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Conserved domains on  [gi|764123366|ref|WP_044309727|]
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MULTISPECIES: cobyrinate a,c-diamide synthase [Pseudomonas]

Protein Classification

hydrogenobyrinic/cobyrinic acid a,c-diamide synthase( domain architecture ID 11479400)

hydrogenobyrinic/cobyrinic acid a,c-diamide synthase catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of hydrogenobyrinate or cobyrinate, using either L-glutamine or ammonia as the nitrogen source

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK01077 PRK01077
cobyrinate a,c-diamide synthase;
5-431 0e+00

cobyrinate a,c-diamide synthase;


:

Pssm-ID: 234896 [Multi-domain]  Cd Length: 451  Bit Score: 595.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366   5 RDCPAVLIAAPASGQGKTTVTAALARLHRNQGRKVRVFKCGPDFLDPMILERASGAPVYQLDMWMVGADESRRLLWEAAD 84
Cdd:PRK01077   1 MRMPALVIAAPASGSGKTTVTLGLMRALRRRGLRVQPFKVGPDYIDPAYHTAATGRPSRNLDSWMMGEELVRALFARAAQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366  85 EADLILIEGVMGLFDGTP------SSADLSRHFGVPVLGVIDGTAMAQTFGALALGLARYQPDLPFAGVLANRVGTVRHA 158
Cdd:PRK01077  81 GADIAVIEGVMGLFDGAGsdpdegSTADIAKLLGAPVVLVVDASGMAQSAAALVLGFATFDPDVRIAGVILNRVGSERHY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366 159 QLLENSLTE-GLRWYGALSREVGFELPSRHLGLVQASELNDLDVRLDMAAAALASTCEVALPPAVTFTAPDPVHV----E 233
Cdd:PRK01077 161 QLLREALERcGIPVLGALPRDAALALPERHLGLVQASEHGDLEARLDALADLVEEHVDLDALLALARAAPPPPPAaappP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366 234 PLLRGVRIAIARDEAFAFLYGASLELLRNMGAELSFFSPIHDRELPEADSLYLPGGYPELHHVALAANGTMQASIRAHHI 313
Cdd:PRK01077 241 PAPPGVRIAVARDAAFNFYYPENLELLRAAGAELVFFSPLADEALPDCDGLYLGGGYPELFAAELAANTSMRASIRAAAA 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366 314 AGKPILAECGGMLYLLEALTDVEGVRAELVGLLSGEAVMQKRLAALALQAVELPEGTL--------HGHTYHHS-LTSTE 384
Cdd:PRK01077 321 AGKPIYAECGGLMYLGESLEDADGERHPMVGLLPGEASMTKRLQALGYREAEALEDTLlgkagerlRGHEFHYStLETPE 400
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 764123366 385 LQPIARGVSPNGGRGAEAVYRLGRLTASYVHFYFPSCPRAIAALFKP 431
Cdd:PRK01077 401 EAPLYRVRDADGRPLGEEGYRRGNVLASYLHLHFASNPDAAARFLAA 447
 
Name Accession Description Interval E-value
PRK01077 PRK01077
cobyrinate a,c-diamide synthase;
5-431 0e+00

cobyrinate a,c-diamide synthase;


Pssm-ID: 234896 [Multi-domain]  Cd Length: 451  Bit Score: 595.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366   5 RDCPAVLIAAPASGQGKTTVTAALARLHRNQGRKVRVFKCGPDFLDPMILERASGAPVYQLDMWMVGADESRRLLWEAAD 84
Cdd:PRK01077   1 MRMPALVIAAPASGSGKTTVTLGLMRALRRRGLRVQPFKVGPDYIDPAYHTAATGRPSRNLDSWMMGEELVRALFARAAQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366  85 EADLILIEGVMGLFDGTP------SSADLSRHFGVPVLGVIDGTAMAQTFGALALGLARYQPDLPFAGVLANRVGTVRHA 158
Cdd:PRK01077  81 GADIAVIEGVMGLFDGAGsdpdegSTADIAKLLGAPVVLVVDASGMAQSAAALVLGFATFDPDVRIAGVILNRVGSERHY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366 159 QLLENSLTE-GLRWYGALSREVGFELPSRHLGLVQASELNDLDVRLDMAAAALASTCEVALPPAVTFTAPDPVHV----E 233
Cdd:PRK01077 161 QLLREALERcGIPVLGALPRDAALALPERHLGLVQASEHGDLEARLDALADLVEEHVDLDALLALARAAPPPPPAaappP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366 234 PLLRGVRIAIARDEAFAFLYGASLELLRNMGAELSFFSPIHDRELPEADSLYLPGGYPELHHVALAANGTMQASIRAHHI 313
Cdd:PRK01077 241 PAPPGVRIAVARDAAFNFYYPENLELLRAAGAELVFFSPLADEALPDCDGLYLGGGYPELFAAELAANTSMRASIRAAAA 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366 314 AGKPILAECGGMLYLLEALTDVEGVRAELVGLLSGEAVMQKRLAALALQAVELPEGTL--------HGHTYHHS-LTSTE 384
Cdd:PRK01077 321 AGKPIYAECGGLMYLGESLEDADGERHPMVGLLPGEASMTKRLQALGYREAEALEDTLlgkagerlRGHEFHYStLETPE 400
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 764123366 385 LQPIARGVSPNGGRGAEAVYRLGRLTASYVHFYFPSCPRAIAALFKP 431
Cdd:PRK01077 401 EAPLYRVRDADGRPLGEEGYRRGNVLASYLHLHFASNPDAAARFLAA 447
CobB COG1797
Cobyrinic acid a,c-diamide synthase [Coenzyme transport and metabolism]; Cobyrinic acid a, ...
7-430 5.53e-159

Cobyrinic acid a,c-diamide synthase [Coenzyme transport and metabolism]; Cobyrinic acid a,c-diamide synthase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441402 [Multi-domain]  Cd Length: 459  Bit Score: 456.49  E-value: 5.53e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366   7 CPAVLIAAPASGQGKTTVTAALARLHRNQGRKVRVFKCGPDFLDPMILERASGAPVYQLDMWMVGADESRRLLWEAADEA 86
Cdd:COG1797    3 IPRLVIAAPHSGSGKTTVTLGLLAALRRRGLKVQPFKVGPDYIDPGYHTLATGRPSRNLDPFLMGEEGVRELFARGSAGA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366  87 DLILIEGVMGLFDG------TPSSADLSRHFGVPVLGVIDGTAMAQTFGALALGLARYQPDLPFAGVLANRVGTVRHAQL 160
Cdd:COG1797   83 DIAVIEGVMGLYDGldgdsgSGSTAHLAKLLGAPVVLVVDASGMSRSAAALVLGFRAFDPDVRIAGVILNRVGSERHEEL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366 161 LENSLTE--GLRWYGALSREVGFELPSRHLGLVQASELNDLDVRLDMAAAALASTC------EVALPPAVTFTAPDPVHV 232
Cdd:COG1797  163 LREAIEHytGIPVLGALPRDEELELPSRHLGLVPAAEREELEEALDRLAELVEEHVdldallELARSAPPLPAPPSPLFA 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366 233 EPLLRGVRIAIARDEAFAFLYGASLELLRNMGAELSFFSPIHDRELPE-ADSLYLPGGYPELHHVALAANGTMQASIRAH 311
Cdd:COG1797  243 PPPGPRVRIAVARDEAFNFYYPENLELLEAAGAELVFFSPLRDEALPEdVDGLYLGGGFPELFAEELSANRSMRESIREA 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366 312 HIAGKPILAECGGMLYLLEALTDVEGVRAELVGLLSGEAVMQKRLAAL------ALQA-VELPEGT-LHGHTYHHS-LTS 382
Cdd:COG1797  323 AEAGMPIYAECGGLMYLCRSITDFEGKGYPMVGVLPGDAVMTKRLQGLgyreatALGDsPLGPAGErIRGHEFHYStLTP 402
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 764123366 383 T-ELQPIARGVSPNGGRGAEAVYRLGRLTASYVHFYFPSCPRAIAALFK 430
Cdd:COG1797  403 EgDLRPAYRLRRGRGIDGGRDGFVYGNVLASYLHLHFASNPEWAERFVA 451
cobB TIGR00379
cobyrinic acid a,c-diamide synthase; This model describes cobyrinic acid a,c-diamide synthase, ...
10-430 1.11e-86

cobyrinic acid a,c-diamide synthase; This model describes cobyrinic acid a,c-diamide synthase, the cobB (cbiA in Salmonella) protein of cobalamin biosynthesis. It is responsible for the amidation of carboxylic groups at positions A and C of either cobyrinic acid or hydrogenobrynic acid. NH(2) groups are provided by glutamine and one molecule of ATP hydrogenolyzed for each amidation. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 273044 [Multi-domain]  Cd Length: 449  Bit Score: 271.29  E-value: 1.11e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366   10 VLIAAPASGQGKTTVTAALARLHRNQGRKVRVFKCGPDFLDPMILERASGAPVYQLDMWMVGADESRRLLWEAADEADLI 89
Cdd:TIGR00379   2 VVIAGTSSGVGKTTISTGIMKALSRRKLRVQPFKVGPDYIDPMFHTQATGRPSRNLDSFFMSEAQIQECFHRHSKGTDYS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366   90 LIEGVMGLFDG------TPSSADLSRHFGVPVLGVIDGTAMAQTFGALALGLARYQPDLPFAGVLANRVGTVRHAQLLEN 163
Cdd:TIGR00379  82 IIEGVRGLYDGisaitdYGSTASVAKALDAPIVLVMNCQRLSRSAAAIVLGYRSFDPGVKLKGVILNRVGSERHLEKLKI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366  164 SLTE--GLRWYGALSREVGFELPSRHLGLVQASELNDLDVRLDMAAAALASTCEV-ALPPAVTFTAPDPVHVEPLL---- 236
Cdd:TIGR00379 162 AVEPlrGIPILGVIPRQQDLKVPDRHLGLVPAGEREIIQQIFDWLAEVVEKYLDLdKLLEIAETARNLPSPMSLLWepqn 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366  237 -RGVRIAIARDEAFAFLYGASLELLRNMGAELSFFSPIHDRELPEADSLYLPGGYPELHHVALAANGTMQASIRAHHIAG 315
Cdd:TIGR00379 242 sKYVRIAVAQDQAFNFYYQDNLDALTHNAAELVPFSPLEDTELPDVDAVYIGGGFPELFAEELSQNQALRDSIKTFIHQG 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366  316 KPILAECGGMLYLLEALTDVEGvRAELVGLLSGEAVMQKRLAALALQAVELPEG--------TLHGHTYHHS-LTSTELQ 386
Cdd:TIGR00379 322 LPIYGECGGLMYLSQSLDNFEG-QIFMVGMLPTAATMTGRVQGLGYVQAEVVNDclilwqgeKFRGHEFHYSrMTKLPNA 400
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 764123366  387 PIARGVSpnggRGAEAVYRL-----GRLTASYVHFYFPSCPRAIAALFK 430
Cdd:TIGR00379 401 QFAYRVE----RGRGIIDQLdgicvGSVLASYLHLHAGSVPKFAAAFVA 445
CobB_N cd05388
N-terminal domain of cobyrinic acid a,c-diamide synthase; Cobyrinic acid a,c-diamide synthase ...
8-192 6.81e-78

N-terminal domain of cobyrinic acid a,c-diamide synthase; Cobyrinic acid a,c-diamide synthase (CobB, CbiA). Biosynthesis of cobalamin (vitamin B12) requires more than two dozen different enzymes. CobB catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinic acid, via the formation of a phosphorylated intermediate, using glutamine or ammonia as the nitrogen source. CobB is comprised of two protein domains: the C-terminal glutaminase domain and the N-terminal ATP-binding domain. The glutaminase domain catalyzes the hydrolysis of glutamine to glutamate and ammonia. It belongs to the triad class of glutamine amidotransferases. This classification is based on the N-terminal domain which catalyzes the ultimate synthesis of the diamide product by using energy from the hydrolysis of ATP and ammonia transferred from the C-terminal domain.


Pssm-ID: 349773 [Multi-domain]  Cd Length: 193  Bit Score: 239.81  E-value: 6.81e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366   8 PAVLIAAPASGQGKTTVTAALARLHRNQGRKVRVFKCGPDFLDPMILERASGAPVYQLDMWMVGADESRRLLWEAADEAD 87
Cdd:cd05388    1 PRIVIAGTSSGSGKTTITLGLMRALARRGLRVQPFKVGPDYIDPGFHEAATGRPSRNLDSWMMGEDGVRELFARAAGGAD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366  88 LILIEGVMGLFDG------TPSSADLSRHFGVPVLGVIDGTAMAQTFGALALGLARYQPDLPFAGVLANRVGTVRHAQLL 161
Cdd:cd05388   81 VAIIEGVMGLYDGrdtdsdEGSTAELARLLGAPVLLVLDCKGMARSAAAIVKGYKEFDPDLNLAGVILNRVGSPRHAELL 160
                        170       180       190
                 ....*....|....*....|....*....|...
gi 764123366 162 ENSLTE--GLRWYGALSREVGFELPSRHLGLVQ 192
Cdd:cd05388  161 KEAIEEytGIPVLGYLPRDDELTLPERHLGLVP 193
F430_CfbB NF033195
Ni-sirohydrochlorin a,c-diamide synthase; Members of this family are Ni-sirohydrochlorin a, ...
9-422 6.24e-77

Ni-sirohydrochlorin a,c-diamide synthase; Members of this family are Ni-sirohydrochlorin a,c-diamide synthase, involving in synthesizing coenzyme F430, used in methanogens by coenzyme M reductase. Members of this family are restricted to archaeal methanogens, and resemble (and may be misannotated as) the enzyme cobyrinic acid a,c-diamide synthase, involved in cobalamin biosynthesis.


Pssm-ID: 467990 [Multi-domain]  Cd Length: 451  Bit Score: 246.33  E-value: 6.24e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366   9 AVLIAAPASGQGKTTVTAALARLhRNQGRKVRVFKCGPDFLDPMILERASGAPVYQLDMWMVGADESRRLLWEAADEADL 88
Cdd:NF033195   1 RVLIAGDRSGSGKTTITTGIMAA-LSKGYNVQPFKVGPDYIDPSYHTGATGRPSRNLDSFFMSEEQIREVFAHGCKGADI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366  89 ILIEGVMGLFDG------TPSSADLSRHFGVPVLGVIDGTAMAQTFGALALGLARYQPDLPFAGVLANRVGTVRHAqlle 162
Cdd:NF033195  80 AIIEGVRGLYEGieslgdVGSTASIAKALNAPVILVINARSITRSAAAIVKGFKAFDPDVNIAGVILNNVGGERHA---- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366 163 NSLTEGLRWY------GALSREVGFELPSRHLGLVQASE---LNDLDVRLDMAAAALASTCEVALPPAVTFTAPD-PVHV 232
Cdd:NF033195 156 KKAKEAIEHYtgvpviGAIPRDEEMKLSMRHLGLVPAVEgreRGEFLERIEKIGEIIEENLDLDALLEIAKEAFPlPEPE 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366 233 EPLL------RGVRIAIARDEAFAFLYGASLELLRNMGAELSFFSPIHDRELPEADSLYLPGGYPELHHVALAANGTMQA 306
Cdd:NF033195 236 EDLFlweenkNDVKIGVALDEAFNFYYADNFDALEANGAEIVYFSPLHDEELPDVDGLYIGGGYPELFAAELEANKSMRE 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366 307 SIRAHHIAGKPILAECGGMLYLLEALT---DVEGVRAELVGLLSGEAVMQKRlaalalQAVELPEGTL------------ 371
Cdd:NF033195 316 SIREFSGDGTPIYAECGGLMYLTESIDlqgKGEESSYEMVGVFPGHTVMKAV------RVLSYVIGEFskdcpigkkget 389
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 764123366 372 -HGHTYHHS----LTSTELQ-PIARGVSPNGGR-GAEAvyrlGRLTASYVHFYFPSCP 422
Cdd:NF033195 390 fRGHEFHYSkvtlDPETKFAyKLSRGTGIIDGLdGLVV----NNTLGSYTHLHAVSYP 443
GATase_3 pfam07685
CobB/CobQ-like glutamine amidotransferase domain;
240-418 1.97e-37

CobB/CobQ-like glutamine amidotransferase domain;


Pssm-ID: 429595 [Multi-domain]  Cd Length: 189  Bit Score: 134.68  E-value: 1.97e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366  240 RIAIARDEAFAFLYGASLELLRNMGAELSFFSPIHDRELPE-ADSLYLPGGYPELHHVALAANGTMQASIRAHHIAGKPI 318
Cdd:pfam07685   1 RIAVIRLPRISNYTDDNLDPLRYEPAVRVRFVPLPDESLGPdADLIILPGGKPTIQDLALLRNSGMDEAIKEAAEDGGPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366  319 LAECGGMLYLLEALTDVEGVRAELVGLLSGEAVMQKRLAALALQAVELPEG-TLHGHTYHHSLTSTE--LQP---IARGV 392
Cdd:pfam07685  81 LGICGGYQMLGETIEDPEGVRIEGLGLLDIETVFQKEKLTGQVVGYLLLEGeTVRGYEIHYGRTILGdgAKPlgrVKVGG 160
                         170       180
                  ....*....|....*....|....*..
gi 764123366  393 SPNGGRGAE-AVYrlGRLTASYVHFYF 418
Cdd:pfam07685 161 GNNGEDGKDgAVS--GNVFGTYLHGHF 185
 
Name Accession Description Interval E-value
PRK01077 PRK01077
cobyrinate a,c-diamide synthase;
5-431 0e+00

cobyrinate a,c-diamide synthase;


Pssm-ID: 234896 [Multi-domain]  Cd Length: 451  Bit Score: 595.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366   5 RDCPAVLIAAPASGQGKTTVTAALARLHRNQGRKVRVFKCGPDFLDPMILERASGAPVYQLDMWMVGADESRRLLWEAAD 84
Cdd:PRK01077   1 MRMPALVIAAPASGSGKTTVTLGLMRALRRRGLRVQPFKVGPDYIDPAYHTAATGRPSRNLDSWMMGEELVRALFARAAQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366  85 EADLILIEGVMGLFDGTP------SSADLSRHFGVPVLGVIDGTAMAQTFGALALGLARYQPDLPFAGVLANRVGTVRHA 158
Cdd:PRK01077  81 GADIAVIEGVMGLFDGAGsdpdegSTADIAKLLGAPVVLVVDASGMAQSAAALVLGFATFDPDVRIAGVILNRVGSERHY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366 159 QLLENSLTE-GLRWYGALSREVGFELPSRHLGLVQASELNDLDVRLDMAAAALASTCEVALPPAVTFTAPDPVHV----E 233
Cdd:PRK01077 161 QLLREALERcGIPVLGALPRDAALALPERHLGLVQASEHGDLEARLDALADLVEEHVDLDALLALARAAPPPPPAaappP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366 234 PLLRGVRIAIARDEAFAFLYGASLELLRNMGAELSFFSPIHDRELPEADSLYLPGGYPELHHVALAANGTMQASIRAHHI 313
Cdd:PRK01077 241 PAPPGVRIAVARDAAFNFYYPENLELLRAAGAELVFFSPLADEALPDCDGLYLGGGYPELFAAELAANTSMRASIRAAAA 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366 314 AGKPILAECGGMLYLLEALTDVEGVRAELVGLLSGEAVMQKRLAALALQAVELPEGTL--------HGHTYHHS-LTSTE 384
Cdd:PRK01077 321 AGKPIYAECGGLMYLGESLEDADGERHPMVGLLPGEASMTKRLQALGYREAEALEDTLlgkagerlRGHEFHYStLETPE 400
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 764123366 385 LQPIARGVSPNGGRGAEAVYRLGRLTASYVHFYFPSCPRAIAALFKP 431
Cdd:PRK01077 401 EAPLYRVRDADGRPLGEEGYRRGNVLASYLHLHFASNPDAAARFLAA 447
CobB COG1797
Cobyrinic acid a,c-diamide synthase [Coenzyme transport and metabolism]; Cobyrinic acid a, ...
7-430 5.53e-159

Cobyrinic acid a,c-diamide synthase [Coenzyme transport and metabolism]; Cobyrinic acid a,c-diamide synthase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441402 [Multi-domain]  Cd Length: 459  Bit Score: 456.49  E-value: 5.53e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366   7 CPAVLIAAPASGQGKTTVTAALARLHRNQGRKVRVFKCGPDFLDPMILERASGAPVYQLDMWMVGADESRRLLWEAADEA 86
Cdd:COG1797    3 IPRLVIAAPHSGSGKTTVTLGLLAALRRRGLKVQPFKVGPDYIDPGYHTLATGRPSRNLDPFLMGEEGVRELFARGSAGA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366  87 DLILIEGVMGLFDG------TPSSADLSRHFGVPVLGVIDGTAMAQTFGALALGLARYQPDLPFAGVLANRVGTVRHAQL 160
Cdd:COG1797   83 DIAVIEGVMGLYDGldgdsgSGSTAHLAKLLGAPVVLVVDASGMSRSAAALVLGFRAFDPDVRIAGVILNRVGSERHEEL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366 161 LENSLTE--GLRWYGALSREVGFELPSRHLGLVQASELNDLDVRLDMAAAALASTC------EVALPPAVTFTAPDPVHV 232
Cdd:COG1797  163 LREAIEHytGIPVLGALPRDEELELPSRHLGLVPAAEREELEEALDRLAELVEEHVdldallELARSAPPLPAPPSPLFA 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366 233 EPLLRGVRIAIARDEAFAFLYGASLELLRNMGAELSFFSPIHDRELPE-ADSLYLPGGYPELHHVALAANGTMQASIRAH 311
Cdd:COG1797  243 PPPGPRVRIAVARDEAFNFYYPENLELLEAAGAELVFFSPLRDEALPEdVDGLYLGGGFPELFAEELSANRSMRESIREA 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366 312 HIAGKPILAECGGMLYLLEALTDVEGVRAELVGLLSGEAVMQKRLAAL------ALQA-VELPEGT-LHGHTYHHS-LTS 382
Cdd:COG1797  323 AEAGMPIYAECGGLMYLCRSITDFEGKGYPMVGVLPGDAVMTKRLQGLgyreatALGDsPLGPAGErIRGHEFHYStLTP 402
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 764123366 383 T-ELQPIARGVSPNGGRGAEAVYRLGRLTASYVHFYFPSCPRAIAALFK 430
Cdd:COG1797  403 EgDLRPAYRLRRGRGIDGGRDGFVYGNVLASYLHLHFASNPEWAERFVA 451
cobB TIGR00379
cobyrinic acid a,c-diamide synthase; This model describes cobyrinic acid a,c-diamide synthase, ...
10-430 1.11e-86

cobyrinic acid a,c-diamide synthase; This model describes cobyrinic acid a,c-diamide synthase, the cobB (cbiA in Salmonella) protein of cobalamin biosynthesis. It is responsible for the amidation of carboxylic groups at positions A and C of either cobyrinic acid or hydrogenobrynic acid. NH(2) groups are provided by glutamine and one molecule of ATP hydrogenolyzed for each amidation. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 273044 [Multi-domain]  Cd Length: 449  Bit Score: 271.29  E-value: 1.11e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366   10 VLIAAPASGQGKTTVTAALARLHRNQGRKVRVFKCGPDFLDPMILERASGAPVYQLDMWMVGADESRRLLWEAADEADLI 89
Cdd:TIGR00379   2 VVIAGTSSGVGKTTISTGIMKALSRRKLRVQPFKVGPDYIDPMFHTQATGRPSRNLDSFFMSEAQIQECFHRHSKGTDYS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366   90 LIEGVMGLFDG------TPSSADLSRHFGVPVLGVIDGTAMAQTFGALALGLARYQPDLPFAGVLANRVGTVRHAQLLEN 163
Cdd:TIGR00379  82 IIEGVRGLYDGisaitdYGSTASVAKALDAPIVLVMNCQRLSRSAAAIVLGYRSFDPGVKLKGVILNRVGSERHLEKLKI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366  164 SLTE--GLRWYGALSREVGFELPSRHLGLVQASELNDLDVRLDMAAAALASTCEV-ALPPAVTFTAPDPVHVEPLL---- 236
Cdd:TIGR00379 162 AVEPlrGIPILGVIPRQQDLKVPDRHLGLVPAGEREIIQQIFDWLAEVVEKYLDLdKLLEIAETARNLPSPMSLLWepqn 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366  237 -RGVRIAIARDEAFAFLYGASLELLRNMGAELSFFSPIHDRELPEADSLYLPGGYPELHHVALAANGTMQASIRAHHIAG 315
Cdd:TIGR00379 242 sKYVRIAVAQDQAFNFYYQDNLDALTHNAAELVPFSPLEDTELPDVDAVYIGGGFPELFAEELSQNQALRDSIKTFIHQG 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366  316 KPILAECGGMLYLLEALTDVEGvRAELVGLLSGEAVMQKRLAALALQAVELPEG--------TLHGHTYHHS-LTSTELQ 386
Cdd:TIGR00379 322 LPIYGECGGLMYLSQSLDNFEG-QIFMVGMLPTAATMTGRVQGLGYVQAEVVNDclilwqgeKFRGHEFHYSrMTKLPNA 400
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 764123366  387 PIARGVSpnggRGAEAVYRL-----GRLTASYVHFYFPSCPRAIAALFK 430
Cdd:TIGR00379 401 QFAYRVE----RGRGIIDQLdgicvGSVLASYLHLHAGSVPKFAAAFVA 445
CobB_N cd05388
N-terminal domain of cobyrinic acid a,c-diamide synthase; Cobyrinic acid a,c-diamide synthase ...
8-192 6.81e-78

N-terminal domain of cobyrinic acid a,c-diamide synthase; Cobyrinic acid a,c-diamide synthase (CobB, CbiA). Biosynthesis of cobalamin (vitamin B12) requires more than two dozen different enzymes. CobB catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinic acid, via the formation of a phosphorylated intermediate, using glutamine or ammonia as the nitrogen source. CobB is comprised of two protein domains: the C-terminal glutaminase domain and the N-terminal ATP-binding domain. The glutaminase domain catalyzes the hydrolysis of glutamine to glutamate and ammonia. It belongs to the triad class of glutamine amidotransferases. This classification is based on the N-terminal domain which catalyzes the ultimate synthesis of the diamide product by using energy from the hydrolysis of ATP and ammonia transferred from the C-terminal domain.


Pssm-ID: 349773 [Multi-domain]  Cd Length: 193  Bit Score: 239.81  E-value: 6.81e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366   8 PAVLIAAPASGQGKTTVTAALARLHRNQGRKVRVFKCGPDFLDPMILERASGAPVYQLDMWMVGADESRRLLWEAADEAD 87
Cdd:cd05388    1 PRIVIAGTSSGSGKTTITLGLMRALARRGLRVQPFKVGPDYIDPGFHEAATGRPSRNLDSWMMGEDGVRELFARAAGGAD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366  88 LILIEGVMGLFDG------TPSSADLSRHFGVPVLGVIDGTAMAQTFGALALGLARYQPDLPFAGVLANRVGTVRHAQLL 161
Cdd:cd05388   81 VAIIEGVMGLYDGrdtdsdEGSTAELARLLGAPVLLVLDCKGMARSAAAIVKGYKEFDPDLNLAGVILNRVGSPRHAELL 160
                        170       180       190
                 ....*....|....*....|....*....|...
gi 764123366 162 ENSLTE--GLRWYGALSREVGFELPSRHLGLVQ 192
Cdd:cd05388  161 KEAIEEytGIPVLGYLPRDDELTLPERHLGLVP 193
F430_CfbB NF033195
Ni-sirohydrochlorin a,c-diamide synthase; Members of this family are Ni-sirohydrochlorin a, ...
9-422 6.24e-77

Ni-sirohydrochlorin a,c-diamide synthase; Members of this family are Ni-sirohydrochlorin a,c-diamide synthase, involving in synthesizing coenzyme F430, used in methanogens by coenzyme M reductase. Members of this family are restricted to archaeal methanogens, and resemble (and may be misannotated as) the enzyme cobyrinic acid a,c-diamide synthase, involved in cobalamin biosynthesis.


Pssm-ID: 467990 [Multi-domain]  Cd Length: 451  Bit Score: 246.33  E-value: 6.24e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366   9 AVLIAAPASGQGKTTVTAALARLhRNQGRKVRVFKCGPDFLDPMILERASGAPVYQLDMWMVGADESRRLLWEAADEADL 88
Cdd:NF033195   1 RVLIAGDRSGSGKTTITTGIMAA-LSKGYNVQPFKVGPDYIDPSYHTGATGRPSRNLDSFFMSEEQIREVFAHGCKGADI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366  89 ILIEGVMGLFDG------TPSSADLSRHFGVPVLGVIDGTAMAQTFGALALGLARYQPDLPFAGVLANRVGTVRHAqlle 162
Cdd:NF033195  80 AIIEGVRGLYEGieslgdVGSTASIAKALNAPVILVINARSITRSAAAIVKGFKAFDPDVNIAGVILNNVGGERHA---- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366 163 NSLTEGLRWY------GALSREVGFELPSRHLGLVQASE---LNDLDVRLDMAAAALASTCEVALPPAVTFTAPD-PVHV 232
Cdd:NF033195 156 KKAKEAIEHYtgvpviGAIPRDEEMKLSMRHLGLVPAVEgreRGEFLERIEKIGEIIEENLDLDALLEIAKEAFPlPEPE 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366 233 EPLL------RGVRIAIARDEAFAFLYGASLELLRNMGAELSFFSPIHDRELPEADSLYLPGGYPELHHVALAANGTMQA 306
Cdd:NF033195 236 EDLFlweenkNDVKIGVALDEAFNFYYADNFDALEANGAEIVYFSPLHDEELPDVDGLYIGGGYPELFAAELEANKSMRE 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366 307 SIRAHHIAGKPILAECGGMLYLLEALT---DVEGVRAELVGLLSGEAVMQKRlaalalQAVELPEGTL------------ 371
Cdd:NF033195 316 SIREFSGDGTPIYAECGGLMYLTESIDlqgKGEESSYEMVGVFPGHTVMKAV------RVLSYVIGEFskdcpigkkget 389
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 764123366 372 -HGHTYHHS----LTSTELQ-PIARGVSPNGGR-GAEAvyrlGRLTASYVHFYFPSCP 422
Cdd:NF033195 390 fRGHEFHYSkvtlDPETKFAyKLSRGTGIIDGLdGLVV----NNTLGSYTHLHAVSYP 443
PRK13896 PRK13896
cobyrinic acid a,c-diamide synthase; Provisional
10-379 9.14e-74

cobyrinic acid a,c-diamide synthase; Provisional


Pssm-ID: 184379 [Multi-domain]  Cd Length: 433  Bit Score: 237.35  E-value: 9.14e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366  10 VLIAAPASGQGKTTVTAALARLHRNQGRKVRVFKCGPDFLDPMILERASGAPVYQLDMWMVGADESRRLLWEAadEADLI 89
Cdd:PRK13896   4 FVLGGTSSGVGKTVATLATIRALEDAGYAVQPAKAGPDFIDPSHHEAVAGRPSRTLDPWLSGEDGMRRNYYRG--EGDIC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366  90 LIEGVMGLFDGTPSS-ADLSRHFGVPVLGVIDGTAMAQTFGALALGLARYQP----DLPFAGVLANRVGTVRHAQLLENS 164
Cdd:PRK13896  82 VVEGVMGLYDGDVSStAMVAEALDLPVVLVVDAKAGMESVAATALGFRAYADrigrDIDVAGVIAQRAHGGRHADGIRDA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366 165 LTEGLRWYGALSREVGFELPSRHLGLVQASELNDLDVRLDMAAAALASTCEVAL---PPAVTFTAPDPVHVEPllrgvRI 241
Cdd:PRK13896 162 LPDELTYFGRIPPRDDLEIPDRHLGLHMGSEAPLDDDALDEAAEHIDAERLAAVarePPRPEPPEEAPATGDP-----TV 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366 242 AIARDEAFAFLYGASLELLRNMgAELSFFSPIHDRELPEADSLYLPGGYPELHHVALAANGTMQaSIRAHHIAGKPILAE 321
Cdd:PRK13896 237 AVARDAAFCFRYPATIERLRER-ADVVTFSPVAGDPLPDCDGVYLPGGYPELHADALADSPALD-ELADRAADGLPVLGE 314
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 764123366 322 CGGMLYLLEALTDVEGVRAELVGLLSGEAVMQKRLAALALQAVELPEGTL--------HGHTYHHS 379
Cdd:PRK13896 315 CGGLMALAESLTTTDGDTHEMAGVLPADVTMQDRYQALDHVELRATDDTLtagagetlRGHEFHYS 380
GATase1_CobB cd03130
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyrinic Acid a,c-Diamide ...
241-429 3.92e-71

Type 1 glutamine amidotransferase (GATase1) domain found in Cobyrinic Acid a,c-Diamide Synthase; Type 1 glutamine amidotransferase (GATase1) domain found in Cobyrinic Acid a,c-Diamide Synthase. CobB plays a role in cobalamin biosythesis catalyzing the conversion of cobyrinic acid to cobyrinic acid a,c-diamide. CobB belongs to the triad family of amidotransferases. Two of the three residues of the catalytic triad that are involved in glutamine binding, hydrolysis and transfer of the resulting ammonia to the acceptor substrate in other triad aminodotransferases are conserved in CobB.


Pssm-ID: 153224 [Multi-domain]  Cd Length: 198  Bit Score: 222.86  E-value: 3.92e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366 241 IAIARDEAFAFLYGASLELLRNMGAELSFFSPIHDRELPEADSLYLPGGYPELHHVALAANGTMQASIRAHHIAGKPILA 320
Cdd:cd03130    1 IAVARDEAFNFYYPENLELLEAAGAELVPFSPLKDEELPDADGLYLGGGYPELFAEELSANQSMRESIRAFAESGGPIYA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366 321 ECGGMLYLLEALTDVEGVRAELVGLLSGEAVMQKRLA-------ALALQAVELPEGTLHGHTYHHS--LTSTELQPIARG 391
Cdd:cd03130   81 ECGGLMYLGESLDDEEGQSYPMAGVLPGDARMTKRLGlgyreaeALGDTLLGKKGTTLRGHEFHYSrlEPPPEPDFAATV 160
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 764123366 392 VSPNGGRGAEAVYRLGRLTASYVHFYFPSCPRAIAALF 429
Cdd:cd03130  161 RRGRGIDGGEDGYVYGNVLASYLHLHWASNPDLAERFV 198
GATase_3 pfam07685
CobB/CobQ-like glutamine amidotransferase domain;
240-418 1.97e-37

CobB/CobQ-like glutamine amidotransferase domain;


Pssm-ID: 429595 [Multi-domain]  Cd Length: 189  Bit Score: 134.68  E-value: 1.97e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366  240 RIAIARDEAFAFLYGASLELLRNMGAELSFFSPIHDRELPE-ADSLYLPGGYPELHHVALAANGTMQASIRAHHIAGKPI 318
Cdd:pfam07685   1 RIAVIRLPRISNYTDDNLDPLRYEPAVRVRFVPLPDESLGPdADLIILPGGKPTIQDLALLRNSGMDEAIKEAAEDGGPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366  319 LAECGGMLYLLEALTDVEGVRAELVGLLSGEAVMQKRLAALALQAVELPEG-TLHGHTYHHSLTSTE--LQP---IARGV 392
Cdd:pfam07685  81 LGICGGYQMLGETIEDPEGVRIEGLGLLDIETVFQKEKLTGQVVGYLLLEGeTVRGYEIHYGRTILGdgAKPlgrVKVGG 160
                         170       180
                  ....*....|....*....|....*..
gi 764123366  393 SPNGGRGAE-AVYrlGRLTASYVHFYF 418
Cdd:pfam07685 161 GNNGEDGKDgAVS--GNVFGTYLHGHF 185
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
10-190 2.22e-18

CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid a,c-diamide synthases. These include CbiA and CbiP from S.typhimurium, and CobQ from R. capsulatus. These amidases catalyze amidations to various side chains of hydrogenobyrinic acid or cobyrinic acid a,c-diamide in the biosynthesis of cobalamin (vitamin B12) from uroporphyrinogen III. Vitamin B12 is an important cofactor and an essential nutrient for many plants and animals and is primarily produced by bacteria. The family also contains dethiobiotin synthetases as well as the plasmid partitioning proteins of the MinD/ParA family.


Pssm-ID: 426369 [Multi-domain]  Cd Length: 228  Bit Score: 83.55  E-value: 2.22e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366   10 VLIAAPASGQGKTTVTAALARLHRNQGRKVRVFKCGPD-----------FLDPMILERASG-APVYQLDMWMVGADES-- 75
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQsnnssveglegDIAPALQALAEGlKGRVNLDPILLKEKSDeg 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366   76 ---------------------------RRLLWEAADEADLILIEGVMGLFDGT----PSSADLSRHFGVPVLGVIDGTAM 124
Cdd:pfam01656  81 gldlipgnidlekfekellgprkeerlREALEALKEDYDYVIIDGAPGLGELLrnalIAADYVIIPLEPEVILVEDAKRL 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366  125 AQTFGALALGLAryQPDLPFAGVLANRVGTVRHAQLLENSLTE---GLRWYGALSREVGF-ELPSRHLGL 190
Cdd:pfam01656 161 GGVIAALVGGYA--LLGLKIIGVVLNKVDGDNHGKLLKEALEEllrGLPVLGVIPRDEAVaEAPARGLPV 228
DTBS cd03109
dethiobiotin synthetase; Dethiobiotin synthetase (DTBS) is the penultimate enzyme in the ...
8-153 7.55e-10

dethiobiotin synthetase; Dethiobiotin synthetase (DTBS) is the penultimate enzyme in the biotin biosynthesis pathway in Escherichia coli and other microorganisms. The enzyme catalyzes formation of the ureido ring of dethiobiotin from (7R,8S)-7,8-diaminononanoic acid (DAPA) and carbon dioxide. The enzyme utilizes carbon dioxide instead of hydrogen carbonate as substrate and is dependent on ATP and divalent metal ions as cofactors.


Pssm-ID: 349763 [Multi-domain]  Cd Length: 189  Bit Score: 57.96  E-value: 7.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366   8 PAVLIAAPASGQGKTTVTAALARLHRNQGRKVRVFK---CGPDFL---DPMILERASGAPVYQLDMWMV----------- 70
Cdd:cd03109    1 KTLFVTGTDTDVGKTVVSAGLARALRKKGIKVGYLKpvqTGCPGLedsDAELLRKLAGLLLDLELINPYrfeaplsphla 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366  71 GADESRRLLWE--------AADEADLILIEGVMGLFDGTPSS---ADLSRHFGVPVLGVIDGT--AMAQTFGALALGLAR 137
Cdd:cd03109   81 AELEGRDIDLEeivraleeLAKSYDVVLVEGAGGLLVPLTEGylnADLARALGLPVILVARGGlgTINHTLLTLEALKSR 160
                        170
                 ....*....|....*.
gi 764123366 138 YqpdLPFAGVLANRVG 153
Cdd:cd03109  161 G---LDVAGVVLNGIP 173
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
241-329 1.05e-07

Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.


Pssm-ID: 153210 [Multi-domain]  Cd Length: 115  Bit Score: 50.29  E-value: 1.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366 241 IAIARDEAFAFLYGAS-LELLRNMGAELSFFSP-----IHDRELPEADSLYLPGGYPELHhvALAANGTMQASIRAHHIA 314
Cdd:cd01653    1 VAVLLFPGFEELELASpLDALREAGAEVDVVSPdggpvESDVDLDDYDGLILPGGPGTPD--DLARDEALLALLREAAAA 78
                         90
                 ....*....|....*
gi 764123366 315 GKPILAECGGMLYLL 329
Cdd:cd01653   79 GKPILGICLGAQLLV 93
CobQ COG1492
Cobyric acid synthase [Coenzyme transport and metabolism]; Cobyric acid synthase is part of ...
8-415 2.43e-07

Cobyric acid synthase [Coenzyme transport and metabolism]; Cobyric acid synthase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441101 [Multi-domain]  Cd Length: 493  Bit Score: 52.75  E-value: 2.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366   8 PAVLIAAPASGQGKTTVTAALARLHRNQGRKVRVFK---------------------------CGpdfLDP---M--IL- 54
Cdd:COG1492    3 KALMVQGTTSDAGKSLLVAALCRILARRGYRVAPFKaqnmslnsavtadggeigraqalqaeaAG---VEPsvdMnpVLl 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366  55 ----ERAS-----GAPVYQLDmwmvGAD--ESRRLLWEA--------ADEADLILIEGV---------------MGLfdg 100
Cdd:COG1492   80 kpegDTGSqvivqGKPVGNMS----ARDyyEYKPRLLEAvlesldrlAAEYDLVVIEGAgspaeinlrdrdianMGF--- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366 101 tpssadlSRHFGVPVLGVID---GTAMAQTFGALALglaryqpdLP------FAGVLANRV-GTVRhaqLLEnsltEGLR 170
Cdd:COG1492  153 -------AEAADAPVILVGDidrGGVFASLVGTLAL--------LPeeerarVKGFIINKFrGDPS---LLE----PGLD 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366 171 WygaLSREVGfeLPSrhLGLVQAseLNDLDvrldmaaaalastcevaLPP--AVTFTAPDPVHVEpllRGVRIAIAR--- 245
Cdd:COG1492  211 W---LEERTG--VPV--LGVLPY--LEDLR-----------------LPAedSLALESRRGSKGG---GRLRIAVIRlpr 261
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366 246 -----DeafaflygasLELLRNM-GAELSFFSPihDRELPEADSLYLPGG---YPELHhvALAANGtMQASIRAHHIAGK 316
Cdd:COG1492  262 isnftD----------FDPLAAEpGVRLRYVRP--PEELGDADLVILPGSkntIADLA--WLRESG-LDDAIRAHARRGG 326
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366 317 PILAECGGMLYLLEALTD---VEGVRAEL--VGLLSGEAVMQ--KRLAALALQAVELPEG-TLHGHTYHHSltSTELQPI 388
Cdd:COG1492  327 PVLGICGGYQMLGRRIADpdgVEGGAGEVpgLGLLPVETVFApeKTLRQVTGTLLGPLSGaPVSGYEIHMG--RTTGPDG 404
                        490       500
                 ....*....|....*....|....*...
gi 764123366 389 ARGVSPNGGRGAE-AVYRLGRLTASYVH 415
Cdd:COG1492  405 ARPLLRRDGREPDgAVSADGRVWGTYLH 432
PtaN COG0857
BioD-like N-terminal domain of phosphotransacetylase [General function prediction only];
10-153 8.48e-07

BioD-like N-terminal domain of phosphotransacetylase [General function prediction only];


Pssm-ID: 440618 [Multi-domain]  Cd Length: 697  Bit Score: 51.37  E-value: 8.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366  10 VLIAAPASGQGKTTVTAALARLHRNQGRKVRVFK---------CGPDFlDPMILERASGAPVYQLDMWMVGADESRRLLW 80
Cdd:COG0857    5 IYIASTEPGSGKTSVALGLARALQRKGLRVGYFKpigqslvggGERDE-DVELIREHLGLDLPYEDASPVTLDEVETLLA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366  81 ----------------EAADEADLILIEG-----VMGLFDGTpSSADLSRHFGVPVLGVI--DGTAMAQTFGALALGLAR 137
Cdd:COG0857   84 egdpdelleriveryeALAAECDVVLVEGsdptgVGSPFELS-LNARIAKNLGAPVLLVAsgGGRTPEELVDALLLAADE 162
                        170
                 ....*....|....*..
gi 764123366 138 Y-QPDLPFAGVLANRVG 153
Cdd:COG0857  163 FrGEGARVLGVIINRVP 179
BioD COG0132
Dethiobiotin synthetase [Coenzyme transport and metabolism]; Dethiobiotin synthetase is part ...
20-152 8.99e-07

Dethiobiotin synthetase [Coenzyme transport and metabolism]; Dethiobiotin synthetase is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 439902 [Multi-domain]  Cd Length: 222  Bit Score: 49.39  E-value: 8.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366  20 GKTTVTAALARLHRNQGRKVRVFK----------CGPDFLDPMILERASGAPV-------YQLDM----WMVGADESRRL 78
Cdd:COG0132   14 GKTVVTAALAAALRAAGLRVGYYKpvqtgceetdGGLRNGDAELLRRLSGLPLsyelvnpYRFEEplspHLAARLEGVPI 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366  79 ----LWEA----ADEADLILIEGVMGLF---DGTPSSADLSRHFGVPV-------LGVIDGTamaqtfgALALGLARyQP 140
Cdd:COG0132   94 dldkILAAlralAARYDLVLVEGAGGLLvplTEDLTLADLAKALGLPVilvvrarLGTINHT-------LLTVEALR-AR 165
                        170
                 ....*....|..
gi 764123366 141 DLPFAGVLANRV 152
Cdd:COG0132  166 GLPLAGIVLNGV 177
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
241-328 1.08e-06

Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain.


Pssm-ID: 153222 [Multi-domain]  Cd Length: 92  Bit Score: 46.42  E-value: 1.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366 241 IAIARDEAFAFLYGAS-LELLRNMGAELSFFSPIHDRE-----LPEADSLYLPGGYPELHhvALAANGTMQASIRAHHIA 314
Cdd:cd03128    1 VAVLLFGGSEELELASpLDALREAGAEVDVVSPDGGPVesdvdLDDYDGLILPGGPGTPD--DLAWDEALLALLREAAAA 78
                         90
                 ....*....|....
gi 764123366 315 GKPILAECGGMLYL 328
Cdd:cd03128   79 GKPVLGICLGAQLL 92
AAA_26 pfam13500
AAA domain; This domain is found in a number of proteins involved in cofactor biosynthesis ...
9-152 7.06e-06

AAA domain; This domain is found in a number of proteins involved in cofactor biosynthesis such as dethiobiotin synthase and cobyric acid synthase. This domain contains a P-loop motif.


Pssm-ID: 433259 [Multi-domain]  Cd Length: 198  Bit Score: 46.48  E-value: 7.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366    9 AVLIAAPASGQGKTTVTAALARLHRNQGRKVRVFK----------------------CGPDFLDPMILERASgAPVYQLD 66
Cdd:pfam13500   2 TLFVTGTDTGVGKTVVSLGLARALKRRGVKVGYWKpvqtglvedgdselvkrllgldQSYEDPEPFRLSAPL-SPHLAAR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366   67 MWMVgADESRRLLWEAADEADLILIEGVMGLFDG---TPSSADLSRHFGVPVLGVIDGT--AMAQTfgALALGLARYQpD 141
Cdd:pfam13500  81 QEGV-TIDLEKIIYELPADADPVVVEGAGGLLVPineDLLNADIAANLGLPVILVARGGlgTINHT--LLTLEALRQR-G 156
                         170
                  ....*....|.
gi 764123366  142 LPFAGVLANRV 152
Cdd:pfam13500 157 IPVLGVILNGV 167
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
8-151 2.56e-05

SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal recognition particle, MinD, and BioD), consists of signal recognition particle (SRP) GTPases, the assemblage of MinD-like ATPases, which are involved in protein localization, chromosome partitioning, and membrane transport, and a group of metabolic enzymes with kinase or related phosphate transferase activity. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion.


Pssm-ID: 349751 [Multi-domain]  Cd Length: 107  Bit Score: 43.19  E-value: 2.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366   8 PAVLIAAPASGQGKTTVTAALARLHRNQGRKVRVFKCgpdfldpmilerasgapvyqldmwmvgadesrrllweaadeAD 87
Cdd:cd01983    1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDL-----------------------------------------DD 39
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 764123366  88 LILIEGVMGLFDGTPS---SADLSRHFGVPVLGVIDGTAMAQTFGALALGLARYQ-PDLPFAGVLANR 151
Cdd:cd01983   40 YVLIDGGGGLETGLLLgtiVALLALKKADEVIVVVDPELGSLLEAVKLLLALLLLgIGIRPDGIVLNK 107
PRK00784 PRK00784
cobyric acid synthase;
7-415 4.46e-05

cobyric acid synthase;


Pssm-ID: 234838 [Multi-domain]  Cd Length: 488  Bit Score: 45.46  E-value: 4.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366   7 CPAVLIAAPASGQGKTTVTAALARLHRNQGRKVRVFK---------------------------CGpdfLDP---M--IL 54
Cdd:PRK00784   2 AKALMVQGTASDAGKSTLVAGLCRILARRGYRVAPFKaqnmslnsavtadggeigraqalqaeaAG---VEPsvdMnpVL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366  55 -----ERAS-----GAPV-------YQldmwmvgadESRRLLWEA--------ADEADLILIEGV-----MGLFDGtpss 104
Cdd:PRK00784  79 lkpqsDRGSqvivqGKPVgnmdardYH---------DYKPRLLEAvlesldrlAAEYDVVVVEGAgspaeINLRDR---- 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366 105 aDL-----SRHFGVPVLGV--ID-GTAMAQTFGALALglaryqpdLP------FAGVLANRV-GTVRhaqLLEnsltEGL 169
Cdd:PRK00784 146 -DIanmgfAEAADAPVILVadIDrGGVFASLVGTLAL--------LPpeerarVKGFIINKFrGDIS---LLE----PGL 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366 170 RWygaLSREVGfeLPSrhLGLVQASELNDLD-----VRLDMAAAALASTCEVALP--PAVT-FTAPDPVHVEPllrGVRI 241
Cdd:PRK00784 210 DW---LEELTG--VPV--LGVLPYLDDLRLPaedslALLERAARAGGGALRIAVIrlPRISnFTDFDPLRAEP---GVDV 279
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366 242 AIARdeafaflygaslellrnmgaelsffspiHDRELPEADSLYLPG-----GypELHhvALAANGtMQASIRAHHIAGK 316
Cdd:PRK00784 280 RYVR----------------------------PGEPLPDADLVILPGskntiA--DLA--WLRESG-WDEAIRAHARRGG 326
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366 317 PILAECGGMLYLLEALTDVEGVRAEL-----VGLLSGEAVMQ--KRLAalALQAVELPEG-TLHGHTYHHSLTSTelQPI 388
Cdd:PRK00784 327 PVLGICGGYQMLGRRIADPDGVEGAPgsvegLGLLDVETVFEpeKTLR--QVTGLLLGSGaPVSGYEIHMGRTTG--PAL 402
                        490       500
                 ....*....|....*....|....*...
gi 764123366 389 ARGVSPNGGRGAE-AVYRLGRLTASYVH 415
Cdd:PRK00784 403 ARPFLRLDDGRPDgAVSADGRVFGTYLH 430
PRK05632 PRK05632
phosphate acetyltransferase; Reviewed
10-153 1.44e-04

phosphate acetyltransferase; Reviewed


Pssm-ID: 235537 [Multi-domain]  Cd Length: 684  Bit Score: 43.99  E-value: 1.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366  10 VLIAAPASGQGKTTVTAALARLHRNQGRKVRVFKcgPDFLDPMILERASGapvyqldmwMVGADESRRLLWE-------A 82
Cdd:PRK05632   5 IYLAPTGTGVGLTSVSLGLMRALERKGVKVGFFK--PIAQPPLTMSEVEA---------LLASGQLDELLEEivaryhaL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366  83 ADEADLILIEGVmgLFDGTPSS-----ADLSRHFGVPVLGVIDG---TAmAQTFGALALGLARYQPDL--PFAGVLANRV 152
Cdd:PRK05632  74 AKDCDVVLVEGL--DPTRKHPFefslnAEIAKNLGAEVVLVSSGgndTP-EELAERIELAASSFGGAKnaNILGVIINKL 150

                 .
gi 764123366 153 G 153
Cdd:PRK05632 151 N 151
GATase1_CobQ cd01750
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type ...
274-415 1.54e-04

Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ). CobQ plays a role in cobalamin biosythesis. CobQ catalyses amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide in the biosynthesis of cobalamin. CobQ belongs to the triad family of amidotransferases. Two of the three residues of the catalytic triad that are involved in glutamine binding, hydrolysis and transfer of the resulting ammonia to the acceptor substrate in other triad aminodotransferases are conserved in CobQ.


Pssm-ID: 153221 [Multi-domain]  Cd Length: 194  Bit Score: 42.62  E-value: 1.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764123366 274 HDRELPEADSLYLPGG--YPE-LhhVALAANGtMQASIRAHHIAGKPILAECGGMLYLLEALTDVEGVRAEL----VGLL 346
Cdd:cd01750   31 VPEGLGDADLIILPGSkdTIQdL--AWLRKRG-LAEAIKNYARAGGPVLGICGGYQMLGKYIVDPEGVEGPGeiegLGLL 107
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 764123366 347 SGEAVMQ--KRLAALALQAVELPEG-TLHGHTYHHSLT--STELQPIARGVSPNGGRGAEAVYRLGRLTASYVH 415
Cdd:cd01750  108 DVETEFGpeKTTRRVTGRLDEEGEGgEVTGYEIHSGRTtlGDGARPLGKGYGNNGEDGTDGAVSGDNVIGTYLH 181
 
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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