ACDA1_METKA
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 03-AUG-2022, entry version 109.
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}; OrderedLocusNames=MK0717;
OS Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 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., Natale D.A.,
RA Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA Koonin E.V., Kozyavkin S.A.;
RT "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT 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). The
CC 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 H(+) + 2
CC reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:21040, Rhea:RHEA-
CC 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. {ECO:0000255|HAMAP-
CC 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 ACDS
CC complex is made up of alpha, epsilon, beta, gamma and delta subunits
CC with a probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-
CC (gamma(1)delta(1))(8). {ECO:0000255|HAMAP-Rule:MF_01137}.
CC -!- DOMAIN: Cluster B is an all-cysteinyl-liganded 4Fe-4S cluster; cluster
CC C is a mixed Ni-Fe-S cluster which is the active site of CO oxidation.
CC Cluster D is also an all-cysteinyl-liganded 4Fe-4S cluster that bridges
CC the two subunits of the CODH dimer. Contains two additional 4Fe-4S
CC clusters, dubbed E and F, that probably transport electrons from
CC ferredoxin to the B cluster. {ECO:0000255|HAMAP-Rule:MF_01137}.
CC -!- SIMILARITY: Belongs to the Ni-containing carbon monoxide dehydrogenase
CC family. {ECO:0000255|HAMAP-Rule:MF_01137}.
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DR EMBL; AE009439; AAM01931.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8TXF7; -.
DR SMR; Q8TXF7; -.
DR STRING; 190192.MK0717; -.
DR EnsemblBacteria; AAM01931; AAM01931; MK0717.
DR KEGG; mka:MK0717; -.
DR PATRIC; fig|190192.8.peg.758; -.
DR HOGENOM; CLU_361186_0_0_2; -.
DR OMA; LCIGHNV; -.
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 GO; GO:0006091; P:generation of precursor metabolites and energy; IEA:InterPro.
DR CDD; cd01916; ACS_1; 1.
DR Gene3D; 1.20.1270.30; -; 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; IPR016101; CO_DH_a-bundle.
DR InterPro; IPR004137; HCP/CODH.
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; 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; Iron; Iron-sulfur; Metal-binding; Nickel; Oxidoreductase;
KW Reference proteome; Repeat.
FT CHAIN 1..760
FT /note="Acetyl-CoA decarbonylase/synthase complex subunit
FT alpha 1"
FT /id="PRO_0000155078"
FT DOMAIN 381..410
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT DOMAIN 418..450
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 56
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 59
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 60
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 62
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 67
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 77
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 100
FT /ligand="CO"
FT /ligand_id="ChEBI:CHEBI:17245"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 231
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 259
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 298
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 390
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 393
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 396
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 400
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 428
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 431
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 434
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 438
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 496
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 525
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 560
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="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
