ID   CROR_METEA              Reviewed;         157 AA.
AC   C5AZ74; Q8RP95;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=3-hydroxybutyryl-CoA dehydratase;
DE            EC=4.2.1.55 {ECO:0000305|PubMed:11872727};
DE   AltName: Full=R-specific crotonase {ECO:0000303|PubMed:11872727};
GN   Name=croR {ECO:0000303|PubMed:11872727};
GN   OrderedLocusNames=MexAM1_META1p3675;
OS   Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB
OS   9133 / AM1) (Methylobacterium extorquens).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Methylobacteriaceae; Methylorubrum.
OX   NCBI_TaxID=272630;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1;
RX   PubMed=11872727; DOI=10.1128/jb.184.6.1750-1758.2002;
RA   Korotkova N., Chistoserdova L., Kuksa V., Lidstrom M.E.;
RT   "Glyoxylate regeneration pathway in the methylotroph Methylobacterium
RT   extorquens AM1.";
RL   J. Bacteriol. 184:1750-1758(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1;
RX   PubMed=19440302; DOI=10.1371/journal.pone.0005584;
RA   Vuilleumier S., Chistoserdova L., Lee M.-C., Bringel F., Lajus A., Zhou Y.,
RA   Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C., Gillett W.,
RA   Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S., Muller E.,
RA   Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G., Roche D.,
RA   Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z., Marx C.J.,
RA   Vorholt J.A., Olson M.V., Kaul R., Weissenbach J., Medigue C.,
RA   Lidstrom M.E.;
RT   "Methylobacterium genome sequences: a reference blueprint to investigate
RT   microbial metabolism of C1 compounds from natural and industrial sources.";
RL   PLoS ONE 4:E5584-E5584(2009).
CC   -!- FUNCTION: Involved in the regeneration of glyoxylate from a molecule of
CC       acetyl-CoA. {ECO:0000269|PubMed:11872727}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3R)-3-hydroxybutanoyl-CoA = (2E)-butenoyl-CoA + H2O;
CC         Xref=Rhea:RHEA:17849, ChEBI:CHEBI:15377, ChEBI:CHEBI:57315,
CC         ChEBI:CHEBI:57332; EC=4.2.1.55;
CC         Evidence={ECO:0000305|PubMed:11872727};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17850;
CC         Evidence={ECO:0000305|PubMed:11872727};
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene lose the ability to grow
CC       on C1 (methanol and methylamine) and C2 (ethanol and ethylamine)
CC       compounds. {ECO:0000269|PubMed:11872727}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF416777; AAL86732.1; -; Genomic_DNA.
DR   EMBL; CP001510; ACS41386.1; -; Genomic_DNA.
DR   RefSeq; WP_003606989.1; NC_012988.1.
DR   AlphaFoldDB; C5AZ74; -.
DR   SMR; C5AZ74; -.
DR   STRING; 272630.MexAM1_META1p3675; -.
DR   EnsemblBacteria; ACS41386; ACS41386; MexAM1_META1p3675.
DR   KEGG; mea:Mex_1p3675; -.
DR   eggNOG; COG2030; Bacteria.
DR   HOGENOM; CLU_094876_3_3_5; -.
DR   OMA; PGPGCIY; -.
DR   OrthoDB; 1563802at2; -.
DR   Proteomes; UP000009081; Chromosome.
DR   GO; GO:0005835; C:fatty acid synthase complex; IEA:InterPro.
DR   GO; GO:0003859; F:3-hydroxybutyryl-CoA dehydratase activity; IMP:UniProtKB.
DR   GO; GO:0004312; F:fatty acid synthase activity; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   GO; GO:0046487; P:glyoxylate metabolic process; IMP:UniProtKB.
DR   InterPro; IPR003965; Fatty_acid_synthase.
DR   InterPro; IPR029069; HotDog_dom_sf.
DR   InterPro; IPR002539; MaoC-like_dom.
DR   Pfam; PF01575; MaoC_dehydratas; 1.
DR   PRINTS; PR01483; FASYNTHASE.
DR   SUPFAM; SSF54637; SSF54637; 1.
PE   4: Predicted;
KW   Lyase.
FT   CHAIN           1..157
FT                   /note="3-hydroxybutyryl-CoA dehydratase"
FT                   /id="PRO_0000428883"
FT   DOMAIN          22..120
FT                   /note="MaoC-like"
SQ   SEQUENCE   157 AA;  17009 MW;  28B20B88F9F3CE2F CRC64;
     MLPELRVLYF EDLEVGLTEI LKKEISSSDV VGFAEITGDR NPIHLSEHFA ARTPFGTRIA
     HGLYTAGLIS AVLGTRLPGP GAVYISQTLN FRAPVRIGDI VEVKVEVAEL IPERRRARLA
     CTCSVGDEVV LDGEALVKVP KKEEADPLAM RMGGGRA