ACDB2_METTE
ID ACDB2_METTE Reviewed; 472 AA.
AC Q9V2Z4;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 2.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Acetyl-CoA decarbonylase/synthase complex subunit beta 2;
DE Short=ACDS complex subunit beta 2;
DE EC=2.3.1.169 {ECO:0000269|PubMed:12464601};
DE AltName: Full=ACDS complex acyltransferase 2;
GN Name=cdhC2;
OS Methanosarcina thermophila.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=2210;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, EPR
RP SPECTROSCOPY, CHARACTERIZATION, AND MUTAGENESIS OF CYS-278; CYS-280 AND
RP HIS-394.
RC STRAIN=ATCC 43570 / DSM 1825 / OCM 12 / TM-1;
RX PubMed=12464601; DOI=10.1074/jbc.m210484200;
RA Gencic S., Grahame D.A.;
RT "Nickel in subunit beta of the acetyl-CoA decarbonylase/synthase
RT multienzyme complex in methanogens. Catalytic properties and evidence for a
RT binuclear Ni-Ni site.";
RL J. Biol. Chem. 278:6101-6110(2003).
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).
CC {ECO:0000269|PubMed:12464601}.
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:0000269|PubMed:12464601};
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}.
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DR EMBL; AF173830; AAD51814.2; -; Genomic_DNA.
DR AlphaFoldDB; Q9V2Z4; -.
DR SMR; Q9V2Z4; -.
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; Iron; Iron-sulfur; Metal-binding; Methanogenesis; Nickel;
KW Transferase.
FT CHAIN 1..472
FT /note="Acetyl-CoA decarbonylase/synthase complex subunit
FT beta 2"
FT /id="PRO_0000155107"
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"
FT MUTAGEN 189
FT /note="C->S: Loss of ability to bind iron."
FT MUTAGEN 278
FT /note="C->S: Loss of ability to bind nickel; loss of
FT activity."
FT /evidence="ECO:0000269|PubMed:12464601"
FT MUTAGEN 280
FT /note="C->S: Loss of ability to bind nickel; loss of
FT activity."
FT /evidence="ECO:0000269|PubMed:12464601"
FT MUTAGEN 394
FT /note="H->N: No effect on nickel binding."
FT /evidence="ECO:0000269|PubMed:12464601"
SQ SEQUENCE 472 AA; 52687 MW; EF5626BCFB84D865 CRC64;
MSEFPFEISP MFEGERVRKE GMFVELGGPK SLGLELVRAK PMDEIEDGKV TIVGPDLKDM
EEGKTYPWAM IFHVGGELVE PDLESVIERR VHDFINYCQG IMHLNQRYDV WMRISKDTAA
KMDSFEPFGK AVMMLFKTEL PFIEKMQVTF YTDQAEVEKQ MAEAMEIFKA RDARTKDLHD
EDVDVFYGCT LCQSFAPTNV CVVSPDRVSL CGAINWFDGR AAAKVDPEGP QFAIEKGELL
DAKTGEYSGV NEVAKKLSSG EFDKIKLHSF FDAPHTSCGC FEDVGFYIPE VDGIGWVNRE
YQGMAPNGLG FSTMAGQTGG GKQIVGFLGI GINYFYSPKF IQADGGWNRV VWLPSMLKEK
IDEAIPDDMK DKIATEKDVT DIESLKTFLK EKNHPVVANW AAEAEEEEEE EGEEEEVAAE
AAPMMMPAAG FQMPAMPAMP MMSGGAGGIK LTFKNAKITI DRMIISEKKE KK
