ACDB2_METAC
ID ACDB2_METAC Reviewed; 470 AA.
AC Q8TJC4;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Acetyl-CoA decarbonylase/synthase complex subunit beta 2;
DE Short=ACDS complex subunit beta 2;
DE EC=2.3.1.169;
DE AltName: Full=ACDS complex acyltransferase 2;
GN Name=cdhC2; OrderedLocusNames=MA_3862;
OS Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS C2A).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=188937;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX PubMed=11932238; DOI=10.1101/gr.223902;
RA Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT physiological diversity.";
RL Genome Res. 12:532-542(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. The alpha-epsilon complex generates CO from CO(2), while the
CC beta subunit (this protein) combines the CO with CoA and a methyl group
CC to form acetyl-CoA. The methyl group, which is incorporated into
CC acetyl-CoA, is transferred to the beta subunit by a corrinoid iron-
CC sulfur protein (the gamma-delta complex). {ECO:0000255|HAMAP-
CC 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 Note=Binds 1 [Ni-Fe-S] cluster.;
CC -!- PATHWAY: One-carbon metabolism; methanogenesis from acetate.
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) (Potential).
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CdhC family. {ECO:0000305}.
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; AE010299; AAM07213.1; -; Genomic_DNA.
DR RefSeq; WP_011023760.1; NC_003552.1.
DR AlphaFoldDB; Q8TJC4; -.
DR SMR; Q8TJC4; -.
DR STRING; 188937.MA_3862; -.
DR PRIDE; Q8TJC4; -.
DR EnsemblBacteria; AAM07213; AAM07213; MA_3862.
DR GeneID; 1475755; -.
DR KEGG; mac:MA_3862; -.
DR HOGENOM; CLU_613408_0_0_2; -.
DR InParanoid; Q8TJC4; -.
DR OMA; FMHLNQR; -.
DR OrthoDB; 26992at2157; -.
DR PhylomeDB; Q8TJC4; -.
DR UniPathway; UPA00642; -.
DR Proteomes; UP000002487; 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 GO; GO:0019385; P:methanogenesis, from acetate; IEA:UniProtKB-UniRule.
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; Methanogenesis; Nickel;
KW Reference proteome; Transferase.
FT CHAIN 1..470
FT /note="Acetyl-CoA decarbonylase/synthase complex subunit
FT beta 2"
FT /id="PRO_0000155100"
FT BINDING 189
FT /ligand="[Ni-Fe-S] cluster"
FT /ligand_id="ChEBI:CHEBI:60400"
FT /evidence="ECO:0000255"
FT BINDING 192
FT /ligand="[Ni-Fe-S] cluster"
FT /ligand_id="ChEBI:CHEBI:60400"
FT /evidence="ECO:0000255"
FT BINDING 278
FT /ligand="[Ni-Fe-S] cluster"
FT /ligand_id="ChEBI:CHEBI:60400"
FT /evidence="ECO:0000255"
FT BINDING 280
FT /ligand="[Ni-Fe-S] cluster"
FT /ligand_id="ChEBI:CHEBI:60400"
FT /evidence="ECO:0000255"
SQ SEQUENCE 470 AA; 52427 MW; BDBFCAC4D78930A1 CRC64;
MAEFPFEISP MFEGERVRKE GMFVELGGPK SLGLELVRAK PMDEIEDDKV TIVGPDLKEM
EEGKTYPWAM IFNIGGELVE PDLESVVERR VHDFINYCQG IMHLNQRYDV WMRVSKDTAA
KMDSFEPFGQ AVMMLFKTEL PFIEKMQVTF YTEQAEVEKQ LEEAKAIFKA RDERTKDLHD
EDVDVFYGCT LCQSFAPTNV CVVSPDRVSL CGAINWFDGR AAAKVDPEGP QFEITKGDLI
DAEKGEYTGV NDIAKKLSAG EFDKIKLHSF FDAPHTSCGC FEVVGFYIPE VDGIGWVNRE
YQGMAPNGIG FSTMAGQTGG GKQIVGFLGI GINYFYSPKF IQADGGWNRV VWLPSMLKDK
IAETIPEDLK DKIATENDAT DIESLKAFLQ EKGHPVVATW AAAEEEEEEE EEEEEEVAVA
AAPMMMPAAG FQMPAMPMMS GGSSGGIKLT FKNAKITIDK MIISEKKEKK
