ACDG_METKA
ID ACDG_METKA Reviewed; 462 AA.
AC Q8TXF1;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=MK0723;
OS Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC Methanopyrus.
OX NCBI_TaxID=190192;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX PubMed=11930014; DOI=10.1073/pnas.032671499;
RA Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA Koonin E.V., Kozyavkin S.A.;
RT "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT monophyly of archaeal methanogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
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}.
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DR EMBL; AE009439; AAM01937.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8TXF1; -.
DR SMR; Q8TXF1; -.
DR STRING; 190192.MK0723; -.
DR EnsemblBacteria; AAM01937; AAM01937; MK0723.
DR KEGG; mka:MK0723; -.
DR PATRIC; fig|190192.8.peg.764; -.
DR HOGENOM; CLU_050002_0_0_2; -.
DR OMA; SCMAFAT; -.
DR Proteomes; UP000001826; 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..462
FT /note="Acetyl-CoA decarbonylase/synthase complex subunit
FT gamma"
FT /id="PRO_0000155121"
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 462 AA; 50852 MW; 1E97B54407368D3B CRC64;
MAQLSAMDVY NLLPKANCGA CGCKTCMEFA TKLVNREAKP EDCPKLDDES LEKLQELLAP
PVKELTIGEG DREVTVGGDE VMFRHELSFF NPPPVFVTVY DDMEEDEIAG KTEEIQEFQV
ERVGEVLKLD GVAVVSRTGD PEKYARAVEI AVERSEDLAV ALITTDPKVM EAGLDVFDER
PLLYPATEEN VEDLAKLAAD GDCPLGLHAR DVEDLVPLVV EAQQYTDDLL LDPGTEFGPH
DVVSTTDKLA EIRKAAIEEF ESFGYPTLVT TFPYAFLEDD PVKAARRESY LASACVLRYA
DILIMDTVEP WALLPVLTQR QCVYTDPREP QEVEPGLYRI GDPDENSPVL VTTNFTLTYH
CVAGDLESAD IDCWLLVIDT GGLAVDVSVA GGQFTGEAVK EVIEETDIED KVEHRVLVIP
GKAAAVKGDV EDATGWDVMI GTQDSSELPE FLEKEGLLRI EE
