Acetyl-CoA decarbonylase/synthase complex subunit alpha 1

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Reviewed, UniProtKB/Swiss-Prot Q8TXF7 (ACDA1_METKA)

Last modified February 9, 2010. Version 51. 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:	MK0717

Organism

Methanopyrus kandleri [Complete proteome] [HAMAP]

Taxonomic identifier

2320 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanopyri › Methanopyrales › Methanopyraceae › Methanopyrus

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Protein attributes

Sequence length	760 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.

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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 – 760

760

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

PRO_0000155078

Regions

Domain

381 – 410

4Fe-4S ferredoxin-type 1

Domain

418 – 450

4Fe-4S ferredoxin-type 2

Sites

Metal binding

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

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

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

Metal binding

231

Nickel-iron-sulfur By similarity

Metal binding

259

Nickel-iron-sulfur By similarity

Metal binding

298

Nickel-iron-sulfur By similarity

Metal binding

390

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

Metal binding

393

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

Metal binding

396

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

Metal binding

400

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

Metal binding

428

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

Metal binding

431

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

Metal binding

434

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

Metal binding

438

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

Metal binding

496

Nickel-iron-sulfur By similarity

Metal binding

525

Nickel-iron-sulfur By similarity

Metal binding

560

Nickel-iron-sulfur By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

Q8TXF7-1 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: E82B0EF7D4163CAA
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FASTA

760

84,637

        10         20         30         40         50         60 
MSPFELEFEG LKVQIGSIEG FEPRGEGPLP CPTVSDLADW DRKLFARYRV IAFPICDMCC 

        70         80         90        100        110        120 
MCTYGRCNLA EGRRGACGID IRSNTARFTA LKTCIGAACH AAHARHLVEY ILEKLGDVEI 

       130        140        150        160        170        180 
DLGSEVDVMT PIFETLVGFK PKTVSDLEKG LEYIERELTK VLSSVHVGQE MDPHDYESKA 

       190        200        210        220        230        240 
LHAGMIDNLA LEIADVAQIA AFDMPKGEAP LVEFGPFAAD DSKPCILLVG HNVAPGTEVL 

       250        260        270        280        290        300 
DYLEERGLDE EVEVLGICCT AWDVSRVDDR SKVIGPLSRQ LHYVRMGIAD VVVLDEQCIR 

       310        320        330        340        350        360 
ADIVEEANEV GSRVIATRDL VMAGLPDVTD EPTEKIIEKM VSGEWMGVFI EDLEKAAEVA 

       370        380        390        400        410        420 
VEVAIRVHER RKKEIPQPDP KKLQKEAKRC LGCGDCERVC PNDLPIVEAM ERAANGDFEG 

       430        440        450        460        470        480 
LADLFDRCVG CARCESECPT KLRVMNMIED AWRLRTKEEK YKVRTGRGPI KDVEIRQVGG 

       490        500        510        520        530        540 
PIVMGDIPGV VAFVACPNYP DDVKQVGKMV EELLERNYIV LTSGCTAMAL GMYTDEDGKT 

       550        560        570        580        590        600 
LYEKYEDRFD AGCLVNTGSC VSNAHILGAC IKIAAIFAKK PLKGNFKEIA DYILNRIGAC 

       610        620        630        640        650        660 
GVLWGTMSQK ALAISTGFTR WGIPIVYGPA GLKYQTLYIG DLDGDWTVYD ARTGKECKEY 

       670        680        690        700        710        720 
CPIHLKYAAE DWREALVQAV KLCIRPNDTP QGRQTKLQNY IELYKEFYNE LPPDLPLYVR 

       730        740        750        760 
DKNDVPITLR DEVMEYLEEV GWKPRKGITE PTLLEENVRG

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References

[1]

"The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens."
Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N., Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A., Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G., Koonin E.V., Kozyavkin S.A.
Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002) [PubMed: 11930014] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AV19 / DSM 6324 / JCM 9639 / NBRC 100938.

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Cross-references

Sequence databases
EMBL GenBank DDBJ	AE009439 Genomic DNA. Translation: AAM01931.1.
RefSeq	NP_614001.1.
3D structure databases
SMR	Q8TXF7. Positions 26-755.
ModBase	Search...
Genome annotation databases
GeneID	1476818.
GenomeReviews	Gene locus MK0717 in contig AE009439_GR.
KEGG	mka:MK0717.
NMPDR	fig\|190192.1.peg.714.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG539676.
OMA	ICCTAID.
Enzyme and pathway databases
BioCyc	MKAN190192:MK0717-MONOMER.
BRENDA	1.2.99.2. 7577.
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. 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: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_METKA

Accession

Primary (citable) accession number: Q8TXF7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 21, 2003
Last sequence update:	June 1, 2002
Last modified:	February 9, 2010
This is version 51 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

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents