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UniProtKB/Swiss-Prot entry Q8TXF7

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ACDA1_METKA
Primary accession number Q8TXF7
Secondary accession numbers None
Integrated into Swiss-Prot on November 21, 2003
Sequence was last modified on June 1, 2002 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 38)
Name and origin of the protein
Protein name Acetyl-CoA decarbonylase/synthase complex subunit alpha 1
Synonyms ACDS complex subunit alpha 1
EC 1.2.99.2
ACDS complex carbon monoxide dehydrogenase 1
ACDS CODH 1
Gene name
Name: cdhA1
OrderedLocusNames: MK0717
From
Methanopyrus kandleri [TaxID: 2320] [HAMAP proteome]
Taxonomy Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae; Methanopyrus.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
DOI=10.1073/pnas.032671499; PubMed=11930014 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.";
Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
Comments
  • FUNCTION: Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing autotrophic growth from CO(2) (By similarity).
  • CATALYTIC ACTIVITY: CO + H2O + A = CO2 + AH2.
  • COFACTOR: Binds 7 4Fe-4S clusters per heterotetramer (Potential).
  • COFACTOR: Binds 2 nickel-iron-sulfur clusters per heterotetramer (Potential).
  • SUBUNIT: 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 (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8) (Potential).
  • 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.
  • SIMILARITY: Belongs to the Ni-containing carbon monoxide dehydrogenase family.
  • SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AE010365; AAM01931.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_614001.1; -.
3D structure databases
HSSP P00214; 1G6B. [HSSP ENTRY / PDB]
ModBase Q8TXF7.
Enzyme and pathway databases
BioCyc MKAN190192:MK0717-MON; -.
Ontologies
GO
GO:0018492; Molecular function: carbon-monoxide dehydrogenase (acceptor) activity (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_01137; -; 1.
PBIL [Tree]
InterPro IPR001450; 4Fe4S_Fe_S_bd.
IPR004460; CO_DHase/Ac-CoA_synth_asu.
IPR016101; CO_DHase_a-bundle.
IPR004137; Prismane.
IPR016099; Prismane-like_a/b-sand.
Graphical view of domain structure.
Gene3D G3DSA:1.20.1270.30; CO_DH_a-bundle; 1.
G3DSA:3.40.50.2030; Prismane-like_a/b-sand; 2.
Pfam PF00037; Fer4; 2.
PF03063; Prismane; 1.
Pfam graphical view of domain structure.
PRINTS PR00353; 4FE4SFRDOXIN.
TIGRFAMs TIGR00314; cdhA; 1.
PROSITE PS00198; 4FE4S_FER_1; 2.
PS51379; 4FE4S_FER_2; 2.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q8TXF7.
Genome annotation databases
GeneID 1476818; -.
GenomeReviews AE009439_GR; MK0717.
KEGG mka:MK0717; -.
NMPDR fig|190192.1.peg.714; -.
Phylogenomic databases
HOGENOM Q8TXF7; -.
Genome annotation databases
CMR Q8TXF7; MK0717.
Other
ProtoNet Q8TXF7.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; Nickel; Oxidoreductase; Repeat.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   760  760     Acetyl-CoA decarbonylase/synthase complex subunit alpha 1. PRO_0000155078
DOMAIN   381   410  30     4Fe-4S ferredoxin-type 1. 
DOMAIN   418   450  33     4Fe-4S ferredoxin-type 2. 
METAL   56    56        Iron-sulfur 1 (4Fe-4S); shared with dimeric partner (By similarity). 
METAL   59    59        Iron-sulfur 1 (4Fe-4S); shared with dimeric partner (By similarity). 
METAL   60    60        Iron-sulfur 2 (4Fe-4S) (By similarity). 
METAL   62    62        Iron-sulfur 2 (4Fe-4S) (By similarity). 
METAL   67    67        Iron-sulfur 2 (4Fe-4S) (By similarity). 
METAL   77    77        Iron-sulfur 2 (4Fe-4S) (By similarity). 
METAL   231   231        Nickel-iron-sulfur (By similarity). 
METAL   259   259        Nickel-iron-sulfur (By similarity). 
METAL   298   298        Nickel-iron-sulfur (By similarity). 
METAL   390   390        Iron-sulfur 3 (4Fe-4S) (Potential). 
METAL   393   393        Iron-sulfur 3 (4Fe-4S) (Potential). 
METAL   396   396        Iron-sulfur 3 (4Fe-4S) (Potential). 
METAL   400   400        Iron-sulfur 3 (4Fe-4S) (Potential). 
METAL   428   428        Iron-sulfur 4 (4Fe-4S) (Potential). 
METAL   431   431        Iron-sulfur 4 (4Fe-4S) (Potential). 
METAL   434   434        Iron-sulfur 4 (4Fe-4S) (Potential). 
METAL   438   438        Iron-sulfur 4 (4Fe-4S) (Potential). 
METAL   496   496        Nickel-iron-sulfur (By similarity). 
METAL   525   525        Nickel-iron-sulfur (By similarity). 
METAL   560   560        Nickel-iron-sulfur (By similarity). 
Sequence information
Length: 760 AA [This is the length of the unprocessed precursor] Molecular weight: 84637 Da [This is the MW of the unprocessed precursor] CRC64: E82B0EF7D4163CAA [This is a checksum on the sequence] 
        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
Q8TXF7 in FASTA format

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