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Conserved domains on  [gi|1934963221|gb|QPF76769|]
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cobyric acid synthase [Kinneretia sp. DAIF2]

Protein Classification

CobQ family protein( domain architecture ID 11445265)

CobQ family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CobQ COG1492
Cobyric acid synthase [Coenzyme transport and metabolism]; Cobyric acid synthase is part of ...
 1-477 0e+00

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: 653.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221   1 MVLGTTSGAGKSFLATALCRWYADQGLKVAPFKAQNMSNNARVVP-GlagqmGEIGSAQYFQALAARRVPEVRMNPVLLK 79
Cdd:COG1492     6 MVQGTTSDAGKSLLVAALCRILARRGYRVAPFKAQNMSLNSAVTAdG-----GEIGRAQALQAEAAGVEPSVDMNPVLLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221  80 PEADTKSQVVVLGEVHPELNATPWRERSEKLWPHARAALHELLAENELVVIEGAGSPAEINLHSSDYVNMRTAREANAAC 159
Cdd:COG1492    81 PEGDTGSQVIVQGKPVGNMSARDYYEYKPRLLEAVLESLDRLAAEYDLVVIEGAGSPAEINLRDRDIANMGFAEAADAPV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221 160 LLATDIDRGGAFAHLYGTHQLLPPEERALIRGFVLNRFRGDARLLAPGPEQLQALTGVPTLATLPMWRGHGLPEEDGVFD 239
Cdd:COG1492   161 ILVGDIDRGGVFASLVGTLALLPEEERARVKGFIINKFRGDPSLLEPGLDWLEERTGVPVLGVLPYLEDLRLPAEDSLAL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221 240 D----GASGSGLRIAIVAYPRLSNLDEFQPLRALPGLRLSWARSPAELAGADWIILPGSKAVAADLAWLREQKLDLAIAA 315
Cdd:COG1492   241 EsrrgSKGGGRLRIAVIRLPRISNFTDFDPLAAEPGVRLRYVRPPEELGDADLVILPGSKNTIADLAWLRESGLDDAIRA 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221 316 HAAAGRPVLGICGGLQMLGEALLDPHQLDGNA---PGLGLLPLVTQFEREKLLRPTRMRFAqrldapwAGLADVAAEGYE 392
Cdd:COG1492   321 HARRGGPVLGICGGYQMLGRRIADPDGVEGGAgevPGLGLLPVETVFAPEKTLRQVTGTLL-------GPLSGAPVSGYE 393

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221 393 IHHGRTAQHP-ALPLASVALRDERGeAIgWQQGPVLGHYVHGLFEQPAVLQALFGQ----------------SGQSLDQV 455
Cdd:COG1492   394 IHMGRTTGPDgARPLLRRDGREPDG-AV-SADGRVWGTYLHGLFDNDAFRRALLNAlrekkglsplaagavdYAARREAA 471

                         490       500
                  ....*....|....*....|..
gi 1934963221 456 FDGLADYVDTHFRPGTLLSLIR 477
Cdd:COG1492   472 LDRLADHVEEHLDLDALLALLG 493
 
Name Accession Description Interval E-value
CobQ COG1492
Cobyric acid synthase [Coenzyme transport and metabolism]; Cobyric acid synthase is part of ...
 1-477 0e+00

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: 653.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221   1 MVLGTTSGAGKSFLATALCRWYADQGLKVAPFKAQNMSNNARVVP-GlagqmGEIGSAQYFQALAARRVPEVRMNPVLLK 79
Cdd:COG1492     6 MVQGTTSDAGKSLLVAALCRILARRGYRVAPFKAQNMSLNSAVTAdG-----GEIGRAQALQAEAAGVEPSVDMNPVLLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221  80 PEADTKSQVVVLGEVHPELNATPWRERSEKLWPHARAALHELLAENELVVIEGAGSPAEINLHSSDYVNMRTAREANAAC 159
Cdd:COG1492    81 PEGDTGSQVIVQGKPVGNMSARDYYEYKPRLLEAVLESLDRLAAEYDLVVIEGAGSPAEINLRDRDIANMGFAEAADAPV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221 160 LLATDIDRGGAFAHLYGTHQLLPPEERALIRGFVLNRFRGDARLLAPGPEQLQALTGVPTLATLPMWRGHGLPEEDGVFD 239
Cdd:COG1492   161 ILVGDIDRGGVFASLVGTLALLPEEERARVKGFIINKFRGDPSLLEPGLDWLEERTGVPVLGVLPYLEDLRLPAEDSLAL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221 240 D----GASGSGLRIAIVAYPRLSNLDEFQPLRALPGLRLSWARSPAELAGADWIILPGSKAVAADLAWLREQKLDLAIAA 315
Cdd:COG1492   241 EsrrgSKGGGRLRIAVIRLPRISNFTDFDPLAAEPGVRLRYVRPPEELGDADLVILPGSKNTIADLAWLRESGLDDAIRA 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221 316 HAAAGRPVLGICGGLQMLGEALLDPHQLDGNA---PGLGLLPLVTQFEREKLLRPTRMRFAqrldapwAGLADVAAEGYE 392
Cdd:COG1492   321 HARRGGPVLGICGGYQMLGRRIADPDGVEGGAgevPGLGLLPVETVFAPEKTLRQVTGTLL-------GPLSGAPVSGYE 393

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221 393 IHHGRTAQHP-ALPLASVALRDERGeAIgWQQGPVLGHYVHGLFEQPAVLQALFGQ----------------SGQSLDQV 455
Cdd:COG1492   394 IHMGRTTGPDgARPLLRRDGREPDG-AV-SADGRVWGTYLHGLFDNDAFRRALLNAlrekkglsplaagavdYAARREAA 471

                         490       500
                  ....*....|....*....|..
gi 1934963221 456 FDGLADYVDTHFRPGTLLSLIR 477
Cdd:COG1492   472 LDRLADHVEEHLDLDALLALLG 493
PRK00784 PRK00784
cobyric acid synthase;
1-476 0e+00

cobyric acid synthase;


Pssm-ID: 234838 [Multi-domain]  Cd Length: 488  Bit Score: 578.58  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221   1 MVLGTTSGAGKSFLATALCRWYADQGLKVAPFKAQNMSNNARVVPGlaGqmGEIGSAQYFQALAARRVPEVRMNPVLLKP 80
Cdd:PRK00784    6 MVQGTASDAGKSTLVAGLCRILARRGYRVAPFKAQNMSLNSAVTAD--G--GEIGRAQALQAEAAGVEPSVDMNPVLLKP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221  81 EADTKSQVVVLGEVHPELNATPWRERSEKLWPHARAALHELLAENELVVIEGAGSPAEINLHSSDYVNMRTAREANAACL 160
Cdd:PRK00784   82 QSDRGSQVIVQGKPVGNMDARDYHDYKPRLLEAVLESLDRLAAEYDVVVVEGAGSPAEINLRDRDIANMGFAEAADAPVI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221 161 LATDIDRGGAFAHLYGTHQLLPPEERALIRGFVLNRFRGDARLLAPGPEQLQALTGVPTLATLPMWRGHGLPEEDGV--- 237
Cdd:PRK00784  162 LVADIDRGGVFASLVGTLALLPPEERARVKGFIINKFRGDISLLEPGLDWLEELTGVPVLGVLPYLDDLRLPAEDSLall 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221 238 -FDDGASGSGLRIAIVAYPRLSNLDEFQPLRALPGLRLSWARSPAELAGADWIILPGSKAVAADLAWLREQKLDLAIAAH 316
Cdd:PRK00784  242 eRAARAGGGALRIAVIRLPRISNFTDFDPLRAEPGVDVRYVRPGEPLPDADLVILPGSKNTIADLAWLRESGWDEAIRAH 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221 317 AAAGRPVLGICGGLQMLGEALLDPHQLDGNA---PGLGLLPLVTQFEREKLLRPTRMRFAqrldapwagLADVAAEGYEI 393
Cdd:PRK00784  322 ARRGGPVLGICGGYQMLGRRIADPDGVEGAPgsvEGLGLLDVETVFEPEKTLRQVTGLLL---------GSGAPVSGYEI 392

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221 394 HHGRTAqhpALPLASVALRDERGEAIGW--QQGPVLGHYVHGLFEQPAVLQALFGQSG--------------QSLDQVFD 457
Cdd:PRK00784  393 HMGRTT---GPALARPFLRLDDGRPDGAvsADGRVFGTYLHGLFDNDAFRRALLNWLGarkglapasaldyaALREAQLD 469

                         490
                  ....*....|....*....
gi 1934963221 458 GLADYVDTHFRPGTLLSLI 476
Cdd:PRK00784  470 RLADLVEEHLDLDALLALL 488
cobQ TIGR00313
cobyric acid synthase CobQ; [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, ...
 1-466 4.57e-131

cobyric acid synthase CobQ; [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 129413 [Multi-domain]  Cd Length: 475  Bit Score: 388.00  E-value: 4.57e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221   1 MVLGTTSGAGKSFLATALCRWYADQGLKVAPFKAQNMSNNARVvpglAGQMGEIGSAQYFQALAARRVPEVRMNPVLLKP 80
Cdd:TIGR00313   2 MVVGTTSSAGKSTLTAGLCRILARRGYRVAPFKSQNMSLNSFV----TKEGGEIAIAQATQALAAGIEPSVHMNPILLKP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221  81 EADTKSQVVVLGEVHPELNATPWR-ERSEKLWPHARAALHELLAENELVVIEGAGSPAEINLHSSDYVNMRTAREANAAC 159
Cdd:TIGR00313  78 KGNFTSQVIVHGRAVGDMNYQEYYkNKVDFFLKAIKESLEILAREYDYVVIEGAGSPAEINLLKRDLANMRIAELANADA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221 160 LLATDIDRGGAFAHLYGTHQLLPPEERALIRGFVLNRFRGDARLLAPGPEQLQALTGVPTLATLPMWRGHgLPEEDG--V 237
Cdd:TIGR00313 158 ILVADIDRGGVFASIYGTLKLLPENWRKLIKGIVINKFRGNVDVLKSGIEKLEELTGIPVLGVLPYDENL-FPEEDSlvI 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221 238 FDDGASGSG--LRIAIVAYPRLSNLDEFQPLRALPGLRLSWARSpaELAGADWIILPGSKAVAADLAWLREQKLDLAIAA 315
Cdd:TIGR00313 237 QERRSRGNAksIRIGVVRLPRISNFTDFEPLRYEAFVKFLDLDD--SLTGCDAVIIPGSKSTIADLYALKQSGFAEEILD 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221 316 HAAAGRPVLGICGGLQMLGEALLDPHQLD---GNAPGLGLLPLVTQFEREKLLRPTRmrfaQRLDAPWAGLadvAAEGYE 392
Cdd:TIGR00313 315 FAKEGGIVIGICGGYQMLGKELIDKEKKEsdvGDIEGLGLLDAKTYFGEDKITKQSQ----GRVEGNNRGE---TVKGYE 387

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221 393 IHHGRTaQHPALPLasvaLRDERGEAIGwQQGPVLGHYVHGLFEQPA-------VLQALFGQSGQSLDQVF-------DG 458
Cdd:TIGR00313 388 IHEGFT-RSKEKPL----FKIERFGNCG-NDGNAWGTYLHGLFENYEfrryiinLLRKRKGPLEIYGGNYKdqrekslDY 461


                  ....*...
gi 1934963221 459 LADYVDTH 466
Cdd:TIGR00313 462 LADVVERS 469
CobQ_N cd05389
N-terminal domain of cobyric acid synthase; Cobyric acid synthase (CobQ, CbiP) N-terminal ...
 1-224 4.04e-113

N-terminal domain of cobyric acid synthase; Cobyric acid synthase (CobQ, CbiP) N-terminal domain. CobQ plays a role in the cobalamin (vitamin B12) biosynthesis pathway. CobQ catalyzes the ATP-dependent amidation of adenosyl-cobyrinic acid a,c-diamide at carboxylates positions b, d, e, and g to produce cobyric acid using glutamine or ammonia as the nitrogen source. The C-terminal glutaminase domain catalyzes the hydrolysis of glutamine to glutamate and ammonia. Ammonia is translocated via an intramolecular tunnel to the N-terminal domain for the synthesis of cobyric acid.


Pssm-ID: 349774  Cd Length: 223  Bit Score: 332.63  E-value: 4.04e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221   1 MVLGTTSGAGKSFLATALCRWYADQGLKVAPFKAQNMSNNARVVPGlaGqmGEIGSAQYFQALAARRVPEVRMNPVLLKP 80
Cdd:cd05389     4 MVQGTASDVGKSTLVAALCRILKRRGYRVAPFKAQNMSLNSFVTKD--G--GEIGRAQAVQAEAAGVEPSVDMNPVLLKP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221  81 EADTKSQVVVLGEVHPELNATPWRERSEKLWPHARAALHELLAENELVVIEGAGSPAEINLHSSDYVNMRTAREANAACL 160
Cdd:cd05389    80 KGDFKSQVIVMGKPIGDMDAREYYEYKGRLAPAVLESLDRLAAEYDLVVIEGAGSPAEINLRDRDIVNMGMARAADAPVI 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1934963221 161 LATDIDRGGAFAHLYGTHQLLPPEERALIRGFVLNRFRGDARLLAPGPEQLQALTGVPTLATLP 224
Cdd:cd05389   160 LVADIDRGGVFASLYGTLALLPEEERKLVKGVVINKFRGDRSLLEPGIEMLEERTGVPVLGVLP 223
GATase_3 pfam07685
CobB/CobQ-like glutamine amidotransferase domain;
248-439 2.05e-43

CobB/CobQ-like glutamine amidotransferase domain;


Pssm-ID: 429595 [Multi-domain]  Cd Length: 189  Bit Score: 151.62  E-value: 2.05e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221 248 RIAIVAYPRLSN--LDEFQPLRALPGLRLSWARSPAE--LAGADWIILPGSKAVAADLAWLREQKLDLAIAAHAAAGRPV 323
Cdd:pfam07685   1 RIAVIRLPRISNytDDNLDPLRYEPAVRVRFVPLPDEslGPDADLIILPGGKPTIQDLALLRNSGMDEAIKEAAEDGGPV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221 324 LGICGGLQMLGEALLDPHQLDgnAPGLGLLPLVTQFEREKLLRPTRMRfaqrldapwAGLADVAAEGYEIHHGRT-AQHP 402
Cdd:pfam07685  81 LGICGGYQMLGETIEDPEGVR--IEGLGLLDIETVFQKEKLTGQVVGY---------LLLEGETVRGYEIHYGRTiLGDG 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1934963221 403 ALPLASVALRDER---GEAIGWQQGPVLGHYVHGLFEQPA 439
Cdd:pfam07685 150 AKPLGRVKVGGGNngeDGKDGAVSGNVFGTYLHGHFLNRN 189
 
Name Accession Description Interval E-value
CobQ COG1492
Cobyric acid synthase [Coenzyme transport and metabolism]; Cobyric acid synthase is part of ...
 1-477 0e+00

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: 653.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221   1 MVLGTTSGAGKSFLATALCRWYADQGLKVAPFKAQNMSNNARVVP-GlagqmGEIGSAQYFQALAARRVPEVRMNPVLLK 79
Cdd:COG1492     6 MVQGTTSDAGKSLLVAALCRILARRGYRVAPFKAQNMSLNSAVTAdG-----GEIGRAQALQAEAAGVEPSVDMNPVLLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221  80 PEADTKSQVVVLGEVHPELNATPWRERSEKLWPHARAALHELLAENELVVIEGAGSPAEINLHSSDYVNMRTAREANAAC 159
Cdd:COG1492    81 PEGDTGSQVIVQGKPVGNMSARDYYEYKPRLLEAVLESLDRLAAEYDLVVIEGAGSPAEINLRDRDIANMGFAEAADAPV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221 160 LLATDIDRGGAFAHLYGTHQLLPPEERALIRGFVLNRFRGDARLLAPGPEQLQALTGVPTLATLPMWRGHGLPEEDGVFD 239
Cdd:COG1492   161 ILVGDIDRGGVFASLVGTLALLPEEERARVKGFIINKFRGDPSLLEPGLDWLEERTGVPVLGVLPYLEDLRLPAEDSLAL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221 240 D----GASGSGLRIAIVAYPRLSNLDEFQPLRALPGLRLSWARSPAELAGADWIILPGSKAVAADLAWLREQKLDLAIAA 315
Cdd:COG1492   241 EsrrgSKGGGRLRIAVIRLPRISNFTDFDPLAAEPGVRLRYVRPPEELGDADLVILPGSKNTIADLAWLRESGLDDAIRA 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221 316 HAAAGRPVLGICGGLQMLGEALLDPHQLDGNA---PGLGLLPLVTQFEREKLLRPTRMRFAqrldapwAGLADVAAEGYE 392
Cdd:COG1492   321 HARRGGPVLGICGGYQMLGRRIADPDGVEGGAgevPGLGLLPVETVFAPEKTLRQVTGTLL-------GPLSGAPVSGYE 393

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221 393 IHHGRTAQHP-ALPLASVALRDERGeAIgWQQGPVLGHYVHGLFEQPAVLQALFGQ----------------SGQSLDQV 455
Cdd:COG1492   394 IHMGRTTGPDgARPLLRRDGREPDG-AV-SADGRVWGTYLHGLFDNDAFRRALLNAlrekkglsplaagavdYAARREAA 471

                         490       500
                  ....*....|....*....|..
gi 1934963221 456 FDGLADYVDTHFRPGTLLSLIR 477
Cdd:COG1492   472 LDRLADHVEEHLDLDALLALLG 493
PRK00784 PRK00784
cobyric acid synthase;
1-476 0e+00

cobyric acid synthase;


Pssm-ID: 234838 [Multi-domain]  Cd Length: 488  Bit Score: 578.58  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221   1 MVLGTTSGAGKSFLATALCRWYADQGLKVAPFKAQNMSNNARVVPGlaGqmGEIGSAQYFQALAARRVPEVRMNPVLLKP 80
Cdd:PRK00784    6 MVQGTASDAGKSTLVAGLCRILARRGYRVAPFKAQNMSLNSAVTAD--G--GEIGRAQALQAEAAGVEPSVDMNPVLLKP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221  81 EADTKSQVVVLGEVHPELNATPWRERSEKLWPHARAALHELLAENELVVIEGAGSPAEINLHSSDYVNMRTAREANAACL 160
Cdd:PRK00784   82 QSDRGSQVIVQGKPVGNMDARDYHDYKPRLLEAVLESLDRLAAEYDVVVVEGAGSPAEINLRDRDIANMGFAEAADAPVI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221 161 LATDIDRGGAFAHLYGTHQLLPPEERALIRGFVLNRFRGDARLLAPGPEQLQALTGVPTLATLPMWRGHGLPEEDGV--- 237
Cdd:PRK00784  162 LVADIDRGGVFASLVGTLALLPPEERARVKGFIINKFRGDISLLEPGLDWLEELTGVPVLGVLPYLDDLRLPAEDSLall 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221 238 -FDDGASGSGLRIAIVAYPRLSNLDEFQPLRALPGLRLSWARSPAELAGADWIILPGSKAVAADLAWLREQKLDLAIAAH 316
Cdd:PRK00784  242 eRAARAGGGALRIAVIRLPRISNFTDFDPLRAEPGVDVRYVRPGEPLPDADLVILPGSKNTIADLAWLRESGWDEAIRAH 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221 317 AAAGRPVLGICGGLQMLGEALLDPHQLDGNA---PGLGLLPLVTQFEREKLLRPTRMRFAqrldapwagLADVAAEGYEI 393
Cdd:PRK00784  322 ARRGGPVLGICGGYQMLGRRIADPDGVEGAPgsvEGLGLLDVETVFEPEKTLRQVTGLLL---------GSGAPVSGYEI 392

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221 394 HHGRTAqhpALPLASVALRDERGEAIGW--QQGPVLGHYVHGLFEQPAVLQALFGQSG--------------QSLDQVFD 457
Cdd:PRK00784  393 HMGRTT---GPALARPFLRLDDGRPDGAvsADGRVFGTYLHGLFDNDAFRRALLNWLGarkglapasaldyaALREAQLD 469

                         490
                  ....*....|....*....
gi 1934963221 458 GLADYVDTHFRPGTLLSLI 476
Cdd:PRK00784  470 RLADLVEEHLDLDALLALL 488
cobQ TIGR00313
cobyric acid synthase CobQ; [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, ...
 1-466 4.57e-131

cobyric acid synthase CobQ; [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 129413 [Multi-domain]  Cd Length: 475  Bit Score: 388.00  E-value: 4.57e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221   1 MVLGTTSGAGKSFLATALCRWYADQGLKVAPFKAQNMSNNARVvpglAGQMGEIGSAQYFQALAARRVPEVRMNPVLLKP 80
Cdd:TIGR00313   2 MVVGTTSSAGKSTLTAGLCRILARRGYRVAPFKSQNMSLNSFV----TKEGGEIAIAQATQALAAGIEPSVHMNPILLKP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221  81 EADTKSQVVVLGEVHPELNATPWR-ERSEKLWPHARAALHELLAENELVVIEGAGSPAEINLHSSDYVNMRTAREANAAC 159
Cdd:TIGR00313  78 KGNFTSQVIVHGRAVGDMNYQEYYkNKVDFFLKAIKESLEILAREYDYVVIEGAGSPAEINLLKRDLANMRIAELANADA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221 160 LLATDIDRGGAFAHLYGTHQLLPPEERALIRGFVLNRFRGDARLLAPGPEQLQALTGVPTLATLPMWRGHgLPEEDG--V 237
Cdd:TIGR00313 158 ILVADIDRGGVFASIYGTLKLLPENWRKLIKGIVINKFRGNVDVLKSGIEKLEELTGIPVLGVLPYDENL-FPEEDSlvI 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221 238 FDDGASGSG--LRIAIVAYPRLSNLDEFQPLRALPGLRLSWARSpaELAGADWIILPGSKAVAADLAWLREQKLDLAIAA 315
Cdd:TIGR00313 237 QERRSRGNAksIRIGVVRLPRISNFTDFEPLRYEAFVKFLDLDD--SLTGCDAVIIPGSKSTIADLYALKQSGFAEEILD 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221 316 HAAAGRPVLGICGGLQMLGEALLDPHQLD---GNAPGLGLLPLVTQFEREKLLRPTRmrfaQRLDAPWAGLadvAAEGYE 392
Cdd:TIGR00313 315 FAKEGGIVIGICGGYQMLGKELIDKEKKEsdvGDIEGLGLLDAKTYFGEDKITKQSQ----GRVEGNNRGE---TVKGYE 387

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221 393 IHHGRTaQHPALPLasvaLRDERGEAIGwQQGPVLGHYVHGLFEQPA-------VLQALFGQSGQSLDQVF-------DG 458
Cdd:TIGR00313 388 IHEGFT-RSKEKPL----FKIERFGNCG-NDGNAWGTYLHGLFENYEfrryiinLLRKRKGPLEIYGGNYKdqrekslDY 461


                  ....*...
gi 1934963221 459 LADYVDTH 466
Cdd:TIGR00313 462 LADVVERS 469
CobQ_N cd05389
N-terminal domain of cobyric acid synthase; Cobyric acid synthase (CobQ, CbiP) N-terminal ...
 1-224 4.04e-113

N-terminal domain of cobyric acid synthase; Cobyric acid synthase (CobQ, CbiP) N-terminal domain. CobQ plays a role in the cobalamin (vitamin B12) biosynthesis pathway. CobQ catalyzes the ATP-dependent amidation of adenosyl-cobyrinic acid a,c-diamide at carboxylates positions b, d, e, and g to produce cobyric acid using glutamine or ammonia as the nitrogen source. The C-terminal glutaminase domain catalyzes the hydrolysis of glutamine to glutamate and ammonia. Ammonia is translocated via an intramolecular tunnel to the N-terminal domain for the synthesis of cobyric acid.


Pssm-ID: 349774  Cd Length: 223  Bit Score: 332.63  E-value: 4.04e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221   1 MVLGTTSGAGKSFLATALCRWYADQGLKVAPFKAQNMSNNARVVPGlaGqmGEIGSAQYFQALAARRVPEVRMNPVLLKP 80
Cdd:cd05389     4 MVQGTASDVGKSTLVAALCRILKRRGYRVAPFKAQNMSLNSFVTKD--G--GEIGRAQAVQAEAAGVEPSVDMNPVLLKP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221  81 EADTKSQVVVLGEVHPELNATPWRERSEKLWPHARAALHELLAENELVVIEGAGSPAEINLHSSDYVNMRTAREANAACL 160
Cdd:cd05389    80 KGDFKSQVIVMGKPIGDMDAREYYEYKGRLAPAVLESLDRLAAEYDLVVIEGAGSPAEINLRDRDIVNMGMARAADAPVI 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1934963221 161 LATDIDRGGAFAHLYGTHQLLPPEERALIRGFVLNRFRGDARLLAPGPEQLQALTGVPTLATLP 224
Cdd:cd05389   160 LVADIDRGGVFASLYGTLALLPEEERKLVKGVVINKFRGDRSLLEPGIEMLEERTGVPVLGVLP 223
GATase1_CobQ cd01750
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type ...
 249-445 1.68e-55

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: 183.60  E-value: 1.68e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221 249 IAIVAYPRLSNLDEFQPLRALPGLRLSWARSPAELAGADWIILPGSKAVAADLAWLREQKLDLAIAAHAAAGRPVLGICG 328
Cdd:cd01750     1 IAVIRYPDISNFTDLDPLAREPGVDVRYVEVPEGLGDADLIILPGSKDTIQDLAWLRKRGLAEAIKNYARAGGPVLGICG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221 329 GLQMLGEALLDPHQL--DGNAPGLGLLPLVTQFEREKLLRPTRMRFAQRLDapwaglaDVAAEGYEIHHGRTAQHP-ALP 405
Cdd:cd01750    81 GYQMLGKYIVDPEGVegPGEIEGLGLLDVETEFGPEKTTRRVTGRLDEEGE-------GGEVTGYEIHSGRTTLGDgARP 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1934963221 406 LASVALRDERGEAIGWQQG-PVLGHYVHGLFEQPAVLQALF 445
Cdd:cd01750   154 LGKGYGNNGEDGTDGAVSGdNVIGTYLHGIFLNDAFRDALL 194
GATase_3 pfam07685
CobB/CobQ-like glutamine amidotransferase domain;
248-439 2.05e-43

CobB/CobQ-like glutamine amidotransferase domain;


Pssm-ID: 429595 [Multi-domain]  Cd Length: 189  Bit Score: 151.62  E-value: 2.05e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221 248 RIAIVAYPRLSN--LDEFQPLRALPGLRLSWARSPAE--LAGADWIILPGSKAVAADLAWLREQKLDLAIAAHAAAGRPV 323
Cdd:pfam07685   1 RIAVIRLPRISNytDDNLDPLRYEPAVRVRFVPLPDEslGPDADLIILPGGKPTIQDLALLRNSGMDEAIKEAAEDGGPV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221 324 LGICGGLQMLGEALLDPHQLDgnAPGLGLLPLVTQFEREKLLRPTRMRfaqrldapwAGLADVAAEGYEIHHGRT-AQHP 402
Cdd:pfam07685  81 LGICGGYQMLGETIEDPEGVR--IEGLGLLDIETVFQKEKLTGQVVGY---------LLLEGETVRGYEIHYGRTiLGDG 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1934963221 403 ALPLASVALRDER---GEAIGWQQGPVLGHYVHGLFEQPA 439
Cdd:pfam07685 150 AKPLGRVKVGGGNngeDGKDGAVSGNVFGTYLHGHFLNRN 189
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 1-224 3.87e-35

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: 130.54  E-value: 3.87e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221   1 MVLGTTSGAGKSFLATALCRWYADQGLKVAPFKAQNMSNNARVvpglAGQMGEIgsAQYFQALAARRVPEVRMNPVLLKP 80
Cdd:pfam01656   2 AIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSV----EGLEGDI--APALQALAEGLKGRVNLDPILLKE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221  81 EADTKSQVVVLGevHPELNATPWRERSEKLWPHARAALHELLAENELVVIEGAGSPAEiNLHSSDYVNMRTAREANAACL 160
Cdd:pfam01656  76 KSDEGGLDLIPG--NIDLEKFEKELLGPRKEERLREALEALKEDYDYVIIDGAPGLGE-LLRNALIAADYVIIPLEPEVI 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1934963221 161 LATDIDR-GGAFAHLYGTHQLLppeeRALIRGFVLNRFRGDA--RLLAPGPEQLqaLTGVPTLATLP 224
Cdd:pfam01656 153 LVEDAKRlGGVIAALVGGYALL----GLKIIGVVLNKVDGDNhgKLLKEALEEL--LRGLPVLGVIP 213
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 277-364 1.03e-10

imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model represents the glutamine amidotransferase subunit (or domain, in eukaryotic systems) of imidazole glycerol phosphate synthase. This subunit catalyzes step 5 of histidine biosynthesis from PRPP. The other subunit, the cyclase, catalyzes step 6. [Amino acid biosynthesis, Histidine family]


Pssm-ID: 273836 [Multi-domain]  Cd Length: 196  Bit Score: 60.80  E-value: 1.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221 277 ARSPAELAGADWIILPGSKAVAADLAWLREQKLDLAIAAHAAAGRPVLGICGGLQMLGEAlldpHQLDGNAPGLGLLP-L 355
Cdd:TIGR01855  28 VKDSKEAELADKLILPGVGAFGAAMARLRENGLDLFVELVVRLGKPVLGICLGMQLLFER----SEEGGGVPGLGLIKgN 103


                  ....*....
gi 1934963221 356 VTQFEREKL 364
Cdd:TIGR01855 104 VVKLEARKV 112
hisH PRK13181
imidazole glycerol phosphate synthase subunit HisH; Provisional
 277-364 1.45e-10

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183878 [Multi-domain]  Cd Length: 199  Bit Score: 60.65  E-value: 1.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221 277 ARSPAELAGADWIILPGSKAVAADLAWLREQKLDLAIAAHAAAGRPVLGICGGLQMLGEalldpHQLDGNAPGLGLLPL- 355
Cdd:PRK13181   29 SSDPEEIAGADKVILPGVGAFGQAMRSLRESGLDEALKEHVEKKQPVLGICLGMQLLFE-----SSEEGNVKGLGLIPGd 103


                  ....*....
gi 1934963221 356 VTQFEREKL 364
Cdd:PRK13181  104 VKRFRSEPL 112
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
 278-354 2.14e-10

Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid transport and metabolism]; Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 439888 [Multi-domain]  Cd Length: 196  Bit Score: 60.05  E-value: 2.14e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1934963221 278 RSPAELAGADWIILPGSKAVAADLAWLREQKLDLAIAAHAAAGRPVLGICGGLQMLGEALLDphqlDGNAPGLGLLP 354
Cdd:COG0118    31 SDPDEIRAADRLVLPGVGAFGDAMENLRERGLDEAIREAVAGGKPVLGICLGMQLLFERSEE----NGDTEGLGLIP 103
hisH PRK13141
imidazole glycerol phosphate synthase subunit HisH; Provisional
 278-354 6.15e-10

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 58.99  E-value: 6.15e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1934963221 278 RSPAELAGADWIILPGSKAVAADLAWLREQKLDLAIAAHAAAGRPVLGICGGLQMLGEALLDphqlDGNAPGLGLLP 354
Cdd:PRK13141   30 SDPEEILAADGVILPGVGAFPDAMANLRERGLDEVIKEAVASGKPLLGICLGMQLLFESSEE----FGETEGLGLLP 102
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 276-354 1.45e-09

Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS); Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS). IGPS incorporates ammonia derived from glutamine into N1-[(5'-phosphoribulosyl)-formimino]-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to form 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR) and imidazole glycerol phosphate (IGP). The glutamine amidotransferase domain generates the ammonia nucleophile which is channeled from the glutaminase active site to the PRFAR active site. IGPS belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153219 [Multi-domain]  Cd Length: 198  Bit Score: 57.51  E-value: 1.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221 276 WARSPAELAGADWIILPGSKAVAADLAWLREQKLDLAIAAHAAAGRPVLGICGGLQMLGEalldpHQL-DGNAPGLGLLP 354
Cdd:cd01748    27 ITSDPEEILSADKLILPGVGAFGDAMANLRERGLIEALKEAIASGKPFLGICLGMQLLFE-----SSEeGGGTKGLGLIP 101
PRK01077 PRK01077
cobyrinate a,c-diamide synthase;
232-447 4.28e-09

cobyrinate a,c-diamide synthase;


Pssm-ID: 234896 [Multi-domain]  Cd Length: 451  Bit Score: 58.61  E-value: 4.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221 232 PEEDGVFDDGASGSGLRIAiVA--------YPrlSNLDEfqpLRALpGLRLS-WarSP---AELAGADWIILPG------ 293
Cdd:PRK01077  231 PPPPAAAPPPPAPPGVRIA-VArdaafnfyYP--ENLEL---LRAA-GAELVfF--SPladEALPDCDGLYLGGgypelf 301

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221 294 SKAVAADLAWLREQKldlaiaAHAAAGRPVLGICGGLQMLGEALLDphqLDGN-APGLGLLPLVTQFEReKLLRpTRMRF 372
Cdd:PRK01077  302 AAELAANTSMRASIR------AAAAAGKPIYAECGGLMYLGESLED---ADGErHPMVGLLPGEASMTK-RLQA-LGYRE 370

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1934963221 373 AQRLDAPWAGLADVAAEGYEIHHGRTAQHPALPLASVALRDERGEAI-GWQQGPVLGHYVHGLF-EQPAVLQALFGQ 447
Cdd:PRK01077  371 AEALEDTLLGKAGERLRGHEFHYSTLETPEEAPLYRVRDADGRPLGEeGYRRGNVLASYLHLHFaSNPDAAARFLAA 447
PLN02617 PLN02617
imidazole glycerol phosphate synthase hisHF
 278-366 4.81e-08

imidazole glycerol phosphate synthase hisHF


Pssm-ID: 178226 [Multi-domain]  Cd Length: 538  Bit Score: 55.49  E-value: 4.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221 278 RSPAELAGADWIILPGSKAVAADLAWLREQKLDLAIAAHAAAGRPVLGICGGLQMlgeaLLDPHQLDGNAPGLGLLP-LV 356
Cdd:PLN02617   37 QTPEDILNADRLIFPGVGAFGSAMDVLNNRGMAEALREYIQNDRPFLGICLGLQL----LFESSEENGPVEGLGVIPgVV 112

                          90
                  ....*....|
gi 1934963221 357 TQFEREKLLR 366
Cdd:PLN02617  113 GRFDSSNGLR 122
hisH PRK13146
imidazole glycerol phosphate synthase subunit HisH; Provisional
 267-354 5.53e-07

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237290 [Multi-domain]  Cd Length: 209  Bit Score: 50.17  E-value: 5.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221 267 RALPGLRLSWARSPAELAGADWIILPGSKAVAADLAWLREQKL-DLAIAAHAAAGRPVLGICGGLQMLGEALLDPhqldG 345
Cdd:PRK13146   23 RAGAGADVVVTADPDAVAAADRVVLPGVGAFADCMRGLRAVGLgEAVIEAVLAAGRPFLGICVGMQLLFERGLEH----G 98


                  ....*....
gi 1934963221 346 NAPGLGLLP 354
Cdd:PRK13146   99 DTPGLGLIP 107
DTBS cd03109
dethiobiotin synthetase; Dethiobiotin synthetase (DTBS) is the penultimate enzyme in the ...
 1-202 9.65e-07

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: 49.10  E-value: 9.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221   1 MVLGTTSGAGKSFLATALCRWYADQGLKVAPFKaqnmsnnarvvPGLAGQMGEIGS-AQYFQALAARRVPEVRMNPVLLK 79
Cdd:cd03109     4 FVTGTDTDVGKTVVSAGLARALRKKGIKVGYLK-----------PVQTGCPGLEDSdAELLRKLAGLLLDLELINPYRFE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221  80 PEADtksqvvvlgevhPELNATpwRERSEKLWPHARAALHELLAENELVVIEGAG---SPAeinlhSSDYVNMRTAREAN 156
Cdd:cd03109    73 APLS------------PHLAAE--LEGRDIDLEEIVRALEELAKSYDVVLVEGAGgllVPL-----TEGYLNADLARALG 133

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1934963221 157 AACLLATDIdRGGAFAHLYGTHQLLppEERAL-IRGFVLNRFRGDAR 202
Cdd:cd03109   134 LPVILVARG-GLGTINHTLLTLEAL--KSRGLdVAGVVLNGIPPEPE 177
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 249-333 2.25e-06

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: 46.44  E-value: 2.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221 249 IAIVAYPRLSNLDEFQPLRAL--PGLRLSWAR-------SPAELAGADWIILPGSKAVAADLAWLREQKLDLAIAAHAaa 319
Cdd:cd01653     1 VAVLLFPGFEELELASPLDALreAGAEVDVVSpdggpveSDVDLDDYDGLILPGGPGTPDDLARDEALLALLREAAAA-- 78

                          90
                  ....*....|....
gi 1934963221 320 GRPVLGICGGLQML 333
Cdd:cd01653    79 GKPILGICLGAQLL 92
COG3442 COG3442
Glutamine amidotransferase related to the GATase domain of CobQ [General function prediction ...
 320-409 3.37e-06

Glutamine amidotransferase related to the GATase domain of CobQ [General function prediction only];


Pssm-ID: 442666 [Multi-domain]  Cd Length: 241  Bit Score: 48.25  E-value: 3.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221 320 GRPVLGICGGLQMLGEALLDPhqlDGN-APGLGLLPLVTqferekLLRPTRMrfaqrldapwagLADVAAE--------- 389
Cdd:COG3442    85 GVPVLAICGGYQLLGHYYETA---DGErIPGLGILDVYT------VAGKKRL------------IGNVVVEtelngefgt 143

                          90       100
                  ....*....|....*....|...
gi 1934963221 390 --GYEIHHGRTAQHPAL-PLASV 409
Cdd:COG3442   144 lvGFENHSGRTYLGPGVkPLGRV 166
hisH PRK13143
imidazole glycerol phosphate synthase subunit HisH; Provisional
 279-354 4.28e-06

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237289 [Multi-domain]  Cd Length: 200  Bit Score: 47.56  E-value: 4.28e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1934963221 279 SPAELAGADWIILPGSKA---VAADLAWLREQKLDLAIAahaaaGRPVLGICGGLQMlgeaLLDPHQLDGNAPGLGLLP 354
Cdd:PRK13143   32 DPEEILDADGIVLPGVGAfgaAMENLSPLRDVILEAARS-----GKPFLGICLGMQL----LFESSEEGGGVRGLGLFP 101
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 249-333 1.62e-05

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: 43.34  E-value: 1.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221 249 IAIVAYPRLSNLDEFQPLRAL--PGLRLSWAR-------SPAELAGADWIILPGSKAVAADLAWLREQKLDLAIAAHAaa 319
Cdd:cd03128     1 VAVLLFGGSEELELASPLDALreAGAEVDVVSpdggpveSDVDLDDYDGLILPGGPGTPDDLAWDEALLALLREAAAA-- 78

                          90
                  ....*....|....
gi 1934963221 320 GRPVLGICGGLQML 333
Cdd:cd03128    79 GKPVLGICLGAQLL 92
AAA_26 pfam13500
AAA domain; This domain is found in a number of proteins involved in cofactor biosynthesis ...
 1-225 3.21e-05

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: 44.94  E-value: 3.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221   1 MVLGTTSGAGKSFLATALCRWYADQGLKVAPFKAqnmsnnarVVPGLAGQMGEIGSAQYFQALAARRVPE-VRMNPVLLK 79
Cdd:pfam13500   4 FVTGTDTGVGKTVVSLGLARALKRRGVKVGYWKP--------VQTGLVEDGDSELVKRLLGLDQSYEDPEpFRLSAPLSP 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221  80 PEADTKSQVVVLgevhpelnatpwrerSEKLWPharaalhELLAENELVVIEGAG---SPAeinlhSSDYVNMRTAREAN 156
Cdd:pfam13500  76 HLAARQEGVTID---------------LEKIIY-------ELPADADPVVVEGAGgllVPI-----NEDLLNADIAANLG 128

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221 157 AACLLATDIDRgGAFAHLYGTHQLLppEERAL-IRGFVLNRFRGDArllapGPEQLQALTGVPTLATLPM 225
Cdd:pfam13500 129 LPVILVARGGL-GTINHTLLTLEAL--RQRGIpVLGVILNGVPNPE-----NVRTIFAFGGVPVLGAVPY 190
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 283-337 2.82e-04

GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP synthase, glutamine amidotransferase domain is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440284 [Multi-domain]  Cd Length: 225  Bit Score: 42.24  E-value: 2.82e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1934963221 283 LAGADWIILPGSKA-VAADLAWL-REQKLDlaiAAHAAAGRPVLGICGGLQMLGEAL 337
Cdd:COG0518    46 LEDPDGLILSGGPMsVYDEDPWLeDEPALI---REAFELGKPVLGICYGAQLLAHAL 99
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 1-81 2.89e-04

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: 40.11  E-value: 2.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221   1 MVLGTTSGAGKSFLATALCRWYADQGLKVAPFKAQNmsnnaRVVPGLAGQMGEIGSAQYFQALAARRVPEVRMnpVLLKP 80
Cdd:cd01983     4 AVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLDD-----YVLIDGGGGLETGLLLGTIVALLALKKADEVI--VVVDP 76


                  .
gi 1934963221  81 E 81
Cdd:cd01983    77 E 77
GATase1_CobB cd03130
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyrinic Acid a,c-Diamide ...
 320-445 5.79e-04

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: 41.04  E-value: 5.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221 320 GRPVLGICGGLQMLGEALLDPHqlDGNAPGLGLLPLVTqfEREKLLRPTRMRfAQRLDAPWAGLADVAAEGYEIHHGR-- 397
Cdd:cd03130    75 GGPIYAECGGLMYLGESLDDEE--GQSYPMAGVLPGDA--RMTKRLGLGYRE-AEALGDTLLGKKGTTLRGHEFHYSRle 149

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1934963221 398 TAQHPALPLASVALRDERGEAIGWQQGPVLGHYVHGLF-EQPAVLQALF 445
Cdd:cd03130   150 PPPEPDFAATVRRGRGIDGGEDGYVYGNVLASYLHLHWaSNPDLAERFV 198
CobB_N cd05388
N-terminal domain of cobyrinic acid a,c-diamide synthase; Cobyrinic acid a,c-diamide synthase ...
 1-33 5.82e-04

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: 41.05  E-value: 5.82e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1934963221   1 MVLGTTSGAGKSFLATALCRWYADQGLKVAPFK 33
Cdd:cd05388     4 VIAGTSSGSGKTTITLGLMRALARRGLRVQPFK 36
hisH PRK13170
imidazole glycerol phosphate synthase subunit HisH; Provisional
 278-354 1.73e-03

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183877 [Multi-domain]  Cd Length: 196  Bit Score: 39.45  E-value: 1.73e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1934963221 278 RSPAELAGADWIILPGSKAVAADLAWLREQKL-DLAIAAHaaagRPVLGICGGLQMLGEAlldpHQLDGNAPGLGLLP 354
Cdd:PRK13170   31 RDPDVILAADKLFLPGVGTAQAAMDQLRERELiDLIKACT----QPVLGICLGMQLLGER----SEESGGVDCLGIID 100
hisH PRK13152
imidazole glycerol phosphate synthase subunit HisH; Provisional
 249-360 3.76e-03

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 171876 [Multi-domain]  Cd Length: 201  Bit Score: 38.67  E-value: 3.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221 249 IAIVAYpRLSNLDEFQPLRALPGLRLSWARSPAELAGADWIILPGSKAVAADLAWLREQKLD-LAIAAHAAAGRPVLGIC 327
Cdd:PRK13152    2 IALIDY-KAGNLNSVAKAFEKIGAINFIAKNPKDLQKADKLLLPGVGSFKEAMKNLKELGFIeALKEQVLVQKKPILGIC 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1934963221 328 GGLQMLGEALLDphqlDGNAPGLGLLP-LVTQFE 360
Cdd:PRK13152   81 LGMQLFLERGYE----GGVCEGLGFIEgEVVKFE 110
hisH CHL00188
imidazole glycerol phosphate synthase subunit hisH; Provisional
 278-362 4.01e-03

imidazole glycerol phosphate synthase subunit hisH; Provisional


Pssm-ID: 214389 [Multi-domain]  Cd Length: 210  Bit Score: 38.71  E-value: 4.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221 278 RSPAELAGADWIILPGSKAVaaDLAWLREQKLDLAIAAHA--AAGRPVLGICGGLQMLGEAlldphQLDGNAPGLGLLP- 354
Cdd:CHL00188   32 NSESELAQVHALVLPGVGSF--DLAMKKLEKKGLITPIKKwiAEGNPFIGICLGLHLLFET-----SEEGKEEGLGIYKg 104


                  ....*...
gi 1934963221 355 LVTQFERE 362
Cdd:CHL00188  105 QVKRLKHS 112
PRK03619 PRK03619
phosphoribosylformylglycinamidine synthase subunit PurQ;
248-354 6.79e-03

phosphoribosylformylglycinamidine synthase subunit PurQ;


Pssm-ID: 235140 [Multi-domain]  Cd Length: 219  Bit Score: 38.17  E-value: 6.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934963221 248 RIAIVAYPRlSN--LDEFQPLRALPGL--RLSWARSpAELAGADWIILPG---------SKAVAA---------DLAwlr 305
Cdd:PRK03619    2 KVAVIVFPG-SNcdRDMARALRDLLGAepEYVWHKE-TDLDGVDAVVLPGgfsygdylrCGAIAAfspimkavkEFA--- 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1934963221 306 eqkldlaiaahaAAGRPVLGICGGLQMLGEAlldphqldgnapglGLLP 354
Cdd:PRK03619   77 ------------EKGKPVLGICNGFQILTEA--------------GLLP 99
 
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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