ACDG2_METTE
ID ACDG2_METTE Reviewed; 468 AA.
AC Q9C4Z0;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Acetyl-CoA decarbonylase/synthase complex subunit gamma 2 {ECO:0000255|HAMAP-Rule:MF_01136};
DE Short=ACDS complex subunit gamma 2 {ECO:0000255|HAMAP-Rule:MF_01136};
DE EC=2.1.1.245 {ECO:0000255|HAMAP-Rule:MF_01136};
DE AltName: Full=5-methyltetrahydrosarcinapterin:corrinoid/iron-sulfur protein Co-methyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_01136};
DE AltName: Full=ACDS complex methyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_01136};
DE AltName: Full=Corrinoid/iron-sulfur component large subunit 2 {ECO:0000255|HAMAP-Rule:MF_01136};
GN Name=cdhE2 {ECO:0000255|HAMAP-Rule:MF_01136};
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).
CC -!- FUNCTION: Part of a complex that catalyzes the reversible cleavage of
CC acetyl-CoA, allowing growth on acetate as sole source of carbon and
CC energy. {ECO:0000255|HAMAP-Rule:MF_01136}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6,7,8-tetrahydrosarcinapterin + methyl-Co(III)-[corrinoid
CC Fe-S protein] = 5-methyltetrahydrosarcinapterin + Co(I)-[corrinoid
CC Fe-S protein] + H(+); Xref=Rhea:RHEA:45196, Rhea:RHEA-COMP:11110,
CC Rhea:RHEA-COMP:11111, ChEBI:CHEBI:15378, ChEBI:CHEBI:59924,
CC ChEBI:CHEBI:64267, ChEBI:CHEBI:85033, ChEBI:CHEBI:85035;
CC EC=2.1.1.245; Evidence={ECO:0000255|HAMAP-Rule:MF_01136};
CC -!- COFACTOR:
CC Name=corrinoid; Xref=ChEBI:CHEBI:33913;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01136};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01136};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_01136};
CC -!- PATHWAY: One-carbon metabolism; methanogenesis from acetate.
CC {ECO:0000255|HAMAP-Rule:MF_01136}.
CC -!- SUBUNIT: Heterodimer of delta and gamma chains. The ACDS complex is
CC made up of alpha, epsilon, beta, gamma and delta chains with a probable
CC stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8).
CC {ECO:0000255|HAMAP-Rule:MF_01136}.
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DR EMBL; AF173830; AAG53714.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9C4Z0; -.
DR SMR; Q9C4Z0; -.
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:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046356; P:acetyl-CoA catabolic process; IEA:InterPro.
DR GO; GO:0019385; P:methanogenesis, from acetate; IEA:UniProtKB-UniRule.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.20; -; 1.
DR HAMAP; MF_01136; CdhE; 1.
DR InterPro; IPR007202; 4Fe-4S_dom.
DR InterPro; IPR016041; Ac-CoA_synth_d_su_TIM-brl.
DR InterPro; IPR016218; AcylCoA_decarb/synth_gsu.
DR InterPro; IPR023427; AcylCoA_decarb/synth_gsu_arc.
DR InterPro; IPR011005; Dihydropteroate_synth-like.
DR Pfam; PF03599; CdhD; 1.
DR Pfam; PF04060; FeS; 1.
DR PIRSF; PIRSF000376; AcCoA_decarb_gamma; 1.
DR SUPFAM; SSF51717; SSF51717; 1.
DR PROSITE; PS51656; 4FE4S; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Cobalt; Iron; Iron-sulfur; Metal-binding; Methanogenesis;
KW Methyltransferase; Transferase.
FT CHAIN 1..468
FT /note="Acetyl-CoA decarbonylase/synthase complex subunit
FT gamma 2"
FT /id="PRO_0000155125"
FT DOMAIN 1..60
FT /note="4Fe-4S"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00989"
FT BINDING 18
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01136"
FT BINDING 21
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01136"
FT BINDING 26
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01136"
FT BINDING 43
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01136"
SQ SEQUENCE 468 AA; 51242 MW; D4EE027D3919BB56 CRC64;
MKINSPLEAY KYLPQTNCGE CGEATCMAFA SKLIDRSGKP TQCPPLVKEK KFAKKLAELE
RLLAPEIREI TIGVGDRAVK IGGDDVLYRH KLTFFNKTKM FYDVTDTMDE AALLERTKKV
ADFRKFYVGR NLLLDGVAIR SVSNDPEKFA AAVKKVSEVG IPMILCSFNP AVLKAGLEVA
KDKNPLIYAA NKDNWKEVGE LALEYNVPVV VSAFNDLDGL KTLAKTFAEA GIKDIVLDPG
TYPSGQGLKD SFTNFLKIRR AGIMGDTEIA YPIMALPITA WMAGISDPVS AAYWETAMAA
IFTIRYGDIM ILHSLEPYAT LPEVHLAETI YTDPRTPVAV DSKMYKVGEP DENSPVLFTT
NFALTYYTVE SDLSSNGITC WLLAVDTDGI GVEAAAAGGQ LTADKVKDAF EKSGFDLKKD
VTHNTVIIPG LAARLQGDLE DKLGARVLVG PMDSGRLPGW FEKNWPPK
