ACDG_METTH
ID ACDG_METTH Reviewed; 458 AA.
AC O27748;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Acetyl-CoA decarbonylase/synthase complex subunit gamma {ECO:0000255|HAMAP-Rule:MF_01136};
DE Short=ACDS complex subunit gamma {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 {ECO:0000255|HAMAP-Rule:MF_01136};
DE AltName: Full=ACDS complex methyltransferase {ECO:0000255|HAMAP-Rule:MF_01136};
DE AltName: Full=Corrinoid/iron-sulfur component large subunit {ECO:0000255|HAMAP-Rule:MF_01136};
GN Name=cdhE {ECO:0000255|HAMAP-Rule:MF_01136}; OrderedLocusNames=MTH_1713;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
CC -!- FUNCTION: Part of a complex that catalyzes the reversible cleavage of
CC acetyl-CoA, allowing autotrophic growth from CO(2). {ECO:0000255|HAMAP-
CC 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 -!- 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE000666; AAB86185.1; -; Genomic_DNA.
DR PIR; C69096; C69096.
DR RefSeq; WP_010877321.1; NC_000916.1.
DR AlphaFoldDB; O27748; -.
DR SMR; O27748; -.
DR IntAct; O27748; 1.
DR STRING; 187420.MTH_1713; -.
DR EnsemblBacteria; AAB86185; AAB86185; MTH_1713.
DR GeneID; 1470798; -.
DR KEGG; mth:MTH_1713; -.
DR PATRIC; fig|187420.15.peg.1674; -.
DR HOGENOM; CLU_050002_0_0_2; -.
DR OMA; SCMAFAT; -.
DR Proteomes; UP000005223; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
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: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; Methyltransferase;
KW Reference proteome; Transferase.
FT CHAIN 1..458
FT /note="Acetyl-CoA decarbonylase/synthase complex subunit
FT gamma"
FT /id="PRO_0000155126"
FT DOMAIN 1..59
FT /note="4Fe-4S"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00989"
FT BINDING 17
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01136"
FT BINDING 20
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01136"
FT BINDING 25
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01136"
FT BINDING 42
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01136"
SQ SEQUENCE 458 AA; 50231 MW; 14224FFBA40DD170 CRC64;
MQVTAMDVYR LLPKTNCGKC NEASCMAFAT KLIEKEVTLD DCPQLSGDER QKLENLLAPA
VKEITFGPEE NQVVVGGDEV LYRYELTYYN PTALVVDLPD DLPSEELLNR AQRIMELEFE
RTGEKLTLDA IALRNRSGSP EKFAEAAEAI SKLNFPVVLC TFDVEAMKAA LEVLGDQKPL
LYAAREDNLG EMAELSVSYG CPLVLFSPGD LEEMKNLSRR LRSLGVTEIV LDPGTFTGEG
IGDTIDNFVM IRRLAVEDGD DDFRFPIMGI PALSRLTVSD KIEANIREAT VAATLMNRYA
DILILAGTEI WEIMPVLTLR QGLYTDPRKP QAVDPGVYEF GDVDENSPVI LTTNFSLTYY
TVEGDLKSGD VTAYLLVLDT EGRAVDVSLA GGQLNGPAVA DLIKETGIEE RVRDKVMIIP
GLAAPASGEI EDDTGWRVLV GPRDSSGIPD YLDKLASE
