ACDG2_METMA
ID ACDG2_METMA Reviewed; 470 AA.
AC Q8PV87;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 126.
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}; OrderedLocusNames=MM_2084;
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA Fritz H.-J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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; AE008384; AAM31780.1; -; Genomic_DNA.
DR RefSeq; WP_011034016.1; NC_003901.1.
DR AlphaFoldDB; Q8PV87; -.
DR SMR; Q8PV87; -.
DR STRING; 192952.MM_2084; -.
DR EnsemblBacteria; AAM31780; AAM31780; MM_2084.
DR GeneID; 24840344; -.
DR KEGG; mma:MM_2084; -.
DR PATRIC; fig|192952.21.peg.2392; -.
DR eggNOG; arCOG01979; Archaea.
DR HOGENOM; CLU_050002_0_0_2; -.
DR OMA; PEDIWAL; -.
DR UniPathway; UPA00642; -.
DR Proteomes; UP000000595; 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: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; Reference proteome; Transferase.
FT CHAIN 1..470
FT /note="Acetyl-CoA decarbonylase/synthase complex subunit
FT gamma 2"
FT /id="PRO_0000155123"
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 470 AA; 51348 MW; FD0B757AD19FE753 CRC64;
MKINSPLEAY KYLPQTNCGE CGQPTCMAFA STLIDRSGKT TDCPPLIKEK KFAKKLAELD
RLLAPEIRQV TIGVGERAAN IGGDDVLYRH KLTFFNKTKM FFDVADNMDE AAIVERVKKI
SDYKKFYVGR NLLLDGVAIR AASNDPAKFA TAVKKVIENT ELPVILCSFN PAVLKAGLEV
AKGKNPLLYA ANKDNWKEVG ELALEYNVPV VVSAFNDLDG LKTLAKTFAE AGIKDIVLDP
GTYPTGKGLK DTFTNFLKIR RAGIMGDTEI AYPIMAMPLT AWMAGIADPV SASYWETVLS
SIFTIRYGDI MLLHSMEPYA TMPEVHLAET IYTDPRSPVA VDSKMYKVGN PTADSPVLFT
TNFALTYYTV ESDLASNGID CWLLAVNTDG IGVEAAAAGG QLTADKVKDA FEKSGFDLKS
DVTHNSVVIP GLAARLQGDI EDKLNVKVMV GPMDSGRLPG WMEKNWPPKK
