ACDG1_METTE
ID ACDG1_METTE Reviewed; 468 AA.
AC Q50539;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Acetyl-CoA decarbonylase/synthase complex subunit gamma 1 {ECO:0000255|HAMAP-Rule:MF_01136};
DE Short=ACDS complex subunit gamma 1 {ECO:0000255|HAMAP-Rule:MF_01136};
DE EC=2.1.1.245 {ECO:0000255|HAMAP-Rule:MF_01136, ECO:0000269|PubMed:8626532};
DE AltName: Full=5-methyltetrahydrosarcinapterin:corrinoid/iron-sulfur protein Co-methyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_01136};
DE AltName: Full=ACDS complex methyltransferase 1 {ECO:0000255|HAMAP-Rule:MF_01136};
DE AltName: Full=Corrinoid/iron-sulfur component large subunit 1 {ECO:0000255|HAMAP-Rule:MF_01136};
GN Name=cdhE1 {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], AND PROTEIN SEQUENCE OF 1-19.
RC STRAIN=ATCC 43570 / DSM 1825 / OCM 12 / TM-1;
RX PubMed=8550451; DOI=10.1128/jb.178.2.340-346.1996;
RA Maupin-Furlow J., Ferry J.G.;
RT "Characterization of the cdhD and cdhE genes encoding subunits of the
RT corrinoid/iron-sulfur enzyme of the CO dehydrogenase complex from
RT Methanosarcina thermophila.";
RL J. Bacteriol. 178:340-346(1996).
RN [2]
RP CHARACTERIZATION OF PARTIAL REACTIONS IN THE ACDS COMPLEX, AND CATALYTIC
RP ACTIVITY.
RX PubMed=8626532; DOI=10.1074/jbc.271.14.8352;
RA Grahame D.A., DeMoll E.;
RT "Partial reactions catalyzed by protein components of the acetyl-CoA
RT decarbonylase synthase enzyme complex from Methanosarcina barkeri.";
RL J. Biol. Chem. 271:8352-8358(1996).
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 ECO:0000269|PubMed:8626532};
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; U30484; AAA93168.1; -; Genomic_DNA.
DR AlphaFoldDB; Q50539; -.
DR SMR; Q50539; -.
DR KEGG; ag:AAA93168; -.
DR BioCyc; MetaCyc:CDHEMSARC-MON; -.
DR BRENDA; 2.1.1.245; 3281.
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 1: Evidence at protein level;
KW 4Fe-4S; Cobalt; Direct protein sequencing; Iron; Iron-sulfur;
KW Metal-binding; Methanogenesis; Methyltransferase; Transferase.
FT CHAIN 1..468
FT /note="Acetyl-CoA decarbonylase/synthase complex subunit
FT gamma 1"
FT /id="PRO_0000155124"
FT DOMAIN 1..61
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; 51036 MW; ACB17B45AF39D45F CRC64;
MKINSPLEAY KYLPQTNCGE CGEPTCMAFA SKLIDRSGKT SDCPPLVKEK KYAKKLAELD
RLLAPEIRQV TIGVGEKAAN IGGDDVLYRH KLTFFNKTKM FFDVSDNMEE DALIERVKKI
ADFKKFYVGR NLLLDGVAIK ATSNDPAKFA AAVKKVAEIG LPMIFCSFNP AVLKAGLEVA
KDKNPLLYAA NKDNWKEVGE LALEYKVPVV VSVFNDLDGL KSLAKTFAEA GIKDIVLDPG
TYPSGKGLKD TFTNFLKIRR AGIMGDTEIA YPIMALPLTA WMAGISDPVS ASYWETVIAS
VFTIRYGDIM ILHSLEPYAA LPEMHLAETI YTDPRTPVSV DGGMYKVGEP DKDSPVFFTT
NFALTYYTVE SDISANGIVC WLLAVDTDGI GVEAAVAGGQ LTSAKVKDAF EKAGFDLKTD
TNHNTLIIPG LSARLQGDLE DTLGANVKVG PMDSGRIPGW VEKNWPPK
