ACDB1_METTE
ID ACDB1_METTE Reviewed; 469 AA.
AC P72021;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Acetyl-CoA decarbonylase/synthase complex subunit beta 1;
DE Short=ACDS complex subunit beta 1;
DE EC=2.3.1.169 {ECO:0000255|HAMAP-Rule:MF_01138};
DE AltName: Full=ACDS complex acyltransferase 1;
GN Name=cdhC1;
OS Methanosarcina thermophila.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=2210;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-26.
RC STRAIN=ATCC 43570 / DSM 1825 / OCM 12 / TM-1;
RX PubMed=8955306; DOI=10.1128/jb.178.23.6849-6856.1996;
RA Maupin-Furlow J.A., Ferry J.G.;
RT "Analysis of the CO dehydrogenase/acetyl-Coenzyme A synthase operon of
RT Methanosarcina thermophila.";
RL J. Bacteriol. 178:6849-6856(1996).
RN [2]
RP COFACTOR, AND EPR SPECTROSCOPY.
RX PubMed=8380157; DOI=10.1016/s0021-9258(18)54153-3;
RA Jablonski P.E., Lu W.P., Ragsdale S.W., Ferry J.G.;
RT "Characterization of the metal centers of the corrinoid/iron-sulfur
RT component of the CO dehydrogenase enzyme complex from Methanosarcina
RT thermophila by EPR spectroscopy and spectroelectrochemistry.";
RL J. Biol. Chem. 268:325-329(1993).
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 Evidence={ECO:0000269|PubMed:8380157};
CC Note=Binds 1 [Ni-Fe-S] cluster. {ECO:0000269|PubMed:8380157};
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}.
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DR EMBL; U66032; AAC44652.1; -; Genomic_DNA.
DR AlphaFoldDB; P72021; -.
DR SMR; P72021; -.
DR KEGG; ag:AAC44652; -.
DR BioCyc; MetaCyc:CDHCMSARC-MON; -.
DR BRENDA; 2.3.1.169; 3281.
DR UniPathway; UPA00642; -.
DR GO; GO:0016407; F:acetyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0018492; F:carbon-monoxide dehydrogenase (acceptor) activity; IDA:MENGO.
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 1: Evidence at protein level;
KW Acyltransferase; Direct protein sequencing; Iron; Iron-sulfur;
KW Metal-binding; Methanogenesis; Nickel; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8955306"
FT CHAIN 2..469
FT /note="Acetyl-CoA decarbonylase/synthase complex subunit
FT beta 1"
FT /id="PRO_0000155106"
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 469 AA; 51882 MW; 3C797F3BB373C8FE CRC64;
MAEFPFEISP MFEGERVRKE GMFVELGGPK SLGLELVRAA DMDAIEDDKV TIVGPDLKDM
EEGKTYPWAM IFNIGGELVE PDLESVVERR VHDFINYCQG IMHLNQRYDV WMRVSKDTAG
KMDSFEPFGK AVMMLFKTEL PFIEKMQVTF YTGKEEVEKQ MELAKEIFKA RDARTKDLHD
EDVDVFYGCT LCQSFAPTNV CVVSPDRISL CGAINWFDGR AAAKVDPEGP QFEIAKGDLL
DAVTGEYTGV NEIAKKLSSG EFDKIKLHSF FDSPHTSCGC FEVVGFYIPE VDGIGWVDRE
YQGMAPNGIG FSTMAGQTGG GKQIVGFLGI GVNYFYSPKF IQADGGWNRV VWLPSGLKAK
IDEAIPADLK DKIATENDAT DIASLKDFLE AKNHPVVATW AAAEEEEEEE EEEEEVAVAA
APMMMPAAGF QMPAMPMMSG GSGGGIKLTF KNAKITIDKL VISEKKEKK
