Acetyl-CoA decarbonylase/synthase complex subunit alpha 1

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Reviewed, UniProtKB/Swiss-Prot O29165 (ACDA1_ARCFU)

Last modified February 9, 2010. Version 63. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Acetyl-CoA decarbonylase/synthase complex subunit alpha 1
      Short name=ACDS complex subunit alpha 1
    EC=1.2.99.2
Alternative name(s):
    ACDS complex carbon monoxide dehydrogenase 1
      Short name=ACDS CODH 1

Gene names

Name:	cdhA1
Ordered Locus Names:	AF_1100

Organism

Archaeoglobus fulgidus [Complete proteome] [HAMAP]

Taxonomic identifier

2234 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Archaeoglobi › Archaeoglobales › Archaeoglobaceae › Archaeoglobus

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Protein attributes

Sequence length	802 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

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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_01137
Catalytic activity	CO + H₂O + A = CO₂ + AH₂. HAMAP MF_01137
Cofactor	Binds 7 4Fe-4S clusters per heterotetramer Potential. HAMAP MF_01137 Binds 2 nickel-iron-sulfur clusters per heterotetramer Potential. HAMAP MF_01137
Subunit structure	Heterotetramer of two alpha and two epsilon chains. 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. HAMAP MF_01137
Domain	Cluster B is an all-cysteinyl-liganded 4Fe4S cluster; cluster C is a mixed Ni-Fe-S cluster which appears to be the active site of CO oxidation. Cluster D is also an all-cysteinyl-liganded 4Fe4S cluster that bridges the two subunits of the CODH dimer. May contain two additional 4Fe-4S clusters, dubbed E and F, that might reroute electron transfer along different paths. HAMAP MF_01137
Sequence similarities	Belongs to the Ni-containing carbon monoxide dehydrogenase family. Contains 2 4Fe-4S ferredoxin-type domains.
Caution	This protein lacks the conserved Cys in positions 65 and 69; they are replaced by a Gln and an Asn, respectively. It is therefore possible that the C- and D-clusters are either altered or missing in this protein, which may not form heterotetramers.

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Ontologies

Keywords
Domain	Repeat
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding Nickel
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	acetyl-CoA metabolic process Inferred from electronic annotation. Source: InterPro generation of precursor metabolites and energy Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW carbon-monoxide dehydrogenase (acceptor) activity Inferred from electronic annotation. Source: HAMAP electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW nickel ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 802

802

Acetyl-CoA decarbonylase/synthase complex subunit alpha 1 HAMAP MF_01137

PRO_0000155072

Regions

Domain

395 – 424

4Fe-4S ferredoxin-type 1

Domain

435 – 464

4Fe-4S ferredoxin-type 2

Sites

Metal binding

Iron-sulfur 1 (4Fe-4S); shared with dimeric partner By similarity

Metal binding

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

243

Nickel-iron-sulfur By similarity

Metal binding

271

Nickel-iron-sulfur By similarity

Metal binding

310

Nickel-iron-sulfur By similarity

Metal binding

405

Iron-sulfur 3 (4Fe-4S) Potential

Metal binding

408

Iron-sulfur 3 (4Fe-4S) Potential

Metal binding

411

Iron-sulfur 3 (4Fe-4S) Potential

Metal binding

415

Iron-sulfur 3 (4Fe-4S) Potential

Metal binding

444

Iron-sulfur 4 (4Fe-4S) Potential

Metal binding

447

Iron-sulfur 4 (4Fe-4S) Potential

Metal binding

450

Iron-sulfur 4 (4Fe-4S) Potential

Metal binding

454

Iron-sulfur 4 (4Fe-4S) Potential

Metal binding

512

Nickel-iron-sulfur By similarity

Metal binding

541

Nickel-iron-sulfur By similarity

Metal binding

576

Nickel-iron-sulfur By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

O29165-1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 81C626EDED06F66C
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FASTA

802

89,524

        10         20         30         40         50         60 
MFELKKGALF VDEMKNVSIR IGKVVEEEEE VWEEAGPTPK PGILELRKWD HKLLERYEPF 

        70         80         90        100        110        120 
YAPMQDFCNL CTMGPCDLSM NKRGACGIDL KTAKARLVTI ACCIGASAHT AHARHLVDHL 

       130        140        150        160        170        180 
IEEFGEDFPI DLGGDVNVEA PIIRTVVGIK PKTLGDLREA LNWAEKEIVK VLHSTHIGNE 

       190        200        210        220        230        240 
ESLLDYESKA MHVSMADHVG MEVADIAQIV AYNFPKAEPD TPLVDTGFGI VDKSKPTIVV 

       250        260        270        280        290        300 
VGHNVMYARP VADYLEEMGR IDDFELAGLC CTAHDMTRYN AKAKIFGPIS YQLRVIRAGI 

       310        320        330        340        350        360 
PDVMISDEQC IRADLLEACK KMGIPLIATS DAAARGLPDV SDWPVEKIVD ALVSGKLPGV 

       370        380        390        400        410        420 
FLPIPEKVGQ VAPLVAEAIF KKHGGERKYK FFESDEALME EINKCTQCMN CVFTCPHSLR 

       430        440        450        460        470        480 
VDQGMAHAQK TGDLSKLAQL EEQCLACMKC EQACPKNIKI INVIMRANYD RLYNKTGKTR 

       490        500        510        520        530        540 
VGRGPIQDTE IRKVGQPIVF GQIPGVIAAV GCINFPDEMK SIREILEEFL KRRYIVVTSG 

       550        560        570        580        590        600 
CHAMDIGMIK DEEGKTLYEK YPGNFDAGGL VNTGSCVANS HIAGAAIKIA NIFAMRPLRG 

       610        620        630        640        650        660 
NYAEIADYVL NRVGAVGFSW GPYSHKAASI ATGFNRLGVP VVVGPHGTKY RRAYIGKPWK 

       670        680        690        700        710        720 
KDKWWVYDIK SRQKVFIEPA PDSLLVAVET KEEAIVQLAR LCIRPNDTNQ GRQIKLTHYI 

       730        740        750        760        770        780 
ELHQKYYGDL PDDWAVYVRS EADLPLKMRD QLLKVLEEQY GWKIDWDKKK IVEGPVRHFD 

       790        800 
AGFNPTIVEE VYEKYAGEKA PR

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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.

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Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000782 Genomic DNA. Translation: AAB90136.1.
PIR	C69387.
RefSeq	NP_069929.1.
3D structure databases
SMR	O29165. Positions 34-791.
ModBase	Search...
Genome annotation databases
GeneID	1484322.
GenomeReviews	Gene locus AF_1100 in contig AE000782_GR.
KEGG	afu:AF1100.
NMPDR	fig\|224325.1.peg.1088.
TIGR	AF_1100.
Phylogenomic databases
HOGENOM	HBG539676.
Enzyme and pathway databases
BioCyc	AFUL224325:AF_1100-MONOMER.
BRENDA	1.2.99.2. 7576.
Family and domain databases
HAMAP	MF_01137. CdhA. [Tree]
InterPro	IPR017896. 4Fe4S_Fe-S-bd. IPR017900. 4Fe4S_Fe_S_CS. IPR004460. CO_DH/Ac-CoA_synth_asu. IPR016101. CO_DH_a-bundle. IPR012285. Fum_reductase_C. IPR009051. Helical_ferredxn. IPR004137. Prismane. IPR011254. Prismane-like. IPR016099. Prismane-like_a/b-sand. [Graphical view]
Gene3D	G3DSA:1.20.1270.30. CO_DH_a-bundle. 1 hit. G3DSA:1.10.1060.10. Fum_reductase_C. 1 hit. G3DSA:3.40.50.2030. Prismane-like_a/b-sand. 2 hits.
Pfam	PF03063. Prismane. 2 hits. [Graphical view]
TIGRFAMs	TIGR00314. cdhA. 1 hit.
PROSITE	PS00198. 4FE4S_FER_1. 2 hits. PS51379. 4FE4S_FER_2. 2 hits. [Graphical view]
ProtoNet	Search...

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Entry information

Entry name

ACDA1_ARCFU

Accession

Primary (citable) accession number: O29165

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 21, 2003
Last sequence update:	January 1, 1998
Last modified:	February 9, 2010
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents