ID A0A062V852_9EURY Unreviewed; 469 AA.
AC A0A062V852;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Acetyl-CoA decarbonylase/synthase complex subunit gamma {ECO:0000256|HAMAP-Rule:MF_01136};
DE Short=ACDS complex subunit gamma {ECO:0000256|HAMAP-Rule:MF_01136};
DE EC=2.1.1.245 {ECO:0000256|HAMAP-Rule:MF_01136};
DE AltName: Full=5-methyltetrahydrosarcinapterin:corrinoid/iron-sulfur protein Co-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01136};
DE AltName: Full=ACDS complex methyltransferase {ECO:0000256|HAMAP-Rule:MF_01136};
DE AltName: Full=Corrinoid/iron-sulfur component large subunit {ECO:0000256|HAMAP-Rule:MF_01136};
GN Name=cdhE {ECO:0000256|HAMAP-Rule:MF_01136};
GN ORFNames=ANME2D_00520 {ECO:0000313|EMBL:KCZ73452.1};
OS Candidatus Methanoperedens nitroreducens.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Candidatus Methanoperedenaceae; Methanoperedens.
OX NCBI_TaxID=1392998 {ECO:0000313|EMBL:KCZ73452.1, ECO:0000313|Proteomes:UP000027153};
RN [1] {ECO:0000313|EMBL:KCZ73452.1, ECO:0000313|Proteomes:UP000027153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANME-2d {ECO:0000313|EMBL:KCZ73452.1,
RC ECO:0000313|Proteomes:UP000027153};
RX PubMed=23892779; DOI=10.1038/nature12375;
RA Haroon M.F., Hu S., Shi Y., Imelfort M., Keller J., Hugenholtz P., Yuan Z.,
RA Tyson G.W.;
RT "Anaerobic oxidation of methane coupled to nitrate reduction in a novel
RT archaeal lineage.";
RL Nature 500:567-570(2013).
CC -!- FUNCTION: Part of a complex that catalyzes the reversible cleavage of
CC acetyl-CoA, allowing autotrophic growth from CO(2). {ECO:0000256|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:0000256|HAMAP-Rule:MF_01136};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01136};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|HAMAP-Rule:MF_01136};
CC -!- COFACTOR:
CC Name=corrinoid; Xref=ChEBI:CHEBI:33913;
CC Evidence={ECO:0000256|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:0000256|HAMAP-Rule:MF_01136}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KCZ73452.1}.
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DR EMBL; JMIY01000001; KCZ73452.1; -; Genomic_DNA.
DR RefSeq; WP_048088916.1; NZ_JMIY01000001.1.
DR AlphaFoldDB; A0A062V852; -.
DR PATRIC; fig|1392998.3.peg.121; -.
DR OrthoDB; 146240at2157; -.
DR Proteomes; UP000027153; Unassembled WGS sequence.
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:0015948; P:methanogenesis; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.11600; -; 1.
DR Gene3D; 3.20.20.20; Dihydropteroate synthase-like; 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_sf.
DR PANTHER; PTHR36214; -; 1.
DR PANTHER; PTHR36214:SF3; ACETYL-COA DECARBONYLASE_SYNTHASE COMPLEX SUBUNIT GAMMA; 1.
DR Pfam; PF03599; CdhD; 1.
DR Pfam; PF04060; FeS; 1.
DR PIRSF; PIRSF000376; AcCoA_decarb_gamma; 1.
DR SUPFAM; SSF51717; Dihydropteroate synthetase-like; 1.
DR PROSITE; PS51656; 4FE4S; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_01136};
KW Cobalt {ECO:0000256|HAMAP-Rule:MF_01136};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01136};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_01136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01136}; Methanogenesis {ECO:0000256|ARBA:ARBA00022994};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW Rule:MF_01136}; Reference proteome {ECO:0000313|Proteomes:UP000027153};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01136}.
FT DOMAIN 1..60
FT /note="4Fe-4S"
FT /evidence="ECO:0000259|PROSITE:PS51656"
FT BINDING 18
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01136,
FT ECO:0000256|PIRSR:PIRSR000376-2"
FT BINDING 21
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01136,
FT ECO:0000256|PIRSR:PIRSR000376-2"
FT BINDING 26
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01136,
FT ECO:0000256|PIRSR:PIRSR000376-2"
FT BINDING 43
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01136,
FT ECO:0000256|PIRSR:PIRSR000376-2"
FT BINDING 358
FT /ligand="5-methoxybenzimidazolylcob(I)amide"
FT /ligand_id="ChEBI:CHEBI:157765"
FT /evidence="ECO:0000256|PIRSR:PIRSR000376-1"
FT BINDING 364
FT /ligand="5-methoxybenzimidazolylcob(I)amide"
FT /ligand_id="ChEBI:CHEBI:157765"
FT /evidence="ECO:0000256|PIRSR:PIRSR000376-1"
FT BINDING 388..391
FT /ligand="5-methoxybenzimidazolylcob(I)amide"
FT /ligand_id="ChEBI:CHEBI:157765"
FT /evidence="ECO:0000256|PIRSR:PIRSR000376-1"
FT BINDING 453
FT /ligand="5-methoxybenzimidazolylcob(I)amide"
FT /ligand_id="ChEBI:CHEBI:157765"
FT /evidence="ECO:0000256|PIRSR:PIRSR000376-1"
SQ SEQUENCE 469 AA; 52082 MW; F8161E33F5BBAAEC CRC64;
MKLNSPLQVY KYLPQINCAE CGDATCMAFA AHLIDRSKKL EDCPPLLKDE FKKKYLELES
LLAPEVREII VGRGEHAKKI GGDDVLYRHQ LTFFNPTTFA YDVWDTMAEQ ELVDRINNIA
NFRKFYVGKF LKVDMVAVRC VSGDALKFAS AVKKVSETTE LPLVLCSFDP AVLRAALEVV
KDKNPLIYAA TEKNWGEVAE LALNYKVPVV LSSSDLDKLR SLALTFQEMG IKELILDPGT
YPQGKQLKET FERCIKLRRA GIKEGQKDIA LPIMALPLSA WLVYNDAVTA SYWETVLASV
FIVRYADIMI LHGLEPYAML PQVHLRDTIY TDPRTPVKVA PGVNEIGSPT KDSPVIITTN
FALTYYTVES DLSSNKINCY IAAVDTDGIG VEAAVAGGQL TAAKIKDTFQ KAGFDFKEKT
DHSTLILPGL AARLQGDVED VTGLRVMIGP PDSGRIPGWM EKNWPPKPK
//
