ACDB_ARCFU
ID ACDB_ARCFU Reviewed; 524 AA.
AC O29868;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 112.
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, ECO:0000269|PubMed:9575239};
DE AltName: Full=ACDS complex acyltransferase {ECO:0000255|HAMAP-Rule:MF_01138};
GN Name=cdhC {ECO:0000255|HAMAP-Rule:MF_01138}; OrderedLocusNames=AF_0379;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP PROTEIN SEQUENCE OF 2-23, FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9575239; DOI=10.1007/s002030050606;
RA Dai Y.R., Reed D.W., Millstein J.H., Hartzell P.L., Grahame D.A.,
RA DeMoll E.;
RT "Acetyl-CoA decarbonylase/synthase complex from Archaeoglobus fulgidus.";
RL Arch. Microbiol. 169:525-529(1998).
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 ECO:0000269|PubMed:9575239}.
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 ECO:0000269|PubMed:9575239};
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; AE000782; AAB90857.1; -; Genomic_DNA.
DR PIR; C69297; C69297.
DR RefSeq; WP_010877886.1; NC_000917.1.
DR AlphaFoldDB; O29868; -.
DR SMR; O29868; -.
DR STRING; 224325.AF_0379; -.
DR PRIDE; O29868; -.
DR EnsemblBacteria; AAB90857; AAB90857; AF_0379.
DR GeneID; 24793918; -.
DR KEGG; afu:AF_0379; -.
DR eggNOG; arCOG04360; Archaea.
DR HOGENOM; CLU_613408_0_0_2; -.
DR OMA; YIEGIMH; -.
DR OrthoDB; 26992at2157; -.
DR PhylomeDB; O29868; -.
DR BioCyc; MetaCyc:AF_RS01935-MON; -.
DR Proteomes; UP000002199; 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 1: Evidence at protein level;
KW Acyltransferase; Direct protein sequencing; Iron; Iron-sulfur;
KW Metal-binding; Nickel; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9575239"
FT CHAIN 2..524
FT /note="Acetyl-CoA decarbonylase/synthase complex subunit
FT beta"
FT /id="PRO_0000155098"
FT REGION 436..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 212
FT /ligand="[Ni-Fe-S] cluster"
FT /ligand_id="ChEBI:CHEBI:60400"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01138"
FT BINDING 215
FT /ligand="[Ni-Fe-S] cluster"
FT /ligand_id="ChEBI:CHEBI:60400"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01138"
FT BINDING 301
FT /ligand="[Ni-Fe-S] cluster"
FT /ligand_id="ChEBI:CHEBI:60400"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01138"
FT BINDING 303
FT /ligand="[Ni-Fe-S] cluster"
FT /ligand_id="ChEBI:CHEBI:60400"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01138"
SQ SEQUENCE 524 AA; 58576 MW; 634ACE1C34A83F6A CRC64;
MVERKRIEIP EGVKVKESVG EEAEFPFDIS PMYEGERIRK GDMYVELGGP TQPGFELVMA
LPMDQVEDMK VTLIGPDLDE MEEGQAYPYA MIYYIAGEMV ETDLEPVIER RNHDFQNYIE
GYMHLNQRYD IWIRIGKNAI KKGLKSLIQI AKATMMLYKN ELPFIEKIEA VYITDKDLVE
KLLNELAMPI FEERDARVEA LSDEDVDEFY SCTLCQSFAP TNVCIVSPDR PSLCGAITWF
DGRAAAKVDP EGPNRAVPKG ELLDPIGGEY SGVNEFAKQE SGGEYERIKL HSFFEYPHTS
CGCFEVIGFY MPEVDGIGWV HRGYAEPAPN GLTFSTMAGQ TGGGKQVVGF LGIGIAYFRS
KKFIQADGGW YRTVWMPKEL KERVAKYIPD DIRDKIATEE DAKTLDELRE FLKKVDHPVV
KGVVRPVDGK KITNGWVEEE EEEAEEVAEE AAAEAAPAAQ PAQAAQPMAM QPMPMQMPGF
QLPALQMPAA SAAPAGVKLV IKDAKITIEK VIIKKAEKEK KGGK
