P27988
Gene name |
|
Protein name |
Carbon monoxide dehydrogenase/acetyl-CoA synthase subunit alpha |
Names |
ACS subunit, Acetyl-CoA synthase subunit, CODH/ACS |
Species |
Moorella thermoacetica (Clostridium thermoaceticum) |
KEGG Pathway |
|
EC number |
2.3.1.169: Transferring groups other than amino-acyl groups |
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
11 structures for P27988
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 1MJG | X-ray | 220 A | M/N/O/P | 1-729 | PDB |
| 1OAO | X-ray | 190 A | C/D | 1-729 | PDB |
| 2Z8Y | X-ray | 251 A | M/N/O/P | 1-729 | PDB |
| 3GIT | X-ray | 300 A | A/B/C/D/E/F | 311-729 | PDB |
| 3I01 | X-ray | 215 A | M/N/O/P | 1-729 | PDB |
| 3I04 | X-ray | 215 A | M/N/O/P | 2-729 | PDB |
| 3S2X | X-ray | 235 A | A/B | 594-729 | PDB |
| 5GOL | X-ray | 211 A | A/B/C/D | 594-728 | PDB |
| 5H6W | X-ray | 220 A | A/B/C/D | 594-728 | PDB |
| 6X5K | X-ray | 247 A | M/N/O/P | 1-729 | PDB |
| AF-P27988-F1 | Predicted | AlphaFoldDB |
No variants for P27988
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P27988 | |||||
No associated diseases with P27988
Functions
| Description | ||
|---|---|---|
| EC Number | 2.3.1.169 | Transferring groups other than amino-acyl groups |
| 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 |
4 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. |
| CO-methylating acetyl-CoA synthase activity | Catalysis of the reaction: acetyl-CoA + corrinoid protein = CO + methylcorrinoid protein + CoA. |
| metal ion binding | Binding to a metal ion. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| acetyl-CoA metabolic process | The chemical reactions and pathways involving acetyl-CoA, a derivative of coenzyme A in which the sulfhydryl group is acetylated; it is a metabolite derived from several pathways (e.g. glycolysis, fatty acid oxidation, amino-acid catabolism) and is further metabolized by the tricarboxylic acid cycle. It is a key intermediate in lipid and terpenoid biosynthesis. |
| carbon fixation | A metabolic process in which carbon (usually derived from carbon dioxide) is incorporated into organic compounds (usually carbohydrates). |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTDFDKIFEG | AIPEGKEPVA | LFREVYHGAI | TATSYAEILL | NQAIRTYGPD | HPVGYPDTAY |
| 70 | 80 | 90 | 100 | 110 | 120 |
| YLPVIRCFSG | EEVKKLGDLP | PILNRKRAQV | SPVLNFENAR | LAGEATWYAA | EIIEALRYLK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| YKPDEPLLPP | PWTGFIGDPV | VRRFGIKMVD | WTIPGEAIIL | GRAKDSKALA | KIVKELMGMG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| FMLFICDEAV | EQLLEENVKL | GIDYIAYPLG | NFTQIVHAAN | YALRAGMMFG | GVTPGAREEQ |
| 250 | 260 | 270 | 280 | 290 | 300 |
| RDYQRRRIRA | FVLYLGEHDM | VKTAAAFGAI | FTGFPVITDQ | PLPEDKQIPD | WFFSVEDYDK |
| 310 | 320 | 330 | 340 | 350 | 360 |
| IVQIAMETRG | IKLTKIKLDL | PINFGPAFEG | ESIRKGDMYV | EMGGNRTPAF | ELVRTVSESE |
| 370 | 380 | 390 | 400 | 410 | 420 |
| ITDGKIEVIG | PDIDQIPEGS | KLPLGILVDI | YGRKMQADFE | GVLERRIHDF | INYGEGLWHT |
| 430 | 440 | 450 | 460 | 470 | 480 |
| GQRNINWLRV | SKDAVAKGFR | FKNYGEILVA | KMKEEFPAIV | DRVQVTIFTD | EAKVKEYMEV |
| 490 | 500 | 510 | 520 | 530 | 540 |
| AREKYKERDD | RMRGLTDETV | DTFYSCVLCQ | SFAPNHVCIV | TPERVGLCGA | VSWLDAKASY |
| 550 | 560 | 570 | 580 | 590 | 600 |
| EINHAGPNQP | IPKEGEIDPI | KGIWKSVNDY | LYTASNRNLE | QVCLYTLMEN | PMTSCGCFEA |
| 610 | 620 | 630 | 640 | 650 | 660 |
| IMAILPECNG | IMITTRDHAG | MTPSGMTFST | LAGMIGGGTQ | TPGFMGIGRT | YIVSKKFISA |
| 670 | 680 | 690 | 700 | 710 | 720 |
| DGGIARIVWM | PKSLKDFLHD | EFVRRSVEEG | LGEDFIDKIA | DETIGTTVDE | ILPYLEEKGH |
| PALTMDPIM |