ACDA1_METTE
ID ACDA1_METTE Reviewed; 806 AA.
AC Q08368; P72019;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 108.
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};
OS Methanosarcina thermophila.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=2210;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-21.
RC STRAIN=ATCC 43570 / DSM 1825 / OCM 12 / TM-1;
RX PubMed=8955306; DOI=10.1128/jb.178.23.6849-6856.1996;
RA Maupin-Furlow J.A., Ferry J.G.;
RT "Analysis of the CO dehydrogenase/acetyl-Coenzyme A synthase operon of
RT Methanosarcina thermophila.";
RL J. Bacteriol. 178:6849-6856(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-107, AND PROTEIN SEQUENCE OF 2-20.
RC STRAIN=ATCC 43570 / DSM 1825 / OCM 12 / TM-1;
RX PubMed=7693685; DOI=10.1016/s0021-9258(19)49443-x;
RA Sowers K.R., Thai T.T., Gunsalus R.P.;
RT "Transcriptional regulation of the carbon monoxide dehydrogenase gene
RT (cdhA) in Methanosarcina thermophila.";
RL J. Biol. Chem. 268:23172-23178(1993).
RN [3]
RP CHARACTERIZATION.
RX PubMed=11607176; DOI=10.1073/pnas.88.8.3272;
RA Abbanat D.R., Ferry J.G.;
RT "Resolution of component proteins in an enzyme complex from Methanosarcina
RT thermophila catalyzing the synthesis or cleavage of acetyl-CoA.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:3272-3276(1991).
CC -!- FUNCTION: Part of the ACDS complex that catalyzes the reversible
CC cleavage of acetyl-CoA, allowing growth on acetate as sole source of
CC carbon and energy. The alpha-epsilon subcomponent functions as a carbon
CC monoxide 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 -!- PATHWAY: One-carbon metabolism; methanogenesis from acetate.
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; U66032; AAC44650.1; -; Genomic_DNA.
DR EMBL; L20952; AAA72034.1; -; Genomic_DNA.
DR PIR; A48868; A48868.
DR AlphaFoldDB; Q08368; -.
DR SMR; Q08368; -.
DR PRIDE; Q08368; -.
DR KEGG; ag:AAC44650; -.
DR BioCyc; MetaCyc:CDHAMSARC-MON; -.
DR UniPathway; UPA00642; -.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0018492; F:carbon-monoxide dehydrogenase (acceptor) activity; IDA:MENGO.
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:0019385; P:methanogenesis, from acetate; IEA:UniProtKB-UniRule.
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; 1.
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 Methanogenesis; Nickel; Oxidoreductase; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7693685,
FT ECO:0000269|PubMed:8955306"
FT CHAIN 2..806
FT /note="Acetyl-CoA decarbonylase/synthase complex subunit
FT alpha 1"
FT /id="PRO_0000155083"
FT DOMAIN 407..436
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT DOMAIN 445..475
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 94
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 117
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 323
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 417
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 420
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 423
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 427
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 458
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 461
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 465
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 523
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 552
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 587
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
SQ SEQUENCE 806 AA; 88538 MW; 6CC1BB8A6DFEBD61 CRC64;
MSKLTTGSFS IEDLESVQIT INNVIGAAKE AADEKAKDLG PMGPSAWPGL ATYRDDWNLK
LLDRYEPVIT PMCDQCCYCT YGPCDLSNNK RGACGIDMLG HNGREFFLRV ITGTACHAAH
GRHLLDHLIE VFGEDLPLKL GQSDVLTPNI TITTGQRPMT LGEIKPAMEH TEEQLTQLLA
TVHAGQESAE IDYDSKALFS GSLDHVGMEI SDIVQIAALD FPKADPEAPL IEMGVGTIDK
EKPFLCVIGH NVGGVTYMMD YMEEHDLTGK MELGGLCCTA IDLTRYKEAD RRAPYTKVIG
SMSQELKIIR SGLPDVIVVD EQCVRGDIVP EAQKLGIPVI ASNAKIMYGL PNRDEQDVDA
TIEELKSGAI PGAVILDYDK LGEISVRLTQ EMHPLREAAG LRKIASDEQM KEWVDKCADC
GSCYLVCPEE LEIPEAMKHA KEGDYSYLVD LHDQCIGCRR CEQVCKKEIP ILSVIEKASQ
KVIAEEKGWM RAGRGQVSDA EIRAEGLNLV MGTTPGIIAI IGCPNYGDGA KSVYYIAEEF
LKRNFIVVGT GCGAMDMGMY KDENGQTLYE RFPGGFQSGG LVNIGSCVSN AHITGAAQKV
AGIFGGRTME GNLAEIADYV LNRVGACGLA WGAFSQKASS IGTGCNIYGI PAVLGPHSSK
YRRALISKNY DDEKWKVYDA RSGEEMAIPP APEFLLITAE TWQEAIPMMA KACIRPSDNS
MGRSIKLTHW MELHQKYIGG MPEDWWKFIR TEADLPLAKR AELMKKLEEE HGWEIDWKRK
KIISGPKIKF DVSAQPTNLK RLCKGA
