ACDB_METKA
ID ACDB_METKA Reviewed; 467 AA.
AC Q8TXF4;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Acetyl-CoA decarbonylase/synthase complex subunit beta {ECO:0000255|HAMAP-Rule:MF_01138};
DE Short=ACDS complex subunit beta {ECO:0000255|HAMAP-Rule:MF_01138};
DE EC=2.3.1.169 {ECO:0000255|HAMAP-Rule:MF_01138};
DE AltName: Full=ACDS complex acyltransferase {ECO:0000255|HAMAP-Rule:MF_01138};
GN Name=cdhC {ECO:0000255|HAMAP-Rule:MF_01138}; OrderedLocusNames=MK0720;
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). The alpha-epsilon
CC complex generates CO from CO(2), while the beta subunit (this protein)
CC combines the CO with CoA and a methyl group to form acetyl-CoA. The
CC methyl group, which is incorporated into acetyl-CoA, is transferred to
CC the beta subunit by a corrinoid iron-sulfur protein (the gamma-delta
CC complex). {ECO:0000255|HAMAP-Rule:MF_01138}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + Co(I)-[corrinoid Fe-S protein] + H(+) = CO + CoA
CC + methyl-Co(III)-[corrinoid Fe-S protein]; Xref=Rhea:RHEA:45212,
CC Rhea:RHEA-COMP:11110, Rhea:RHEA-COMP:11111, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17245, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:85033, ChEBI:CHEBI:85035; EC=2.3.1.169;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01138};
CC -!- COFACTOR:
CC Name=[Ni-Fe-S] cluster; Xref=ChEBI:CHEBI:60400;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01138};
CC Note=Binds 1 [Ni-Fe-S] cluster. {ECO:0000255|HAMAP-Rule:MF_01138};
CC -!- SUBUNIT: Monomer. The ACDS complex is made up of alpha, epsilon, beta,
CC gamma and delta chains with a probable stoichiometry of
CC (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8).
CC {ECO:0000255|HAMAP-Rule:MF_01138}.
CC -!- SIMILARITY: Belongs to the CdhC family. {ECO:0000255|HAMAP-
CC Rule:MF_01138}.
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DR EMBL; AE009439; AAM01934.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8TXF4; -.
DR SMR; Q8TXF4; -.
DR STRING; 190192.MK0720; -.
DR EnsemblBacteria; AAM01934; AAM01934; MK0720.
DR KEGG; mka:MK0720; -.
DR PATRIC; fig|190192.8.peg.761; -.
DR HOGENOM; CLU_613408_0_0_2; -.
DR OMA; FMHLNQR; -.
DR Proteomes; UP000001826; Chromosome.
DR GO; GO:0016407; F:acetyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0018492; F:carbon-monoxide dehydrogenase (acceptor) activity; IEA:InterPro.
DR GO; GO:0043884; F:CO-methylating acetyl-CoA synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0016151; F:nickel cation binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006084; P:acetyl-CoA metabolic process; IEA:InterPro.
DR Gene3D; 3.30.1650.10; -; 1.
DR HAMAP; MF_01138; CdhC; 1.
DR InterPro; IPR045822; ACS_CODH_B_C.
DR InterPro; IPR004461; CO_DH/Ac-CoA_synth_bsu.
DR InterPro; IPR038571; CO_DH/Ac-CoA_synth_bsu_3_sf.
DR InterPro; IPR023432; CO_DH/Ac-CoA_synth_bsu_arc.
DR InterPro; IPR011254; Prismane-like_sf.
DR PANTHER; PTHR42281; PTHR42281; 1.
DR Pfam; PF19436; ACS_CODH_B_C; 1.
DR Pfam; PF03598; CdhC; 1.
DR SUPFAM; SSF56821; SSF56821; 1.
DR TIGRFAMs; TIGR00316; cdhC; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Iron; Iron-sulfur; Metal-binding; Nickel;
KW Reference proteome; Transferase.
FT CHAIN 1..467
FT /note="Acetyl-CoA decarbonylase/synthase complex subunit
FT beta"
FT /id="PRO_0000155103"
FT REGION 403..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..419
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 193
FT /ligand="[Ni-Fe-S] cluster"
FT /ligand_id="ChEBI:CHEBI:60400"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01138"
FT BINDING 196
FT /ligand="[Ni-Fe-S] cluster"
FT /ligand_id="ChEBI:CHEBI:60400"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01138"
FT BINDING 282
FT /ligand="[Ni-Fe-S] cluster"
FT /ligand_id="ChEBI:CHEBI:60400"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01138"
FT BINDING 284
FT /ligand="[Ni-Fe-S] cluster"
FT /ligand_id="ChEBI:CHEBI:60400"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01138"
SQ SEQUENCE 467 AA; 53016 MW; D8D30B08C2440AD3 CRC64;
MTSLADLPVD VSPRHEGERI RSGDMYVELA GPKSFGAELF KVVDPDEIEP DKVEVIGPDI
DEMEEGGRYP FAIYVKAAGE ELEEDVEGVL ERRIHEFCNY VEGFMHLNQR DQIWCRVSKN
VTEKGFRLEH LGIALRELYK EEFGNVIDSV EVTIMTDEEK VEEFLEYARR VYKKRDERAK
GLSEEDVNEF YVCLMCQSFA PTHVCVITPD RPSLCGSITW HDAKAAYKID PEGPIFPIEK
GECLDPEAGE YEGVNEAVKE HSQGTVERVY LHSCLEYPHT SCGCFQAVVF YIPEVDGFGI
VDREYPGETP IGLPFSTMAG EASGGEQQPG FVGVSYGYME SDKFLQYDGG WERVVWMPKA
LKERMKHAIP DELYDKIATE EDATTVEELR EFLEKVEHPV VERWAEEEEE EEEKAPEEEA
PAEEPTMEVK ELPIAPGGGL NVKIVLKNAK IYAEKVIIKR ADREDKS
