ACDA2_METTE
ID ACDA2_METTE Reviewed; 803 AA.
AC Q9C4Z4;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Acetyl-CoA decarbonylase/synthase complex subunit alpha 2 {ECO:0000255|HAMAP-Rule:MF_01137};
DE Short=ACDS complex subunit alpha 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_01137};
DE Short=ACDS CODH subunit alpha 2 {ECO:0000255|HAMAP-Rule:MF_01137};
GN Name=cdhA2 {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].
RC STRAIN=ATCC 43570 / DSM 1825 / OCM 12 / TM-1;
RX PubMed=12464601; DOI=10.1074/jbc.m210484200;
RA Gencic S., Grahame D.A.;
RT "Nickel in subunit beta of the acetyl-CoA decarbonylase/synthase
RT multienzyme complex in methanogens. Catalytic properties and evidence for a
RT binuclear Ni-Ni site.";
RL J. Biol. Chem. 278:6101-6110(2003).
RN [2]
RP CRYSTALLIZATION.
RX PubMed=12657792; DOI=10.1107/s0907444903001987;
RA Balbo P., Oliveira M.;
RT "Crystallization and preliminary X-ray data of the alpha2epsilon2
RT subcomponent of the acetyl-CoA decarbonylase/synthase multienzyme complex
RT from Methanosarcina thermophila.";
RL Acta Crystallogr. D 59:721-723(2003).
RN [3]
RP ELECTRON MICROSCOPY OF ALPHA-EPSILON COMPLEX.
RX PubMed=10600570; DOI=10.1006/jsbi.1999.4163;
RA Kocsis E., Kessel M., DeMoll E., Grahame D.A.;
RT "Structure of the Ni/Fe-S protein subcomponent of the acetyl-CoA
RT decarbonylase/synthase complex from Methanosarcina thermophila at 26-A
RT resolution.";
RL J. Struct. Biol. 128:165-174(1999).
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
CC (PubMed:10600570, PubMed:12657792). The ACDS complex is made up of
CC alpha, epsilon, beta, gamma and delta subunits with a probable
CC stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8)
CC (By similarity). {ECO:0000255|HAMAP-Rule:MF_01137,
CC ECO:0000269|PubMed:10600570, ECO:0000269|PubMed:12657792}.
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; AF173830; AAG53710.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9C4Z4; -.
DR SMR; Q9C4Z4; -.
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; Iron; Iron-sulfur; Metal-binding; Methanogenesis; Nickel;
KW Oxidoreductase; Repeat.
FT CHAIN 1..803
FT /note="Acetyl-CoA decarbonylase/synthase complex subunit
FT alpha 2"
FT /id="PRO_0000155084"
FT DOMAIN 405..433
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT DOMAIN 443..472
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 72
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 75
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 76
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 78
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 83
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 249
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 277
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 322
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 414
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 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 424
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 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 462
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 520
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 549
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
FT BINDING 584
FT /ligand="[Ni-4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:47739"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01137"
SQ SEQUENCE 803 AA; 87738 MW; 1C9565D8E1EAEC14 CRC64;
MAKLTTGSFS IEDLESVQIT INNIVGAAKE AAEKAEEELG PMGPTPFPTA ATVRDWSFTL
FDRYEPVYTP MCDQCCYCTF GPCNLEGNRR GACGLDMKGQ AAREFFLRCI TGCACHSAHG
RHLLDHIISI FGEDMPINMG ASNVIAPNIQ LITGRQPKTL GDLKPIMEYV EEELGQLLAT
VHAGQEGAAI DYDNKAMLAG ILDHVGMEVS DIAQVTALGF PKSDPEAPLV EVGMGTLDAS
KPVIIAIGHN VAGVTYIMDY MEDNNLTDKM EIGGLCCTAF DMTRYKREDR KPPYAKIVGT
ISKELKVVRS GIPDVIVIDE QCVRADLVEE GKKLKIPVIA SNEKVMYGLP DRTNDDVDAI
IEDIKTGKIP GCVMLDYEKL GELVPRLAME MAPLREGISA IPSDEEMASL VAKCVACGEC
ALACPEELDI PDAIQAAKEG DFTALDFLHD LCVGCRRCEQ VCNKEIPILS VIDKAAQKAI
AEEKGLVRAG RGQVSDAEIR AEGLNLVMGT TPGVIAIIGC ANYPAGSKDV YRIAEEFLNR
NYIVAVSGCS AMDIGMYKDA DGKTLYERFP GRFERGNILN TGSCVSNSHI SGTCHKVAAI
FAGRNLSGNL AEIADYTLNR VGAVGLAWGA YSQKAAAIGT GCNMYGIPAV LGPHSGKYRR
ALIAKTYDEN KWKVYDSRNG SELDIPPSPE FLITTAETWQ EACVLLAKNC IRPSDNNMGR
SIKLTHWIEL SEKYLGVLPE DWWKFVRHEA DLPLSRREEL LKKLETEHGW EIDWKKKKII
SGPKIKFDVS SQPTNLKRLC KEA
