ACDA_METTH
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 03-AUG-2022, entry version 137.
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}; OrderedLocusNames=MTH_1708;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium 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., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT 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). 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; AE000666; AAB86180.1; -; Genomic_DNA.
DR PIR; E69095; E69095.
DR AlphaFoldDB; O27743; -.
DR SMR; O27743; -.
DR IntAct; O27743; 2.
DR STRING; 187420.MTH_1708; -.
DR EnsemblBacteria; AAB86180; AAB86180; MTH_1708.
DR KEGG; mth:MTH_1708; -.
DR PATRIC; fig|187420.15.peg.1669; -.
DR HOGENOM; CLU_361186_0_0_2; -.
DR OMA; LCIGHNV; -.
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; 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; 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..780
FT /note="Acetyl-CoA decarbonylase/synthase complex subunit
FT alpha"
FT /id="PRO_0000155085"
FT DOMAIN 399..429
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT DOMAIN 440..469
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 73
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 76
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="1"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 79
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 84
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 93
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 116
FT /ligand="CO"
FT /ligand_id="ChEBI:CHEBI:17245"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 250
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 278
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 317
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 409
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 412
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 415
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 419
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 449
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 452
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 455
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 459
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 517
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 546
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 581
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="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
