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Database: UniProt
Entry: O27743
LinkDB: O27743
Original site: O27743 
ID   ACDA_METTH              Reviewed;         780 AA.
AC   O27743;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   10-APR-2019, entry version 127.
DE   RecName: Full=Acetyl-CoA decarbonylase/synthase complex subunit alpha {ECO:0000255|HAMAP-Rule:MF_01137};
DE            Short=ACDS complex subunit alpha {ECO:0000255|HAMAP-Rule:MF_01137};
DE            EC=1.2.7.4 {ECO:0000255|HAMAP-Rule:MF_01137};
DE   AltName: Full=ACDS complex carbon monoxide dehydrogenase subunit alpha {ECO:0000255|HAMAP-Rule:MF_01137};
DE            Short=ACDS CODH subunit alpha {ECO:0000255|HAMAP-Rule:MF_01137};
GN   Name=cdhA {ECO:0000255|HAMAP-Rule:MF_01137};
GN   OrderedLocusNames=MTH_1708;
OS   Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 /
OS   JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium
OS   thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=187420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA   Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA   Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K.,
RA   Harrison D., Hoang L., Keagle P., Lumm W., Pothier B., Qiu D.,
RA   Spadafora R., Vicare R., Wang Y., Wierzbowski J., Gibson R.,
RA   Jiwani N., Caruso A., Bush D., Safer H., Patwell D., Prabhakar S.,
RA   McDougall S., Shimer G., Goyal A., Pietrovski S., Church G.M.,
RA   Daniels C.J., Mao J.-I., Rice P., Noelling J., Reeve J.N.;
RT   "Complete genome sequence of Methanobacterium thermoautotrophicum
RT   deltaH: functional analysis and comparative genomics.";
RL   J. Bacteriol. 179:7135-7155(1997).
CC   -!- FUNCTION: Part of the ACDS complex that catalyzes the reversible
CC       cleavage of acetyl-CoA, allowing autotrophic growth from CO(2).
CC       The alpha-epsilon subcomponent functions as a carbon monoxide
CC       dehydrogenase. {ECO:0000255|HAMAP-Rule:MF_01137}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CO + H2O + 2 oxidized [2Fe-2S]-[ferredoxin] = CO2 + 2
CC         H(+) + 2 reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:21040,
CC         Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:17245,
CC         ChEBI:CHEBI:33737, ChEBI:CHEBI:33738; EC=1.2.7.4;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01137};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01137};
CC       Note=Binds 7 [4Fe-4S] clusters per heterotetramer.
CC       {ECO:0000255|HAMAP-Rule:MF_01137};
CC   -!- COFACTOR:
CC       Name=[Ni-4Fe-4S] cluster; Xref=ChEBI:CHEBI:47739;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01137};
CC       Note=Binds 2 [Ni-4Fe-4S] clusters per heterotetramer.
CC       {ECO:0000255|HAMAP-Rule:MF_01137};
CC   -!- SUBUNIT: Heterotetramer of two alpha and two epsilon subunits. The
CC       ACDS complex is made up of alpha, epsilon, beta, gamma and delta
CC       subunits with a probable stoichiometry of (alpha(2)epsilon(2))(4)-
CC       beta(8)-(gamma(1)delta(1))(8). {ECO:0000255|HAMAP-Rule:MF_01137}.
CC   -!- DOMAIN: Cluster B is an all-cysteinyl-liganded 4Fe-4S cluster;
CC       cluster C is a mixed Ni-Fe-S cluster which is the active site of
CC       CO oxidation. Cluster D is also an all-cysteinyl-liganded 4Fe-4S
CC       cluster that bridges the two subunits of the CODH dimer. Contains
CC       two additional 4Fe-4S clusters, dubbed E and F, that probably
CC       transport electrons from ferredoxin to the B cluster.
CC       {ECO:0000255|HAMAP-Rule:MF_01137}.
CC   -!- SIMILARITY: Belongs to the Ni-containing carbon monoxide
CC       dehydrogenase family. {ECO:0000255|HAMAP-Rule:MF_01137}.
DR   EMBL; AE000666; AAB86180.1; -; Genomic_DNA.
DR   PIR; E69095; E69095.
DR   ProteinModelPortal; O27743; -.
DR   SMR; O27743; -.
DR   IntAct; O27743; 2.
DR   PRIDE; O27743; -.
DR   EnsemblBacteria; AAB86180; AAB86180; MTH_1708.
DR   KEGG; mth:MTH_1708; -.
DR   PATRIC; fig|187420.15.peg.1669; -.
DR   eggNOG; arCOG02428; Archaea.
DR   eggNOG; COG1152; LUCA.
DR   KO; K00192; -.
DR   OMA; EVCGICC; -.
DR   Proteomes; UP000005223; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0018492; F:carbon-monoxide dehydrogenase (acceptor) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0043885; F:carbon-monoxide dehydrogenase (ferredoxin) activity; IEA:UniProtKB-EC.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016151; F:nickel cation binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006084; P:acetyl-CoA metabolic process; IEA:InterPro.
DR   CDD; cd01916; ACS_1; 1.
DR   Gene3D; 1.10.1060.10; -; 1.
DR   Gene3D; 3.40.50.2030; -; 2.
DR   HAMAP; MF_01137; CdhA; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR004460; CDHA.
DR   InterPro; IPR004137; HCP/CODH.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   InterPro; IPR016099; Prismane-like_a/b-sand.
DR   InterPro; IPR011254; Prismane-like_sf.
DR   PANTHER; PTHR30109; PTHR30109; 1.
DR   Pfam; PF13187; Fer4_9; 1.
DR   Pfam; PF03063; Prismane; 2.
DR   SUPFAM; SSF46548; SSF46548; 1.
DR   SUPFAM; SSF56821; SSF56821; 1.
DR   TIGRFAMs; TIGR00314; cdhA; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   3: Inferred from homology;
KW   4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; Nickel;
KW   Oxidoreductase; Reference proteome; Repeat.
FT   CHAIN         1    780       Acetyl-CoA decarbonylase/synthase complex
FT                                subunit alpha.
FT                                /FTId=PRO_0000155085.
FT   DOMAIN      399    429       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   DOMAIN      440    469       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL        73     73       Iron-sulfur 1 (4Fe-4S); shared with
FT                                dimeric partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_01137}.
FT   METAL        76     76       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL        77     77       Iron-sulfur 1 (4Fe-4S); shared with
FT                                dimeric partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_01137}.
FT   METAL        79     79       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL        84     84       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL        93     93       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       250    250       Nickel-iron-sulfur (Ni-4Fe-4S); via tele
FT                                nitrogen. {ECO:0000255|HAMAP-
FT                                Rule:MF_01137}.
FT   METAL       278    278       Nickel-iron-sulfur (Ni-4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       317    317       Nickel-iron-sulfur (Ni-4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       409    409       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       412    412       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       415    415       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       419    419       Iron-sulfur 4 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       449    449       Iron-sulfur 4 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       452    452       Iron-sulfur 4 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       455    455       Iron-sulfur 4 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       459    459       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       517    517       Nickel-iron-sulfur (Ni-4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       546    546       Nickel-iron-sulfur (Ni-4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       581    581       Nickel-iron-sulfur (Ni-4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   BINDING     116    116       Carbon monoxide; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
SQ   SEQUENCE   780 AA;  86068 MW;  98AB06D10C300685 CRC64;
     MIDVAPESKK AKDLKGDFWD AKNIQISIGE IITEEKPPEE EVKGPKPRPH VTDLRSWDMK
     LLERYEPFYA PFCDMCCLCT YGKCELLGKK GACGIDAATQ QARTVLLACL IGTAAHAGHA
     RHLVDHLIER LGEDYKIDLG SNVDIEAPIT RTVMGKRPAT LGDLREVMDY AEEQMSHLLS
     ACHTGQEGDS KDFESKAFHA GLMDDLTREV ADLAQIVALD LPKGDEDAPL VELGFGTIDT
     EKPVVLCIGH NVLPGADIVD YLDENEMEDQ VEVCGICCAA IDVTRYNEAA KVVGPLSKQL
     RFIRSGVADV IVVDEQCVRT DVLEEALKNR SAVIATTDKM CLGLPDMTDE DPDKIVNDLI
     NGNIEGALIL DPEKVGEVAV KTAMKLAPIR KSLKKLPDID EIIELASECT DCGWCQRVCP
     NSLPVMDAVK KAADGDLSKL EEMAIEELCY TCGRCEQECE RNIPIVSMVT KAGERRVKDE
     KYRIRAGRGP AQDVEIRRVG APIVLGDIPG VVAFVGCSNY PEGGKDVALM AKEFLERNYI
     VVTTGCGAMS IGEYRDEDGQ TLYEKYGGQF DAKGLVNMGS CVSNAHVSGA AIKIANIFAQ
     KPLEGNFEEI ADYILNRVGA CGVAWGAYSQ KAAAIATGVN RWGIPVVLGP HGSKYRRLFL
     GRADDEEKWK LKDLRTGEVI DGEPAPEHLL YAAENREEAT VMIAKLCIRP TDTPKGRQMK
     LSNYIDLHRK YLGTIPDDID RFIRTEKDIP IVYKRDVMKI LEEKNWKPRE LPKEPSLLER
//
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