BCT_SYNWW
ID BCT_SYNWW Reviewed; 447 AA.
AC Q0AVM5;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Probable butyrate:acetyl-CoA coenzyme A-transferase {ECO:0000255|HAMAP-Rule:MF_03228, ECO:0000305|PubMed:23468890};
DE Short=Butyrate CoA-transferase {ECO:0000255|HAMAP-Rule:MF_03228, ECO:0000305|PubMed:23468890};
DE EC=2.8.3.- {ECO:0000255|HAMAP-Rule:MF_03228, ECO:0000305|PubMed:23468890};
GN OrderedLocusNames=Swol_1932;
OS Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Syntrophomonadaceae;
OC Syntrophomonas.
OX NCBI_TaxID=335541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2245B / Goettingen;
RX PubMed=21966920; DOI=10.1111/j.1462-2920.2010.02237.x;
RA Sieber J.R., Sims D.R., Han C., Kim E., Lykidis A., Lapidus A.L.,
RA McDonnald E., Rohlin L., Culley D.E., Gunsalus R., McInerney M.J.;
RT "The genome of Syntrophomonas wolfei: new insights into syntrophic
RT metabolism and biohydrogen production.";
RL Environ. Microbiol. 12:2289-2301(2010).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, INDUCTION, SUBCELLULAR LOCATION,
RP FUNCTION, AND PATHWAY.
RX PubMed=23468890; DOI=10.1371/journal.pone.0056905;
RA Schmidt A., Mueller N., Schink B., Schleheck D.;
RT "A proteomic view at the biochemistry of syntrophic butyrate oxidation in
RT Syntrophomonas wolfei.";
RL PLoS ONE 8:E56905-E56905(2013).
CC -!- FUNCTION: Coenzyme A-transferase that converts butyrate to butyryl-CoA.
CC Involved in the syntrophic growth of S.wolfei on butyrate in
CC cooperation with methanogens or an appropriate hydrogen-scavenging
CC bacterium, as part of the butyrate oxidation pathway.
CC {ECO:0000255|HAMAP-Rule:MF_03228, ECO:0000305|PubMed:23468890}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + butanoate = acetate + butanoyl-CoA;
CC Xref=Rhea:RHEA:30071, ChEBI:CHEBI:17968, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:57371; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03228, ECO:0000305|PubMed:23468890};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30072;
CC Evidence={ECO:0000305|PubMed:23468890};
CC -!- PATHWAY: Lipid metabolism; butanoate metabolism. {ECO:0000255|HAMAP-
CC Rule:MF_03228, ECO:0000305|PubMed:23468890}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03228,
CC ECO:0000269|PubMed:23468890}.
CC -!- INDUCTION: Expressed during syntrophic growth with butyrate (at protein
CC level). Seems to be constitutively expressed.
CC {ECO:0000269|PubMed:23468890}.
CC -!- SIMILARITY: Belongs to the acetyl-CoA hydrolase/transferase family.
CC {ECO:0000255|HAMAP-Rule:MF_03228, ECO:0000305}.
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DR EMBL; CP000448; ABI69229.1; -; Genomic_DNA.
DR RefSeq; WP_011641322.1; NC_008346.1.
DR AlphaFoldDB; Q0AVM5; -.
DR SMR; Q0AVM5; -.
DR STRING; 335541.Swol_1932; -.
DR EnsemblBacteria; ABI69229; ABI69229; Swol_1932.
DR KEGG; swo:Swol_1932; -.
DR eggNOG; COG0427; Bacteria.
DR HOGENOM; CLU_030703_1_0_9; -.
DR OMA; PPDDFGW; -.
DR OrthoDB; 319106at2; -.
DR UniPathway; UPA00863; -.
DR Proteomes; UP000001968; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008775; F:acetate CoA-transferase activity; IEA:InterPro.
DR GO; GO:0003986; F:acetyl-CoA hydrolase activity; IEA:InterPro.
DR GO; GO:0006083; P:acetate metabolic process; IEA:InterPro.
DR GO; GO:0006084; P:acetyl-CoA metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0019605; P:butyrate metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0019679; P:propionate metabolic process, methylcitrate cycle; IEA:InterPro.
DR Gene3D; 3.40.1080.20; -; 1.
DR HAMAP; MF_03228; But_CoA_trans; 1.
DR InterPro; IPR026888; AcetylCoA_hyd_C.
DR InterPro; IPR038460; AcetylCoA_hyd_C_sf.
DR InterPro; IPR003702; ActCoA_hydro.
DR InterPro; IPR023990; Butryl-CoA_acetate_CoA_Tfrase.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR Pfam; PF13336; AcetylCoA_hyd_C; 1.
DR Pfam; PF02550; AcetylCoA_hydro; 1.
DR SUPFAM; SSF100950; SSF100950; 2.
PE 1: Evidence at protein level;
KW Cytoplasm; Fatty acid metabolism; Lipid metabolism; Reference proteome;
KW Transferase.
FT CHAIN 1..447
FT /note="Probable butyrate:acetyl-CoA coenzyme A-transferase"
FT /id="PRO_0000442210"
FT ACT_SITE 245
FT /note="5-glutamyl coenzyme A thioester intermediate"
FT /evidence="ECO:0000250|UniProtKB:B3EY95, ECO:0000255|HAMAP-
FT Rule:MF_03228"
FT BINDING 220..224
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:B3EY95, ECO:0000255|HAMAP-
FT Rule:MF_03228"
FT BINDING 320
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:B3EY95, ECO:0000255|HAMAP-
FT Rule:MF_03228"
FT BINDING 343
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:B3EY95, ECO:0000255|HAMAP-
FT Rule:MF_03228"
SQ SEQUENCE 447 AA; 49841 MW; 8F0BC31D9F187B5D CRC64;
MYQKLLEEYK SKLVTADEAA KQVKSGDWVE YGFGINCARD FDEALAKRKD ELEDVKIRCD
IGAYQHFTAE VDPDNKHFTW NSWHVAGHDR KFINKNLFYI PMKFHENPMM TRKDCVPTNV
AVIQCTAMDK HGYFNFGGSS VNCCAMMETA RVTILEVNEK MPRCLGGNQE CLHISQVDYI
IQSKNEPIAT IGSAEPSPVE IAMAQHIIER LYDGNCIQLG IGGTPNAVGS MVAASDLKDL
GVHTEMYVDA YLLMAKAGKI TGARKSIDKY KQVYSFAMGS QELYDYIDDN PGLASYSVDY
TNNPWVVAQI DDFVSINACI EVDLYGQVCA ESVGTRHISG TGGQLDFVEG AYKSKNGQSF
ICLPSTIEIK GEVTSRIKPI LTPGAIVTDP RTATHMMVTE FGIATLKGRS TWERAEELIK
IAHPDFQDEL VKEAQKMNIW RKSNKIG
