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UniProtKB/Swiss-Prot entry P26692

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

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Entry information
Entry name ACDA_METSO
Primary accession number P26692
Secondary accession numbers None
Integrated into Swiss-Prot on August 1, 1992
Sequence was last modified on August 1, 1992 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 58)
Name and origin of the protein
Protein name Acetyl-CoA decarbonylase/synthase complex subunit alpha
Synonyms ACDS complex subunit alpha
EC 1.2.99.2
ACDS complex carbon monoxide dehydrogenase
ACDS CODH
Gene name
Name: cdhA
From
Methanothrix soehngenii [TaxID: 2223] 
Taxonomy Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales; Methanosaetaceae; Methanosaeta.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
STRAIN=Opfikon / DSM 2139;
PubMed=1901858 [NCBI, ExPASy, EBI, Israel, Japan]
Eggen R.I.L., Geerling A.C.M., Jetten M.S.M., de Vos W.M.;
"Cloning, expression, and sequence analysis of the genes for carbon monoxide dehydrogenase of Methanothrix soehngenii.";
J. Biol. Chem. 266:6883-6887(1991).
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.
  • CAUTION: This protein lacks the conserved Cys in positions 52 and 56; they are replaced by an Asp and a Thr, respectively. It is therefore possible that the C- and D-clusters are either altered or missing in this protein, which may not form heterotetramers.
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
M55280; AAA72934.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A39764; A39764.
3D structure databases
ModBase P26692.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0051539; Molecular function: 4 iron, 4 sulfur cluster binding (inferred from electronic annotation from InterPro).
GO:0018492; Molecular function: carbon-monoxide dehydrogenase (acceptor) activity (inferred from electronic annotation from HAMAP).
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0016151; Molecular function: nickel ion binding (inferred from electronic annotation from InterPro).
GO:0006084; Biological process: acetyl-CoA metabolic process (inferred from electronic annotation from InterPro).
GO:0006091; Biological process: generation of precursor metabolites and energy (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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.
TIGRFAMs TIGR00314; cdhA; 1.
PROSITE PS00198; 4FE4S_FER_1; 2.
PS51379; 4FE4S_FER_2; 2.
PROSITE graphical view of domain structure (profiles).
ProtoNet P26692.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
4Fe-4S; Direct protein sequencing; 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   793  793     Acetyl-CoA decarbonylase/synthase complex subunit alpha. PRO_0000155082
DOMAIN   393   422  30     4Fe-4S ferredoxin-type 1. 
DOMAIN   432   461  30     4Fe-4S ferredoxin-type 2. 
METAL   55    55        Iron-sulfur 1 (4Fe-4S); shared with dimeric partner (By similarity). 
METAL   58    58        Iron-sulfur 2 (4Fe-4S) (By similarity). 
METAL   63    63        Iron-sulfur 2 (4Fe-4S) (By similarity). 
METAL   73    73        Iron-sulfur 2 (4Fe-4S) (By similarity). 
METAL   229   229        Nickel-iron-sulfur (By similarity). 
METAL   257   257        Nickel-iron-sulfur (By similarity). 
METAL   309   309        Nickel-iron-sulfur (By similarity). 
METAL   403   403        Iron-sulfur 3 (4Fe-4S) (Potential). 
METAL   406   406        Iron-sulfur 3 (4Fe-4S) (Potential). 
METAL   409   409        Iron-sulfur 3 (4Fe-4S) (Potential). 
METAL   413   413        Iron-sulfur 3 (4Fe-4S) (Potential). 
METAL   441   441        Iron-sulfur 4 (4Fe-4S) (Potential). 
METAL   444   444        Iron-sulfur 4 (4Fe-4S) (Potential). 
METAL   447   447        Iron-sulfur 4 (4Fe-4S) (Potential). 
METAL   451   451        Iron-sulfur 4 (4Fe-4S) (Potential). 
METAL   509   509        Nickel-iron-sulfur (By similarity). 
METAL   538   538        Nickel-iron-sulfur (By similarity). 
METAL   573   573        Nickel-iron-sulfur (By similarity). 
Sequence information
Length: 793 AA [This is the length of the unprocessed precursor] Molecular weight: 88152 Da [This is the MW of the unprocessed precursor] CRC64: 7CBCB187B1860A2B [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MKNVQINIGA VVKEEDEWDQ EMGPFPKPGV ATLRDWDFKI CNRYKIMYSP ADDTCTLCTY 

        70         80         90        100        110        120 
GPCDLTGNKK GACGIDMAAA CGKIVLVAVL MGTCAHTAHG RHLYHWCLDK FGDMPFDMGS 

       130        140        150        160        170        180 
EILVDAPLYR TILGKKPKSL KDFGEALEYC EEEIVQLLAA CHTGQEGHYM DFESKSLHSG 

       190        200        210        220        230        240 
MIDSLGKEIC DMLQTVAYDM PRGAADAPLV EIGMGTLDQN KGVLIAYGHN LAAGAEAMIY 

       250        260        270        280        290        300 
TEEHNLWDKV DIGGVCCTAI DLTRITETGR ESKIPANLGP KAKVAGAMGW WRKMVRAGIM 

       310        320        330        340        350        360 
DTVIVDEQCV FCDVLEDCQQ RHIPVIASND KIMLGLPDRT NDSADAIVED LVSFKMPGVA 

       370        380        390        400        410        420 
ILDPVKAGEV AIRTAVAVKP KREQYKKESL FTEQQFKDTL ATCTECNQCA FVCPPHIRIS 

       430        440        450        460        470        480 
EMISEALKGN LEPFSSTYEV CVGCQRCEQT CPQEIPILKL YEYANREYIR NQKFKMRAGR 

       490        500        510        520        530        540 
GPVLDTEIRK VGAPLVLGQI PGVIALVGCS NYPNGTKECY DIAKEFVDRG YIVVATGCMA 

       550        560        570        580        590        600 
MDMSLYKDED GKTIWEQYEG AFDGRNICNI GSCVANAHIH GAAIKVATIF AHRNERANYD 

       610        620        630        640        650        660 
DIADYIMSKV GACGVAWGAY SQKAASIATG VNRIGIPVVV QPSSVIYRRT FMGRTDKPED 

       670        680        690        700        710        720 
WMVIDAKNGN MQQIEPAPEA MLYIAETKEE AMLEMAKLCF RPSDNTQGRG IKLTHYCDIS 

       730        740        750        760        770        780 
MKYFGKLPDD WHLFVRDVKD LPLNYQTQMM KELEEKHGWK IDWKAKKFIS GPLRPADVSF 

       790 
DPTNIPRKIR AKK
P26692 in FASTA format

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