ID   CRCH_SYNWW              Reviewed;         260 AA.
AC   Q0AVM1;
DT   25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Crotonyl-CoA hydratase {ECO:0000303|PubMed:23468890};
DE            EC=4.2.1.150 {ECO:0000305|PubMed:23468890};
GN   OrderedLocusNames=Swol_1936 {ECO:0000312|EMBL:ABI69233.1};
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: Involved in syntrophic growth of S.wolfei with butyrate, as
CC       part of the butyrate oxidation pathway. Probably catalyzes the
CC       hydration of crotonyl-CoA to 3-hydroxybutyryl-CoA.
CC       {ECO:0000305|PubMed:23468890}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-hydroxybutanoyl-CoA = (2E)-butenoyl-CoA + H2O;
CC         Xref=Rhea:RHEA:45584, ChEBI:CHEBI:15377, ChEBI:CHEBI:57332,
CC         ChEBI:CHEBI:78611; Evidence={ECO:0000305|PubMed:23468890};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a short-chain (3S)-3-hydroxyacyl-CoA = a short-chain (2E)-
CC         enoyl-CoA + H2O; Xref=Rhea:RHEA:52664, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:87488, ChEBI:CHEBI:136760; EC=4.2.1.150;
CC         Evidence={ECO:0000305|PubMed:23468890};
CC   -!- PATHWAY: Lipid metabolism; butanoate metabolism.
CC       {ECO:0000305|PubMed:23468890}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P52046}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23468890}.
CC   -!- INDUCTION: Highly expressed during syntrophic growth with butyrate (at
CC       protein level). Seems to be constitutively expressed.
CC       {ECO:0000269|PubMed:23468890}.
CC   -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; CP000448; ABI69233.1; -; Genomic_DNA.
DR   RefSeq; WP_011641326.1; NC_008346.1.
DR   AlphaFoldDB; Q0AVM1; -.
DR   SMR; Q0AVM1; -.
DR   STRING; 335541.Swol_1936; -.
DR   PRIDE; Q0AVM1; -.
DR   EnsemblBacteria; ABI69233; ABI69233; Swol_1936.
DR   KEGG; swo:Swol_1936; -.
DR   eggNOG; COG1024; Bacteria.
DR   HOGENOM; CLU_009834_7_6_9; -.
DR   OMA; GLRFERH; -.
DR   OrthoDB; 1498685at2; -.
DR   UniPathway; UPA00863; -.
DR   Proteomes; UP000001968; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0120092; F:crotonyl-CoA hydratase activity; IEA:RHEA.
DR   GO; GO:0019605; P:butyrate metabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.12.10; -; 1.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR   InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR   InterPro; IPR014748; Enoyl-CoA_hydra_C.
DR   Pfam; PF00378; ECH_1; 1.
DR   SUPFAM; SSF52096; SSF52096; 1.
DR   PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Fatty acid metabolism; Lipid metabolism; Lyase;
KW   Reference proteome.
FT   CHAIN           1..260
FT                   /note="Crotonyl-CoA hydratase"
FT                   /id="PRO_0000442215"
FT   ACT_SITE        114
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q5LLW6"
FT   ACT_SITE        134
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q5LLW6"
SQ   SEQUENCE   260 AA;  27944 MW;  A52D1637D982807E CRC64;
     MAYENIILEK EEKLAVLYIN RPKAMNALNK DTLLEIKDAV TAVNDDPAVE LLIITGSGDK
     SFVAGADIAF MQNLSAMEAR EFGALGQKVF RLIEAMEKPV IAAVNGFALG GGCELAMCCD
     FRIAASNAKF GQPEVGLGIT PGFGGTQRLP RLVGPGMAKQ LLYTADVINA DEAFRIGLVN
     KVVQPEELLP EVKKIAGRIL SKGQLAVRLS KAAANEGMQT DIDRAMSIEA DAFGLCFATQ
     DQKEGMTAFL EKRKANFISK