL----LEYVP--NLIIQEFIEG 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  213 wKEYELELMRDRNDNVVVVCPIENVDPVGVHTGDSITVapvftltdrEYQKLRDIGIAIIRGVGVDtGGCNIQFAMHPat 292
Cdd:PRK12767  192 -QEYTVDVLCDLNGEVISIVPRKRIEVRAGETSKGVTV---------KDPELFKLAERLAEALGAR-GPLNIQCFVTD-- 258
                         250       260
                  ....*....|....*....|..
gi 651883668  293 GRIIVIEMNPRVSRSSALASKA 314
Cdd:PRK12767  259 GEPYLFEINPRFGGGYPLSYMA 280
PRK12767 PRK12767
carbamoyl phosphate synthase-like protein; Provisional
622-888 1.88e-12

carbamoyl phosphate synthase-like protein; Provisional


Pssm-ID: 237195 [Multi-domain]  Cd Length: 326  Bit Score: 69.91  E-value: 1.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  622 EDVIEIYEAEKkmgpIKGVIVqlGGQTPLSLAA----RLKAAGVPILGTTPESIDLAENRELFGEVLRAEKLNAPRFGTA 697
Cdd:PRK12767   59 DRLLDICKKEK----IDLLIP--LIDPELPLLAqnrdRFEEIGVKVLVSSKEVIEICNDKWLTYEFLKENGIPTPKSYLP 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  698 LSLEEAL--DAAHSIGYPVLVRPSYVLGGRGMEIVYDDAQLEKYVNRALNeakadtvvsgrlpspLLIDKFLQDaIEIDV 775
Cdd:PRK12767  133 ESLEDFKaaLAKGELQFPLFVKPRDGSASIGVFKVNDKEELEFLLEYVPN---------------LIIQEFIEG-QEYTV 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  776 DALFDGDELYIGGI-MEHIEeagVHSG--DAACTLPPSTLsDDQIRRLREATYAIakgcgvcGLINVQYAFMANTLYVIE 852
Cdd:PRK12767  197 DVLCDLNGEVISIVpRKRIE---VRAGetSKGVTVKDPEL-FKLAERLAEALGAR-------GPLNIQCFVTDGEPYLFE 265
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 651883668  853 ANPRASRTVPFASKAtGVALAKAAARIMAGETIAQQ 888
Cdd:PRK12767  266 INPRFGGGYPLSYMA-GANEPDWIIRNLLGGENEPI 300
PRK08654 PRK08654
acetyl-CoA carboxylase biotin carboxylase subunit;
635-883 2.52e-12

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236325 [Multi-domain]  Cd Length: 499  Bit Score: 70.78  E-value: 2.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  635 GPIKGVIVQLGGQtplsLAAR--LKAAGVPILGTTPESIDlaenrelfgevlraeklnaprfgtalSLEEALDAAHSIGY 712
Cdd:PRK08654  104 GPSSDVIEAMGSK----INAKklMKKAGVPVLPGTEEGIE--------------------------DIEEAKEIAEEIGY 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  713 PVLVRPSYVLGGRGMEIVYDDAQLEKYVNRALNEAKA---DTVVsgrlpsplLIDKFLQDA--IEIDVDALFDGDELYIG 787
Cdd:PRK08654  154 PVIIKASAGGGGIGMRVVYSEEELEDAIESTQSIAQSafgDSTV--------FIEKYLEKPrhIEIQILADKHGNVIHLG 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  788 ----GIM-EH---IEEAgvhsgdaactlpPSTLSDDQIR-RLREATYAIAKGCGVCGLINVQYAFMANTLYVIEANPRAS 858
Cdd:PRK08654  226 drecSIQrRHqklIEEA------------PSPIMTPELReRMGEAAVKAAKAINYENAGTVEFLYSNGNFYFLEMNTRLQ 293
                         250       260
                  ....*....|....*....|....*
gi 651883668  859 RTVPFASKATGVALAKAAARIMAGE 883
Cdd:PRK08654  294 VEHPITEMVTGIDIVKEQIKIAAGE 318
PRK12999 PRK12999
pyruvate carboxylase; Reviewed
652-886 8.13e-12

pyruvate carboxylase; Reviewed


Pssm-ID: 237263 [Multi-domain]  Cd Length: 1146  Bit Score: 69.78  E-value: 8.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  652 LAARLKAAGVPILGTTPESIDLAEN----RELfgevlrAEKLNAPRF-GT---ALSLEEALDAAHSIGYPVLVRPSYVLG 723
Cdd:PRK12999   95 FARACAEAGITFIGPTAEVLRLLGDkvaaRNA------AIKAGVPVIpGSegpIDDIEEALEFAEEIGYPIMLKASAGGG 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  724 GRGMEIVYDDAQLEKYVNRALNEAKA----DTVvsgrlpsplLIDKFLQDAIEIDVDALfdGDELyiGGIMeHIEEAgvh 799
Cdd:PRK12999  169 GRGMRIVRSEEELEEAFERAKREAKAafgnDEV---------YLEKYVENPRHIEVQIL--GDKH--GNVV-HLYER--- 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  800 sgDaaCTL-----------PPSTLSDDQIRRLREATYAIAKGCGVCGLINVQyaF---MANTLYVIEANPR--ASRTVpf 863
Cdd:PRK12999  232 --D--CSVqrrhqkvveiaPAPGLSEELRERICEAAVKLARAVGYVNAGTVE--FlvdADGNFYFIEVNPRiqVEHTV-- 303
                         250       260
                  ....*....|....*....|...
gi 651883668  864 ASKATGVALAKAAARIMAGETIA 886
Cdd:PRK12999  304 TEEVTGIDIVQSQILIAEGATLH 326
PRK05586 PRK05586
acetyl-CoA carboxylase biotin carboxylase subunit;
664-886 1.21e-11

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180150 [Multi-domain]  Cd Length: 447  Bit Score: 68.20  E-value: 1.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  664 LGTTPESIDLAENRELFGEVLRaeKLNAPRF----GTALSLEEALDAAHSIGYPVLVRPSYVLGGRGMEIVYDDAQLEKY 739
Cdd:PRK05586  103 IGPDSETIELMGNKSNAREIMI--KAGVPVVpgseGEIENEEEALEIAKEIGYPVMVKASAGGGGRGIRIVRSEEELIKA 180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  740 VNRALNEAKA----DTvvsgrlpspLLIDKFLQDAIEIDVDALfdGDELyiGGImehieeagVHSGDAACTL-------- 807
Cdd:PRK05586  181 FNTAKSEAKAafgdDS---------MYIEKFIENPKHIEFQIL--GDNY--GNV--------VHLGERDCSLqrrnqkvl 239
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  808 ---PPSTLSDDQIRRLREATYAIAKGCGVCGLINVQYAF-MANTLYVIEANPRASRTVPFASKATGVALAKAAARIMAGE 883
Cdd:PRK05586  240 eeaPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLdKDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGE 319

                  ...
gi 651883668  884 TIA 886
Cdd:PRK05586  320 KLS 322
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
653-886 1.76e-11

Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440660 [Multi-domain]  Cd Length: 1144  Bit Score: 68.95  E-value: 1.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  653 AARL--KAAGVPILGTTPESIDlaenrelfgevlraeklnaprfgtalSLEEALDAAHSIGYPVLVRPSYVLGGRGMEIV 730
Cdd:COG1038   121 AARAaaIEAGVPVIPGTEGPVD--------------------------DLEEALAFAEEIGYPVMLKAAAGGGGRGMRVV 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  731 YDDAQLEKYVNRALNEAKA----DTVvsgrlpsplLIDKFLQDAIEIDVDALfdGDELyiGGIMeH-------------- 792
Cdd:COG1038   175 RSEEELEEAFESARREAKAafgdDEV---------FLEKYIERPKHIEVQIL--GDKH--GNIV-Hlferdcsvqrrhqk 240
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  793 -IEEAgvhsgdaactlPPSTLSDDQIRRLREATYAIAKgcgvcgliNVQYA------FM---ANTLYVIEANPR--ASRT 860
Cdd:COG1038   241 vVEIA-----------PAPNLDEELREAICEAAVKLAK--------AVGYVnagtveFLvddDGNFYFIEVNPRiqVEHT 301
                         250       260
                  ....*....|....*....|....*.
gi 651883668  861 VpfASKATGVALAKAAARIMAGETIA 886
Cdd:COG1038   302 V--TEEVTGIDIVQSQILIAEGYSLD 325
DdlA COG1181
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ...
21-302 2.14e-11

D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, General function prediction only]; D-alanine-D-alanine ligase or related ATP-grasp enzyme is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440794 [Multi-domain]  Cd Length: 303  Bit Score: 66.28  E-value: 2.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   21 GQAAEFD---YSGTQACRVLREEGIRVILVNSNPATIMTDpemadatyiepiatpileriIAKERPDALLPTLGGqtaln 97
Cdd:COG1181     9 GRSAEREvslKSGRAVAAALDKAGYDVVPIGIDVEDLPAA--------------------LKELKPDVVFPALHG----- 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   98 aavALGE----AGVLKKYNVELIGASLEAIDRGEDRESFKEVVEAAGAESARSDI--AHTLEEVDAIAERFGFPLVVRPS 171
Cdd:COG1181    64 ---RGGEdgtiQGLLELLGIPYTGSGVLASALAMDKALTKRVLAAAGLPTPPYVVlrRGELADLEAIEEELGLPLFVKPA 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  172 FtmggLGS--GI--AHNTEELHRIAGAGIHYSptDEVLIEEGIEGwKEYELELMrdRNDNVVVVCPIENVDPVGV----- 242
Cdd:COG1181   141 R----EGSsvGVskVKNAEELAAALEEAFKYD--DKVLVEEFIDG-REVTVGVL--GNGGPRALPPIEIVPENGFydyea 211
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 651883668  243 --HTGDSITVAPVfTLTDREYQKLRDIGIAI-----IRGVG-VDtggcniqfAMHPATGRIIVIEMNP 302
Cdd:COG1181   212 kyTDGGTEYICPA-RLPEELEERIQELALKAfralgCRGYArVD--------FRLDEDGEPYLLEVNT 270
PRK05586 PRK05586
acetyl-CoA carboxylase biotin carboxylase subunit;
105-339 1.53e-09

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180150 [Multi-domain]  Cd Length: 447  Bit Score: 61.65  E-value: 1.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  105 AGVLKKYNVELIGASLEAIDRGEDRESFKEVVEAA------GAESARSDIAHTLEevdaIAERFGFPLVVRPSFTMGGLG 178
Cdd:PRK05586   92 AKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAgvpvvpGSEGEIENEEEALE----IAKEIGYPVMVKASAGGGGRG 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  179 SGIAHNTEELHRIAGAGIHYSPT----DEVLIEEGIEGWKEYELELMRDRNDNVVVVCpiENVDPVGVHTGDSITVAPVF 254
Cdd:PRK05586  168 IRIVRSEEELIKAFNTAKSEAKAafgdDSMYIEKFIENPKHIEFQILGDNYGNVVHLG--ERDCSLQRRNQKVLEEAPSP 245
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  255 TLTDREYQKLRDIGIAIIRGVGVDTGGcNIQFAMHpATGRIIVIEMNPRVSRSSALASKATGFPIAKIATKLALGYTLDE 334
Cdd:PRK05586  246 VMTEELRKKMGEIAVKAAKAVNYKNAG-TIEFLLD-KDGNFYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGEKLSI 323

                  ....*
gi 651883668  335 IQNDI 339
Cdd:PRK05586  324 KQEDI 328
PRK08591 PRK08591
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
699-883 1.57e-09

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 236307 [Multi-domain]  Cd Length: 451  Bit Score: 61.74  E-value: 1.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  699 SLEEALDAAHSIGYPVLVRPSYVLGGRGMEIVYDDAQLEKYVNRALNEAKA----DTVvsgrlpsplLIDKFLQDAIEID 774
Cdd:PRK08591  140 DEEEALAIAKEIGYPVIIKATAGGGGRGMRVVRTEAELEKAFSMARAEAKAafgnPGV---------YMEKYLENPRHIE 210
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  775 VDALFDGDelyiGGImehieeagVHSGDAACTL-----------PPSTLSDDQIRRLREATYAIAKGCGVCGLINVQYAF 843
Cdd:PRK08591  211 IQVLADGH----GNA--------IHLGERDCSLqrrhqkvleeaPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLY 278
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 651883668  844 MAN-TLYVIEANPRASRTVPFASKATGVALAKAAARIMAGE 883
Cdd:PRK08591  279 EKNgEFYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGE 319
MGS-like cd00532
MGS-like domain. This domain composes the whole protein of methylglyoxal synthetase, which ...
972-1095 1.98e-09

MGS-like domain. This domain composes the whole protein of methylglyoxal synthetase, which catalyzes the enolization of dihydroxyacetone phosphate (DHAP) to produce methylglyoxal. The family also includes the C-terminal domain in carbamoyl phosphate synthetase (CPS) where it catalyzes the last phosphorylation of a coaboxyphosphate intermediate to form the product carbamoyl phosphate and may also play a regulatory role. This family also includes inosine monophosphate cyclohydrolase. The known structures in this family show a common phosphate binding site.


Pssm-ID: 238297 [Multi-domain]  Cd Length: 112  Bit Score: 56.37  E-value: 1.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  972 VFISVNDTDKRQLPLFAVRLVELGFQIWATEGTASVLRRYGIESKIVDKITArvDSDPdapvqidkaegsvgkNVVELIE 1051
Cdd:cd00532     2 VFLSVSDHVKAMLVDLAPKLSSDGFPLFATGGTSRVLADAGIPVRAVSKRHE--DGEP---------------TVDAAIA 64
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 651883668 1052 E-GTIDLILNTPNSRGSRS---DGYSIRAAAIAADVPQFTTMTEFSAV 1095
Cdd:cd00532    65 EkGKFDVVINLRDPRRDRCtdeDGTALLRLARLYKIPVTTPNATAMFV 112
PRK08654 PRK08654
acetyl-CoA carboxylase biotin carboxylase subunit;
30-340 4.85e-09

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236325 [Multi-domain]  Cd Length: 499  Bit Score: 60.00  E-value: 4.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   30 GTQACRVLR---EEGIRVILVNSNPATIMTDPEMADATYiePIATPI-------LERIIA---KERPDALLPTLGgqtAL 96
Cdd:PRK08654   11 GEIAIRVMRacrELGIKTVAVYSEADKNALFVKYADEAY--PIGPAPpsksylnIERIIDvakKAGADAIHPGYG---FL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   97 NAAVALGEAgvLKKYNVELIGASLEAIDRGEDRESFKEVVEAAG------AESARSDIahtlEEVDAIAERFGFPLVVRP 170
Cdd:PRK08654   86 AENPEFAKA--CEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGvpvlpgTEEGIEDI----EEAKEIAEEIGYPVIIKA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  171 SFTMGGLGSGIAHNTEEL-------HRIAGAGIHYSptdEVLIEEGIEGWKEYELELMRDRNDNVvvvcpienvdpvgVH 243
Cdd:PRK08654  160 SAGGGGIGMRVVYSEEELedaiestQSIAQSAFGDS---TVFIEKYLEKPRHIEIQILADKHGNV-------------IH 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  244 TGDS-----------ITVAPVFTLTDREYQKLRDIGIAIIRGVGVDTGGcNIQFAMhpATGRIIVIEMNPRVSRSSALAS 312
Cdd:PRK08654  224 LGDRecsiqrrhqklIEEAPSPIMTPELRERMGEAAVKAAKAINYENAG-TVEFLY--SNGNFYFLEMNTRLQVEHPITE 300
                         330       340
                  ....*....|....*....|....*...
gi 651883668  313 KATGFPIAKIATKLALGYTLDEIQNDIT 340
Cdd:PRK08654  301 MVTGIDIVKEQIKIAAGEELSFKQEDIT 328
Dala_Dala_lig_C pfam07478
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ...
150-302 1.30e-07

D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).


Pssm-ID: 429483 [Multi-domain]  Cd Length: 204  Bit Score: 53.47  E-value: 1.30e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   150 HTLEEVDAIAERFGFPLVVRPSFTMGGLGSGIAHNTEELHRIAGAGIHYSPTdeVLIEEGIEGwKEYELELMrdRNDNVV 229
Cdd:pfam07478   23 NPKEWCAQVEEALGYPVFVKPARLGSSVGVSKVESREELQAAIEEAFQYDEK--VLVEEGIEG-REIECAVL--GNEDPE 97
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 651883668   230 VVCPIENVDPVGV---HTGDSITVAPVFT---LTDREYQKLRDIGIAIIRGVGVdTGGCNIQFaMHPATGRIIVIEMNP 302
Cdd:pfam07478   98 VSPVGEIVPSGGFydyEAKYIDDSAQIVVpadLEEEQEEQIQELALKAYKALGC-RGLARVDF-FLTEDGEIVLNEVNT 174
rimK_fam TIGR00768
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ...
620-873 1.81e-07

alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione synthetases, contains at least three different alpha-L-glutamate ligases. One is RimK, as in E. coli, which adds additional Glu residues to the native Glu-Glu C-terminus of ribosomal protein S6, but not to Lys-Glu mutants. Most species with a member of this subfamily lack an S6 homolog ending in Glu-Glu, however. Members in Methanococcus jannaschii act instead as a tetrahydromethanopterin:alpha-l-glutamate ligase (MJ0620) and a gamma-F420-2:alpha-l-glutamate ligase (MJ1001).


Pssm-ID: 273261 [Multi-domain]  Cd Length: 276  Bit Score: 53.89  E-value: 1.81e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   620 TFEDVIEIYEAEKKMGPIKGVIVQ-LGGQTPLSLAARLKAAGVPILgTTPESIDLAENRELFGEVLRAEKLNAPRFGTAL 698
Cdd:TIGR00768   32 PPAINLTFNEGPRALAELDVVIVRiVSMFRGLAVLRYLESLGVPVI-NSSDAILNAGDKFLSHQLLAKAGIPLPRTGLAG 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   699 SLEEALDAAHSIGYPVLVRPSYVLGGRGMEIVYDDAQLEKyVNRALNEAKADTVVsgrlpspLLIDKFLQDAIEIDVDAL 778
Cdd:TIGR00768  111 SPEEALKLIEEIGFPVVLKPVFGSWGRGVSLARDRQAAES-LLEHFEQLNGPQNL-------FLVQEYIKKPGGRDIRVF 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   779 FDGDELyIGGIMEHIEE---AGVHSGDAA--CTLppstlsDDQIRRLR-EATYAIakGCGVCGlinVQYAFMANTLYVIE 852
Cdd:TIGR00768  183 VVGDEV-VAAIYRITSGhwrSNLARGGKAepCSL------TEEIEELAiKAAKAL--GLDVAG---VDLLESEDGLLVNE 250
                          250       260
                   ....*....|....*....|...
gi 651883668   853 ANPrasrTVPF--ASKATGVALA 873
Cdd:TIGR00768  251 VNA----NPEFknSVKTTGVNIA 269
PRK08463 PRK08463
acetyl-CoA carboxylase subunit A; Validated
634-905 2.72e-07

acetyl-CoA carboxylase subunit A; Validated


Pssm-ID: 169452 [Multi-domain]  Cd Length: 478  Bit Score: 54.43  E-value: 2.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  634 MGPIKGVIVQLGGQTplslAAR--LKAAGVPILGTTpesidlaenrelfgevlraEKLNAPrfgtalSLEEALDAAHSIG 711
Cdd:PRK08463  102 IGPKSEVIRKMGNKN----IARylMKKNGIPIVPGT-------------------EKLNSE------SMEEIKIFARKIG 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  712 YPVLVRPSYVLGGRGMEIVYDDAQLEKYVNRALNEAKA----DTVvsgrlpsplLIDKFLQDAIEIDVDALFDGdelyIG 787
Cdd:PRK08463  153 YPVILKASGGGGGRGIRVVHKEEDLENAFESCKREALAyfnnDEV---------FMEKYVVNPRHIEFQILGDN----YG 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  788 GImehieeagVHSGDAACTL-----------PPSTLSDDQIRRLREATYAIAKGCGVCGLINVQYAF-MANTLYVIEANP 855
Cdd:PRK08463  220 NI--------IHLCERDCSIqrrhqkvieiaPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLdDYNRFYFMEMNT 291
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 651883668  856 RASRTVPFASKATGVALAKAAARIMAGETIAQQRANglLLPHGDGGDVRL 905
Cdd:PRK08463  292 RIQVEHGVTEEITGIDLIVRQIRIAAGEILDLEQSD--IKPRGFAIEARI 339
PRK08462 PRK08462
acetyl-CoA carboxylase biotin carboxylase subunit;
695-888 9.46e-07

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236269 [Multi-domain]  Cd Length: 445  Bit Score: 52.82  E-value: 9.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  695 GTALSLEEALDAAHSIGYPVLVRPSYVLGGRGMEIVYDDAQLEKYVNRALNEAkadtvVSGRLPSPLLIDKFLQDAIEID 774
Cdd:PRK08462  138 GALKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVEDESDLENLYLAAESEA-----LSAFGDGTMYMEKFINNPRHIE 212
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  775 VDALfdGDELyiGGImehieeagVHSGDAACTL----------PPSTLSDDQIR-RLREATYAIAKGCGVCGLINVQYAF 843
Cdd:PRK08462  213 VQIL--GDKH--GNV--------IHVGERDCSLqrrhqklieeSPAVVLDEKTReRLHETAIKAAKAIGYEGAGTFEFLL 280
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 651883668  844 MAN-TLYVIEANPRASRTVPFASKATGVALAKAAARIMAGETIAQQ 888
Cdd:PRK08462  281 DSNlDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEELPSQ 326
PRK02186 PRK02186
argininosuccinate lyase; Provisional
651-883 1.02e-06

argininosuccinate lyase; Provisional


Pssm-ID: 235010 [Multi-domain]  Cd Length: 887  Bit Score: 52.93  E-value: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  651 SLAARLkaaGVPilGTTPESIDLAENRELFGEVLRAEKLNAPRFGTALSLEEALDAAHSIGYPVLVRPSYVLGGRGMEIV 730
Cdd:PRK02186   87 EVARRL---GLP--AANTEAIRTCRDKKRLARTLRDHGIDVPRTHALALRAVALDALDGLTYPVVVKPRMGSGSVGVRLC 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  731 YDDAQLEKYVNRALNEAKADTVVSGRLPSPllidkflqdaiEIDVDALFDGDELYIGGIMEHIEEAGVHSGDAACTLPPS 810
Cdd:PRK02186  162 ASVAEAAAHCAALRRAGTRAALVQAYVEGD-----------EYSVETLTVARGHQVLGITRKHLGPPPHFVEIGHDFPAP 230
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 651883668  811 TLSDDQIRRLREATYAIAKGCGVCGLINVQYAFMANTLYVIEANPR-ASRTVPFA-SKATGVALAKAAARIMAGE 883
Cdd:PRK02186  231 LSAPQRERIVRTVLRALDAVGYAFGPAHTELRVRGDTVVIIEINPRlAGGMIPVLlEEAFGVDLLDHVIDLHLGV 305
PRK07178 PRK07178
acetyl-CoA carboxylase biotin carboxylase subunit;
632-883 1.02e-06

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180865 [Multi-domain]  Cd Length: 472  Bit Score: 52.80  E-value: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  632 KKMGPIKGVIVQLGGQTplslAAR--LKAAGVPIlgtTPESidlaenrelfgevlraeklnaprFGTALSLEEALDAAHS 709
Cdd:PRK07178  100 KFIGPSAEVIRRMGDKT----EARraMIKAGVPV---TPGS-----------------------EGNLADLDEALAEAER 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  710 IGYPVLVRPSYVLGGRGMEIVYDDAQLEKYVNRALNEAkadTVVSGRlpSPLLIDKFLQDAIEIDVDALFDgdelYIGGI 789
Cdd:PRK07178  150 IGYPVMLKATSGGGGRGIRRCNSREELEQNFPRVISEA---TKAFGS--AEVFLEKCIVNPKHIEVQILAD----SHGNV 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  790 mehieeagVHSGDAACTL-----------PPSTLSDDQIRRLREATYAIAKGCGVCGLINVQYAFMA-NTLYVIEANPRA 857
Cdd:PRK07178  221 --------VHLFERDCSIqrrnqklieiaPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLDAdGEVYFMEMNTRV 292
                         250       260
                  ....*....|....*....|....*.
gi 651883668  858 SRTVPFASKATGVALAKAAARIMAGE 883
Cdd:PRK07178  293 QVEHTITEEITGIDIVREQIRIASGL 318
PRK12833 PRK12833
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
1-339 1.38e-06

acetyl-CoA carboxylase biotin carboxylase subunit; Provisional


Pssm-ID: 183781 [Multi-domain]  Cd Length: 467  Bit Score: 52.06  E-value: 1.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668    1 MPKRndIKSVMVIGSGPIvigqaaefdysgtqACRVLR---EEGIRVILVNSN------PA-----TIMTDPEMADATYI 66
Cdd:PRK12833    1 MPSR--IRKVLVANRGEI--------------AVRIIRaarELGMRTVAACSDadrdslAArmadeAVHIGPSHAAKSYL 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   67 EPIAtpilerIIAKER---PDALLPTLGGqTALNAAVA--LGEAGVLkkynveLIGASLEAIDRGEDRESFKEVVEAAGA 141
Cdd:PRK12833   65 NPAA------ILAAARqcgADAIHPGYGF-LSENAAFAeaVEAAGLI------FVGPDAQTIRTMGDKARARRTARRAGV 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  142 ES--ARSDIAHTLEEVDAIAERFGFPLVVRPSFTMGGLGSGIAHNTEELHR---IAGAGIHYSPTD-EVLIEEGIEGWKE 215
Cdd:PRK12833  132 PTvpGSDGVVASLDAALEVAARIGYPLMIKAAAGGGGRGIRVAHDAAQLAAelpLAQREAQAAFGDgGVYLERFIARARH 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  216 YELELMRDRNDnvvVVCPIENVDPVGVHTGDSITVAPVFTLTDREYQKLRDIGIAIIRGVGVDTGGcNIQFAMHPATGRI 295
Cdd:PRK12833  212 IEVQILGDGER---VVHLFERECSLQRRRQKILEEAPSPSLTPAQRDALCASAVRLARQVGYRGAG-TLEYLFDDARGEF 287
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 651883668  296 IVIEMNPRVSRSSALASKATGFPIAKIATKLALGYTLDEIQNDI 339
Cdd:PRK12833  288 YFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEPLRFAQGDI 331
ddl PRK01372
D-alanine--D-alanine ligase; Reviewed
683-862 2.52e-06

D-alanine--D-alanine ligase; Reviewed


Pssm-ID: 234948 [Multi-domain]  Cd Length: 304  Bit Score: 50.49  E-value: 2.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  683 VLRAEKLNAPRFGTALSLEEALDAAHSIGYPVLVRPsyVLGGR--GMEIVYDDAQLEKYVNRAL---NEAKADTVVSGR- 756
Cdd:PRK01372  105 VWQAAGLPTPPWIVLTREEDLLAAIDKLGLPLVVKP--AREGSsvGVSKVKEEDELQAALELAFkydDEVLVEKYIKGRe 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  757 LPSPLLIDKFLqDAIEIDVDALF-DGDELYIGGIMEHIEEAGvhsgdaactLPPSTLsdDQIRRLREATYAIAkGCGVCG 835
Cdd:PRK01372  183 LTVAVLGGKAL-PVIEIVPAGEFyDYEAKYLAGGTQYICPAG---------LPAEIE--AELQELALKAYRAL-GCRGWG 249
                         170       180       190
                  ....*....|....*....|....*....|
gi 651883668  836 LINvqyaFM---ANTLYVIEANprasrTVP 862
Cdd:PRK01372  250 RVD----FMldeDGKPYLLEVN-----TQP 270
PRK07178 PRK07178
acetyl-CoA carboxylase biotin carboxylase subunit;
83-336 2.55e-06

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 180865 [Multi-domain]  Cd Length: 472  Bit Score: 51.26  E-value: 2.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   83 PDALLPTLGGQTALNAAVALG----------------EAGVLKKYNVELIGASLEAIDRGEDRESFKEVVEAA------G 140
Cdd:PRK07178   53 ADPLAGYLNPRRLVNLAVETGcdalhpgygflsenaeLAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAgvpvtpG 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  141 AESARSDIAHTLEEvdaiAERFGFPLVVRPsfTMGGLGSGI--AHNTEELHR-----IAGAGIHYSPTdEVLIEEGIEGW 213
Cdd:PRK07178  133 SEGNLADLDEALAE----AERIGYPVMLKA--TSGGGGRGIrrCNSREELEQnfprvISEATKAFGSA-EVFLEKCIVNP 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  214 KEYELELMRDRNDNVVVV----CPIENvdpvgvHTGDSITVAPVFTLTDREYQKLRDIGIAIIRGVGVDTGGcNIQFAMh 289
Cdd:PRK07178  206 KHIEVQILADSHGNVVHLferdCSIQR------RNQKLIEIAPSPQLTPEQRAYIGDLAVRAAKAVGYENAG-TVEFLL- 277
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 651883668  290 PATGRIIVIEMNPRVSRSSALASKATGFPIAK----IATKLALGYTLDEIQ 336
Cdd:PRK07178  278 DADGEVYFMEMNTRVQVEHTITEEITGIDIVReqirIASGLPLSYKQEDIQ 328
PRK08463 PRK08463
acetyl-CoA carboxylase subunit A; Validated
18-339 4.48e-06

acetyl-CoA carboxylase subunit A; Validated


Pssm-ID: 169452 [Multi-domain]  Cd Length: 478  Bit Score: 50.58  E-value: 4.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   18 IVIGQAAEFDYSGTQACRVLReegIRVILVNSNPATIMTDPEMADATY---IEPI-----ATPILEriIAKE-RPDALLP 88
Cdd:PRK08463    5 ILIANRGEIAVRVIRACRDLH---IKSVAIYTEPDRECLHVKIADEAYrigTDPIkgyldVKRIVE--IAKAcGADAIHP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   89 TLGGQTAlNA--AVALGEAGVLkkynveLIGASLEAIDRGEDRESFKEVVE------AAGAESARSdiaHTLEEVDAIAE 160
Cdd:PRK08463   80 GYGFLSE-NYefAKAVEDAGII------FIGPKSEVIRKMGNKNIARYLMKkngipiVPGTEKLNS---ESMEEIKIFAR 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  161 RFGFPLVVRPSFTMGGLGSGIAHNTEELHRIAGA----GIHYSPTDEVLIEEGIEGWKEYELELMRDRNDNVVVVCpiEN 236
Cdd:PRK08463  150 KIGYPVILKASGGGGGRGIRVVHKEEDLENAFESckreALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLC--ER 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  237 VDPVGVHTGDSITVAPVFTLTDREYQKLRDIGIAIIRGVGVDTGGcNIQFAMHPaTGRIIVIEMNPRVSRSSALASKATG 316
Cdd:PRK08463  228 DCSIQRRHQKVIEIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAG-TIEFLLDD-YNRFYFMEMNTRIQVEHGVTEEITG 305
                         330       340
                  ....*....|....*....|...
gi 651883668  317 FPIAKIATKLALGYTLDEIQNDI 339
Cdd:PRK08463  306 IDLIVRQIRIAAGEILDLEQSDI 328
PRK06111 PRK06111
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
109-339 4.86e-06

acetyl-CoA carboxylase biotin carboxylase subunit; Validated


Pssm-ID: 180406 [Multi-domain]  Cd Length: 450  Bit Score: 50.41  E-value: 4.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  109 KKYNVELIGASLEAIDRGEDRESFKEVVEAA------GAESARSDIahtlEEVDAIAERFGFPLVVRPSFTMGGLGSGIA 182
Cdd:PRK06111   96 KEEGIVFIGPSADIIAKMGSKIEARRAMQAAgvpvvpGITTNLEDA----EEAIAIARQIGYPVMLKASAGGGGIGMQLV 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  183 HNTEELhRIAGAGIHYSPTD-----EVLIEEGIEGWKEYELELMRDRNDNVVVV----CPIENvdpvgvHTGDSITVAPV 253
Cdd:PRK06111  172 ETEQEL-TKAFESNKKRAANffgngEMYIEKYIEDPRHIEIQLLADTHGNTVYLwereCSVQR------RHQKVIEEAPS 244
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  254 FTLTDREYQKLRDIGIAIIRGVGVdTGGCNIQFAMHPAtGRIIVIEMNPRVSRSSALASKATGFPIAKIATKLALGYTLD 333
Cdd:PRK06111  245 PFLDEETRKAMGERAVQAAKAIGY-TNAGTIEFLVDEQ-KNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGEKLS 322

                  ....*.
gi 651883668  334 EIQNDI 339
Cdd:PRK06111  323 FTQDDI 328
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
35-321 2.34e-05

Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 439959 [Multi-domain]  Cd Length: 289  Bit Score: 47.63  E-value: 2.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   35 RVLREEGIRVILVNsnpatimtdpemADATYIEPIATPILERIIAKERPDALLP-TLGGQTALNAAVALGEAGVLkkynv 113
Cdd:COG0189    21 EAAQRRGHEVEVID------------PDDLTLDLGRAPELYRGEDLSEFDAVLPrIDPPFYGLALLRQLEAAGVP----- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  114 eLIGaSLEAIDRGEDRESFKEVVEAAGAESARSDIAHTLEEVDAIAERFGFPLVVRPSFTMGGLGSGIAHNTEELHRIAg 193
Cdd:COG0189    84 -VVN-DPEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEELGGPVVLKPLDGSGGRGVFLVEDEDALESIL- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  194 AGIHYSPTDEVLIEEGIEGWKEYELelmrdR----NDNVVVVC---PIENVDPVGVHTGDSITVAPvftLTDREyqklRD 266
Cdd:COG0189   161 EALTELGSEPVLVQEFIPEEDGRDI-----RvlvvGGEPVAAIrriPAEGEFRTNLARGGRAEPVE---LTDEE----RE 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 651883668  267 IGIAIIRGVGVDTGGcnIQFAMHPatGRIIVIEMNPrvsrSSALA--SKATGFPIAK 321
Cdd:COG0189   229 LALRAAPALGLDFAG--VDLIEDD--DGPLVLEVNV----TPGFRglERATGVDIAE 277
ATP-grasp pfam02222
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ...
137-304 7.78e-05

ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.


Pssm-ID: 396689 [Multi-domain]  Cd Length: 169  Bit Score: 44.55  E-value: 7.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   137 EAAGAESARSDIAHTLEEVDAIAERFGFPLVVRPSfTMG--GLGSGIAHNTEELH---RIAGAGihysptdEVLIEEGIE 211
Cdd:pfam02222    1 QKLGLPTPRFMAAESLEELIEAGQELGYPCVVKAR-RGGydGKGQYVVRSEADLPqawEELGDG-------PVIVEEFVP 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   212 gwKEYELELM--RDRNDNVVVVCPIENVDpvgvHTGDSITVAPVFTLTDREYQKLRDIGIAIIR---GVGVdtggcniqF 286
Cdd:pfam02222   73 --FDRELSVLvvRSVDGETAFYPVVETIQ----EDGICRLSVAPARVPQAIQAEAQDIAKRLVDelgGVGV--------F 138
                          170       180
                   ....*....|....*....|.
gi 651883668   287 AMH---PATGRIIVIEMNPRV 304
Cdd:pfam02222  139 GVElfvTEDGDLLINELAPRP 159
PRK08462 PRK08462
acetyl-CoA carboxylase biotin carboxylase subunit;
107-349 8.44e-05

acetyl-CoA carboxylase biotin carboxylase subunit;


Pssm-ID: 236269 [Multi-domain]  Cd Length: 445  Bit Score: 46.28  E-value: 8.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  107 VLKKYNVELIGASLEAIDRGEDRESFKEVVEAAGAESAR-SDIA-HTLEEVDAIAERFGFPLVVRPSFTMGGLGSGIAHN 184
Cdd:PRK08462   96 ICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPgSDGAlKSYEEAKKIAKEIGYPVILKAAAGGGGRGMRVVED 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  185 TEELHRiagagIHYSPTDEVL---------IEEGIEGWKEYELELMRDRNDNVVVV----CPIENvdpvgvHTGDSITVA 251
Cdd:PRK08462  176 ESDLEN-----LYLAAESEALsafgdgtmyMEKFINNPRHIEVQILGDKHGNVIHVgerdCSLQR------RHQKLIEES 244
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  252 PVFTLTDREYQKLRDIGIAIIRGVGVDTGGcNIQFaMHPATGRIIVIEMNPRVSRSSALASKATGFPIAKIATKLALGYT 331
Cdd:PRK08462  245 PAVVLDEKTRERLHETAIKAAKAIGYEGAG-TFEF-LLDSNLDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEE 322
                         250       260
                  ....*....|....*....|....*...
gi 651883668  332 LDE----------IQNDITKSTPASFEP 349
Cdd:PRK08462  323 LPSqesiklkghaIECRITAEDPKKFYP 350
ATPgrasp_Ter pfam15632
ATP-grasp in the biosynthetic pathway with Ter operon; This ATP-grasp family is related to ...
810-883 7.04e-04

ATP-grasp in the biosynthetic pathway with Ter operon; This ATP-grasp family is related to carbamoyl phosphate synthetase. These genes are found in the biosynthetic operon associated with the Ter stress response operon and are predicted to be involved in the biosynthesis of a ribo-nucleoside involved in stress response.


Pssm-ID: 434824 [Multi-domain]  Cd Length: 131  Bit Score: 40.67  E-value: 7.04e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 651883668   810 STLSDDQirRLREATYAIAKGCGVCGLINVQYAFMANTLYVIEANPRASRTVPfASKATGVALAKAAARIMAGE 883
Cdd:pfam15632   41 QTLEDDP--ELIEAARRLAEAFGLDGLFNVQFRYDGDGPKLLEINPRMSGGIG-YSCLAGVNLPYLALKLLLGL 111
purT PRK09288
formate-dependent phosphoribosylglycinamide formyltransferase;
673-750 1.08e-03

formate-dependent phosphoribosylglycinamide formyltransferase;


Pssm-ID: 236454 [Multi-domain]  Cd Length: 395  Bit Score: 42.82  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668  673 LAENRELfgevLR---AEKLNAP--RFGTALSLEEALDAAHSIGYPVLVRPsyVLG--GRGMEIVYDDAQLEKYVNRALN 745
Cdd:PRK09288  110 LTMNREG----IRrlaAEELGLPtsPYRFADSLEELRAAVEEIGYPCVVKP--VMSssGKGQSVVRSPEDIEKAWEYAQE 183

                  ....*
gi 651883668  746 EAKAD 750
Cdd:PRK09288  184 GGRGG 188
ATP-grasp_2 pfam08442
ATP-grasp domain;
133-264 1.14e-03

ATP-grasp domain;


Pssm-ID: 400651 [Multi-domain]  Cd Length: 202  Bit Score: 41.48  E-value: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   133 KEVVEAAGAESARSDIAHTLEEVDAIAERFG-FPLVVRPSFTMGGLGSG----IAHNTEELHRIAGA-----------GI 196
Cdd:pfam08442    8 KEIFAKYGIPVPRGEVATSPEEAEEIAKKLGgKVYVVKAQVLAGGRGKAggvkLAKSPEEAKEVAKEmlgknlvtkqtGP 87
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 651883668   197 HYSPTDEVLIEEGIEGWKEYELELMRDRNDN-VVVVCPIE---NVDPVGVHTGDSI---TVAPVFTLTDREYQKL 264
Cdd:pfam08442   88 DGQPVNKVLVEEALDIKKEYYLSIVLDRASKgPVIIASTEggvDIEEVAAKNPEKIhkfPIDPLKGLTPYQAREI 162
PurH COG0138
AICAR transformylase/IMP cyclohydrolase PurH [Nucleotide transport and metabolism]; AICAR ...
974-1022 3.30e-03

AICAR transformylase/IMP cyclohydrolase PurH [Nucleotide transport and metabolism]; AICAR transformylase/IMP cyclohydrolase PurH is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 439908  Cd Length: 512  Bit Score: 41.55  E-value: 3.30e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 651883668  974 ISVndTDKRQLPLFAVRLVELGFQIWATEGTASVLRRYGIESKIVDKIT 1022
Cdd:COG0138     8 ISV--SDKTGLVEFARALVELGVEIISTGGTAKALREAGIPVTEVSEVT 54
PRK14016 PRK14016
cyanophycin synthetase; Provisional
672-738 5.48e-03

cyanophycin synthetase; Provisional


Pssm-ID: 237586 [Multi-domain]  Cd Length: 727  Bit Score: 40.91  E-value: 5.48e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 651883668  672 DLAENRELFGEVLRAEKLNAPRFGTALSLEEALDAAHSIGYPVLVRPSYVLGGRGMEI-VYDDAQLEK 738
Cdd:PRK14016  210 DIACDKELTKRLLAAAGVPVPEGRVVTSAEDAWEAAEEIGYPVVVKPLDGNHGRGVTVnITTREEIEA 277
ddl PRK01966
D-alanine--D-alanine ligase;
84-218 6.14e-03

D-alanine--D-alanine ligase;


Pssm-ID: 234993 [Multi-domain]  Cd Length: 333  Bit Score: 40.10  E-value: 6.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 651883668   84 DALLPTLGGqtalnaavALGE----AGVLKKYNVELIGASLEAIDRGEDRESFKEVVEAAGAESA------RSDIAHTLe 153
Cdd:PRK01966   83 DVVFPVLHG--------PPGEdgtiQGLLELLGIPYVGCGVLASALSMDKILTKRLLAAAGIPVApyvvltRGDWEEAS- 153
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 651883668  154 eVDAIAERFGFPLVVRPSftmgGLGS--GI--AHNTEELHriagAGIH----YSPtdEVLIEEGIEGwKEYEL 218
Cdd:PRK01966  154 -LAEIEAKLGLPVFVKPA----NLGSsvGIskVKNEEELA----AALDlafeYDR--KVLVEQGIKG-REIEC 214
PLN02891 PLN02891
IMP cyclohydrolase
951-1022 9.60e-03

IMP cyclohydrolase


Pssm-ID: 178479 [Multi-domain]  Cd Length: 547  Bit Score: 39.77  E-value: 9.60e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 651883668  951 PHAFAKSQLSAYEGGLPtsgNVFISVndTDKRQLPLFAVRLVELGFQIWATEGTASVLRRYGIESKIVDKIT 1022
Cdd:PLN02891    7 AARAPAQPQSSPSSGKK---QALISL--SDKTDLALLANGLQELGYTIVSTGGTASALEAAGVSVTKVEELT 73
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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