ACDA_METSH
ID ACDA_METSH Reviewed; 793 AA.
AC P26692;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 112.
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};
OS Methanothrix soehngenii (Methanosaeta concilii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanotrichales; Methanotrichaceae; Methanothrix.
OX NCBI_TaxID=2223;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=Opfikon / DSM 2139;
RX PubMed=1901858; DOI=10.1016/s0021-9258(20)89584-2;
RA Eggen R.I.L., Geerling A.C.M., Jetten M.S.M., de Vos W.M.;
RT "Cloning, expression, and sequence analysis of the genes for carbon
RT monoxide dehydrogenase of Methanothrix soehngenii.";
RL J. Biol. Chem. 266:6883-6887(1991).
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 6 [4Fe-4S] clusters per heterotetramer. {ECO:0000305};
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}.
CC -!- CAUTION: This protein lacks the conserved Cys in positions 52 and 56;
CC they are replaced by an Asp and a Thr, respectively. It is therefore
CC possible that the D-cluster is either altered or missing in this
CC protein, which may not form heterotetramers. {ECO:0000305}.
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DR EMBL; M55280; AAA72934.1; -; Genomic_DNA.
DR PIR; A39764; A39764.
DR AlphaFoldDB; P26692; -.
DR SMR; P26692; -.
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; 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 1: Evidence at protein level;
KW 4Fe-4S; Direct protein sequencing; Iron; Iron-sulfur; Metal-binding;
KW Nickel; Oxidoreductase; Repeat.
FT CHAIN 1..793
FT /note="Acetyl-CoA decarbonylase/synthase complex subunit
FT alpha"
FT /id="PRO_0000155082"
FT DOMAIN 393..422
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT DOMAIN 432..461
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 55
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 58
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 63
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 73
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 96
FT /ligand="CO"
FT /ligand_id="ChEBI:CHEBI:17245"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 229
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 257
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 309
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 403
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 406
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 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 413
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 441
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 444
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 447
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 451
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 509
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 538
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 573
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
SQ SEQUENCE 793 AA; 88152 MW; 7CBCB187B1860A2B CRC64;
MKNVQINIGA VVKEEDEWDQ EMGPFPKPGV ATLRDWDFKI CNRYKIMYSP ADDTCTLCTY
GPCDLTGNKK GACGIDMAAA CGKIVLVAVL MGTCAHTAHG RHLYHWCLDK FGDMPFDMGS
EILVDAPLYR TILGKKPKSL KDFGEALEYC EEEIVQLLAA CHTGQEGHYM DFESKSLHSG
MIDSLGKEIC DMLQTVAYDM PRGAADAPLV EIGMGTLDQN KGVLIAYGHN LAAGAEAMIY
TEEHNLWDKV DIGGVCCTAI DLTRITETGR ESKIPANLGP KAKVAGAMGW WRKMVRAGIM
DTVIVDEQCV FCDVLEDCQQ RHIPVIASND KIMLGLPDRT NDSADAIVED LVSFKMPGVA
ILDPVKAGEV AIRTAVAVKP KREQYKKESL FTEQQFKDTL ATCTECNQCA FVCPPHIRIS
EMISEALKGN LEPFSSTYEV CVGCQRCEQT CPQEIPILKL YEYANREYIR NQKFKMRAGR
GPVLDTEIRK VGAPLVLGQI PGVIALVGCS NYPNGTKECY DIAKEFVDRG YIVVATGCMA
MDMSLYKDED GKTIWEQYEG AFDGRNICNI GSCVANAHIH GAAIKVATIF AHRNERANYD
DIADYIMSKV GACGVAWGAY SQKAASIATG VNRIGIPVVV QPSSVIYRRT FMGRTDKPED
WMVIDAKNGN MQQIEPAPEA MLYIAETKEE AMLEMAKLCF RPSDNTQGRG IKLTHYCDIS
MKYFGKLPDD WHLFVRDVKD LPLNYQTQMM KELEEKHGWK IDWKAKKFIS GPLRPADVSF
DPTNIPRKIR AKK
