O29868 (ACDB_ARCFU) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 70.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Acetyl-CoA decarbonylase/synthase complex subunit beta Short name=ACDS complex subunit beta EC=2.3.1.- Alternative name(s): ACDS complex acyltransferase | ||||
| Gene names |
| ||||
| Organism | Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126) | ||||
| Taxonomic identifier | 224325 [NCBI] | ||||
| Taxonomic lineage | Archaea › Euryarchaeota › Archaeoglobi › Archaeoglobales › Archaeoglobaceae › Archaeoglobus |
Protein attributes
| Sequence length | 524 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO2 By similarity. HAMAP MF_01138 |
| Catalytic activity | Acetyl-CoA + [acetyl-CoA decarbonylase/synthase complex beta subunit] = CoA + acetyl-[acetyl-CoA decarbonylase/synthase complex beta subunit]. HAMAP MF_01138 |
| Cofactor | Binds 1 nickel-iron-sulfur cluster By similarity. HAMAP MF_01138 |
| Subunit structure | Monomer. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta chains with a probable stoichiometry of (alpha2epsilon2)(4)-beta(8)-(gamma1delta1)8 Potential. |
| Sequence similarities | Belongs to the CdhC family. |
Ontologies
| Keywords | |
|---|---|
| Ligand | Iron Iron-sulfur Metal-binding Nickel |
| Molecular function | Acyltransferase Transferase |
| Technical term | Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological process | acetyl-CoA metabolic process Inferred from electronic annotation. Source: InterPro |
| Molecular function | carbon-monoxide dehydrogenase (acceptor) activity Inferred from electronic annotation. Source: InterPro iron-sulfur cluster bindingInferred from electronic annotation. Source: UniProtKB-KW metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW transferase activity, transferring acyl groupsInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Ref.2 | ||||||
| Chain | 2 – 524 | 523 | Acetyl-CoA decarbonylase/synthase complex subunit beta HAMAP MF_01138 | PRO_0000155098 | |||||
Regions | |||||||||
| Compositional bias | 438 – 450 | 13 | Glu-rich HAMAP MF_01138 | ||||||
Sites | |||||||||
| Metal binding | 212 | 1 | Nickel-iron-sulfur Potential | ||||||
| Metal binding | 215 | 1 | Nickel-iron-sulfur Potential | ||||||
| Metal binding | 301 | 1 | Nickel-iron-sulfur Potential | ||||||
| Metal binding | 303 | 1 | Nickel-iron-sulfur Potential | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus." Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G. Venter J.C.Nature 390:364-370(1997) [PubMed: 9389475] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126. |
| [2] | "Acetyl-CoA decarbonylase/synthase complex from Archaeoglobus fulgidus." Dai Y.R., Reed D.W., Millstein J.H., Hartzell P.L., Grahame D.A., DeMoll E. Arch. Microbiol. 169:525-529(1998) [PubMed: 9575239] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-23. Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE000782 Genomic DNA. Translation: AAB90857.1. |
| PIR | C69297. |
| RefSeq | NP_069215.1. NC_000917.1. |
3D structure databases | |
| ProteinModelPortal | O29868. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 1483594. |
| GenomeReviews | Gene locus AF_0379 in contig AE000782_GR. |
| KEGG | afu:AF0379. |
| NMPDR | fig|224325.1.peg.374. |
| TIGR | AF_0379. |
Phylogenomic databases | |
| HOGENOM | HBG456963. |
| OMA | CPHTSCG. |
| ProtClustDB | PRK04456. |
Enzyme and pathway databases | |
| BioCyc | AFUL224325:AF_0379-MONOMER. |
Family and domain databases | |
| HAMAP | MF_01138. CdhC. [Tree] |
| InterPro | IPR004461. CO_DH/Ac-CoA_synth_bsu. IPR023432. CO_DH/Ac-CoA_synth_bsu_arc. IPR011254. Prismane-like. [Graphical view] |
| KO | K00193. |
| Pfam | PF03598. CdhC. 1 hit. [Graphical view] |
| SUPFAM | SSF56821. Prismane_like. 1 hit. |
| TIGRFAMs | TIGR00316. CdhC. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | ACDB_ARCFU | ||||||||
| Accession | Primary (citable) accession number: O29868 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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