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Database: UniProt
Entry: Q8TXF7
LinkDB: Q8TXF7
Original site: Q8TXF7 
ID   ACDA1_METKA             Reviewed;         760 AA.
AC   Q8TXF7;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   10-APR-2019, entry version 100.
DE   RecName: Full=Acetyl-CoA decarbonylase/synthase complex subunit alpha 1 {ECO:0000255|HAMAP-Rule:MF_01137};
DE            Short=ACDS complex subunit alpha 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_01137};
DE            Short=ACDS CODH subunit alpha 1 {ECO:0000255|HAMAP-Rule:MF_01137};
GN   Name=cdhA1 {ECO:0000255|HAMAP-Rule:MF_01137};
GN   OrderedLocusNames=MK0717;
OS   Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC
OS   100938).
OC   Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC   Methanopyrus.
OX   NCBI_TaxID=190192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX   PubMed=11930014; DOI=10.1073/pnas.032671499;
RA   Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA   Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L.,
RA   Natale D.A., Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O.,
RA   Malykh A.G., Koonin E.V., Kozyavkin S.A.;
RT   "The complete genome of hyperthermophile Methanopyrus kandleri AV19
RT   and monophyly of archaeal methanogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
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; AE009439; AAM01931.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q8TXF7; -.
DR   SMR; Q8TXF7; -.
DR   EnsemblBacteria; AAM01931; AAM01931; MK0717.
DR   KEGG; mka:MK0717; -.
DR   PATRIC; fig|190192.8.peg.758; -.
DR   eggNOG; arCOG02428; Archaea.
DR   eggNOG; COG1152; LUCA.
DR   HOGENOM; HOG000224351; -.
DR   KO; K00192; -.
DR   OMA; EVCGICC; -.
DR   Proteomes; UP000001826; 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    760       Acetyl-CoA decarbonylase/synthase complex
FT                                subunit alpha 1.
FT                                /FTId=PRO_0000155078.
FT   DOMAIN      381    410       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   DOMAIN      418    450       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL        56     56       Iron-sulfur 1 (4Fe-4S); shared with
FT                                dimeric partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_01137}.
FT   METAL        59     59       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL        60     60       Iron-sulfur 1 (4Fe-4S); shared with
FT                                dimeric partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_01137}.
FT   METAL        62     62       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL        67     67       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL        77     77       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       231    231       Nickel-iron-sulfur (Ni-4Fe-4S); via tele
FT                                nitrogen. {ECO:0000255|HAMAP-
FT                                Rule:MF_01137}.
FT   METAL       259    259       Nickel-iron-sulfur (Ni-4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       298    298       Nickel-iron-sulfur (Ni-4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       390    390       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       393    393       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       396    396       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       400    400       Iron-sulfur 4 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       428    428       Iron-sulfur 4 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       431    431       Iron-sulfur 4 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       434    434       Iron-sulfur 4 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       438    438       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       496    496       Nickel-iron-sulfur (Ni-4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       525    525       Nickel-iron-sulfur (Ni-4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   METAL       560    560       Nickel-iron-sulfur (Ni-4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
FT   BINDING     100    100       Carbon monoxide; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01137}.
SQ   SEQUENCE   760 AA;  84637 MW;  E82B0EF7D4163CAA CRC64;
     MSPFELEFEG LKVQIGSIEG FEPRGEGPLP CPTVSDLADW DRKLFARYRV IAFPICDMCC
     MCTYGRCNLA EGRRGACGID IRSNTARFTA LKTCIGAACH AAHARHLVEY ILEKLGDVEI
     DLGSEVDVMT PIFETLVGFK PKTVSDLEKG LEYIERELTK VLSSVHVGQE MDPHDYESKA
     LHAGMIDNLA LEIADVAQIA AFDMPKGEAP LVEFGPFAAD DSKPCILLVG HNVAPGTEVL
     DYLEERGLDE EVEVLGICCT AWDVSRVDDR SKVIGPLSRQ LHYVRMGIAD VVVLDEQCIR
     ADIVEEANEV GSRVIATRDL VMAGLPDVTD EPTEKIIEKM VSGEWMGVFI EDLEKAAEVA
     VEVAIRVHER RKKEIPQPDP KKLQKEAKRC LGCGDCERVC PNDLPIVEAM ERAANGDFEG
     LADLFDRCVG CARCESECPT KLRVMNMIED AWRLRTKEEK YKVRTGRGPI KDVEIRQVGG
     PIVMGDIPGV VAFVACPNYP DDVKQVGKMV EELLERNYIV LTSGCTAMAL GMYTDEDGKT
     LYEKYEDRFD AGCLVNTGSC VSNAHILGAC IKIAAIFAKK PLKGNFKEIA DYILNRIGAC
     GVLWGTMSQK ALAISTGFTR WGIPIVYGPA GLKYQTLYIG DLDGDWTVYD ARTGKECKEY
     CPIHLKYAAE DWREALVQAV KLCIRPNDTP QGRQTKLQNY IELYKEFYNE LPPDLPLYVR
     DKNDVPITLR DEVMEYLEEV GWKPRKGITE PTLLEENVRG
//
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