Ontology | Accession | Term | GO Evidence | Evidence Ontology (ECO) Code | Reference | Comments |
---|---|---|---|---|---|---|
Molecular Function | GO:0003824 | catalytic activity |
Inferred from Sequence Model
Term mapped from: InterPro:TIGR00313
|
ECO:0000259 match to InterPro signature evidence used in automatic assertion |
||
Biological Process | GO:0009236 | cobalamin biosynthetic process |
Inferred from Sequence Model
Term mapped from: InterPro:TIGR00313
|
ECO:0000259 match to InterPro signature evidence used in automatic assertion |
|
Analysis | Accession | Description | Interpro Accession | Interpro Description | Amino Acid Start | Amino Acid Stop | E-value |
---|---|---|---|---|---|---|---|
NCBIfam | TIGR00313 | JCVI: cobyric acid synthase CobQ | IPR004459 | Cobyric acid synthase CobQ | 4 | 474 | 0.0 |
CDD | cd05389 | CobQ_N | IPR047045 | Cobyric acid synthase, N-terminal domain | 2 | 224 | 0.0 |
Hamap | MF_00028 | Cobyric acid synthase [cobQ]. | IPR004459 | Cobyric acid synthase CobQ | 1 | 483 | 214.078125 |
Gene3D | G3DSA:3.40.50.880 | - | IPR029062 | Class I glutamine amidotransferase-like | 255 | 393 | 1.0E-15 |
Gene3D | G3DSA:3.40.50.300 | - | IPR027417 | P-loop containing nucleoside triphosphate hydrolase | 2 | 237 | 8.6E-62 |
Pfam | PF07685 | CobB/CobQ-like glutamine amidotransferase domain | IPR011698 | CobB/CobQ-like glutamine amidotransferase | 250 | 433 | 3.0E-56 |
Pfam | PF13500 | AAA domain | - | - | 3 | 230 | 7.8E-22 |
CDD | cd01750 | GATase1_CobQ | IPR033949 | Cobyric acid synthase, glutamine amidotransferase type 1 | 251 | 440 | 4.53056E-69 |
SUPERFAMILY | SSF52317 | Class I glutamine amidotransferase-like | IPR029062 | Class I glutamine amidotransferase-like | 251 | 443 | 3.64E-40 |
SUPERFAMILY | SSF52540 | P-loop containing nucleoside triphosphate hydrolases | IPR027417 | P-loop containing nucleoside triphosphate hydrolase | 1 | 237 | 2.51E-60 |
PANTHER | PTHR21343 | DETHIOBIOTIN SYNTHETASE | - | - | 1 | 482 | 0.0 |