Q58138
Gene name |
cooS (MJ0728) |
Protein name |
Carbon monoxide dehydrogenase |
Names |
CODH |
Species |
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) |
KEGG Pathway |
mja:MJ_0728 |
EC number |
1.2.7.4: With an iron-sulfur protein as acceptor |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q58138
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q58138-F1 | Predicted | AlphaFoldDB |
No variants for Q58138
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q58138 | |||||
No associated diseases with Q58138
No regional properties for Q58138
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q58138 | |||
Functions
| Description | ||
|---|---|---|
| EC Number | 1.2.7.4 | With an iron-sulfur protein as acceptor |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
6 GO annotations of molecular function
| Name | Definition |
|---|---|
| 4 iron, 4 sulfur cluster binding | Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands. |
| carbon-monoxide dehydrogenase (acceptor) activity | Catalysis of the reaction: CO + H2O + acceptor = CO2 + reduced acceptor. |
| carbon-monoxide dehydrogenase (ferredoxin) activity | Catalysis of the reaction: CO + H2O + oxidized ferredoxin = CO2 + reduced ferredoxin. |
| hydroxylamine reductase activity | Catalysis of the reaction: NH3 + H2O + acceptor = hydroxylamine + reduced acceptor. |
| nickel cation binding | Binding to a nickel (Ni) cation. |
| peroxidase activity | Catalysis of the reaction: a donor + a peroxide = an oxidized donor + 2 H2O. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| generation of precursor metabolites and energy | The chemical reactions and pathways resulting in the formation of precursor metabolites, substances from which energy is derived, and any process involved in the liberation of energy from these substances. |
| nitrogen compound metabolic process | The chemical reactions and pathways involving organic or inorganic compounds that contain nitrogen. |
| response to hydrogen peroxide | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a hydrogen peroxide (H2O2) stimulus. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MKNCIAAIPE | VKEMVEKAKL | KGIETPHTRF | PNQFPKCPYG | LKGVYCILCA | NGPCRITEKT |
| 70 | 80 | 90 | 100 | 110 | 120 |
| PYGVCGATAD | VIVARNLCRA | VAAGTSCYVH | CAENAARALL | SAGKGEGSYE | IRNEKKLKFL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| AKKLGFDANK | DAKQLAVEVA | EFILDDMYKP | RWEKSELVPK | LCPEKRLEVF | EKLDILPGGA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KGEIVDALTK | TSTNLNSNPM | DLLVHCLRLG | LHAGFTGLLM | TCWLNDILFG | SPKITVVENG |
| 250 | 260 | 270 | 280 | 290 | 300 |
| FSSVKPNNVN | IMITGHQHAL | IQPLCEAAME | EDLIKMAKEA | GADEIKIIGA | TCNGQDMETR |
| 310 | 320 | 330 | 340 | 350 | 360 |
| IAHLPESFVG | YIANNFTTEP | LVATGLIDAV | VSEFNCTFHG | LKFVAEKTKT | KLICIDDMAY |
| 370 | 380 | 390 | 400 | 410 | 420 |
| VEGAEYIPWE | PENAKEKARE | IIKKAIEAFK | ERKGMQKDYY | DEKVKSVVGV | GEESLVEFLG |
| 430 | 440 | 450 | 460 | 470 | 480 |
| GSVKPLIELI | ASGKIKGVVG | VVGCSNLASG | GHDNIIVTLT | KELIKRDILV | LAGGCVNSPL |
| 490 | 500 | 510 | 520 | 530 | 540 |
| KHAGLFDPAS | AELAGENLKE | VCKSLGIPPV | LNFGACLSIA | RIEQVAVAIA | EELGVDIPDL |
| 550 | 560 | 570 | 580 | 590 | 600 |
| PVAASAPQWL | EEQALADATY | AVDMGFTVHV | SPVPFVTGSE | LVTKVLTEAV | EGLTGGKLIP |
| 610 | 620 | ||||
| EPNPYKAADL | LEQTIMEKRK | KLGI |