ID   ECH17_MYCBO             Reviewed;         261 AA.
AC   Q7TXE1; A0A1R3Y2Z0; X2BMF2;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-MAY-2022, sequence version 2.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Probable enoyl-CoA hydratase EchA17;
DE            EC=4.2.1.17;
GN   Name=echA17; OrderedLocusNames=BQ2027_MB3065C;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND INDUCTION.
RC   STRAIN=BCG / Pasteur;
RX   PubMed=16006064; DOI=10.1016/j.femsle.2005.06.004;
RA   Dosanjh N.S., Rawat M., Chung J.-H., Av-Gay Y.;
RT   "Thiol specific oxidative stress response in Mycobacteria.";
RL   FEMS Microbiol. Lett. 249:87-94(2005).
CC   -!- FUNCTION: Could possibly oxidize fatty acids using specific components.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3S)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O;
CC         Xref=Rhea:RHEA:16105, ChEBI:CHEBI:15377, ChEBI:CHEBI:57318,
CC         ChEBI:CHEBI:58856; EC=4.2.1.17;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 4-saturated-(3S)-3-hydroxyacyl-CoA = a (3E)-enoyl-CoA + H2O;
CC         Xref=Rhea:RHEA:20724, ChEBI:CHEBI:15377, ChEBI:CHEBI:58521,
CC         ChEBI:CHEBI:137480; EC=4.2.1.17;
CC   -!- INDUCTION: Down-regulated in response to the thiol oxidant diamide.
CC       {ECO:0000269|PubMed:16006064}.
CC   -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=SIU01690.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000250|UniProtKB:P9WNN3};
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DR   EMBL; LT708304; SIU01690.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_856710.1; NC_002945.3.
DR   RefSeq; WP_003415942.1; NC_002945.4.
DR   AlphaFoldDB; Q7TXE1; -.
DR   SMR; Q7TXE1; -.
DR   EnsemblBacteria; SIU01690; SIU01690; BQ2027_MB3065C.
DR   GeneID; 45427032; -.
DR   PATRIC; fig|233413.5.peg.3367; -.
DR   OMA; AMEMIMT; -.
DR   Proteomes; UP000001419; Chromosome.
DR   GO; GO:0004300; F:enoyl-CoA hydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.12.10; -; 1.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
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.
PE   1: Evidence at protein level;
KW   Fatty acid metabolism; Lipid metabolism; Lyase.
FT   CHAIN           1..261
FT                   /note="Probable enoyl-CoA hydratase EchA17"
FT                   /id="PRO_0000383562"
FT   SITE            143
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   261 AA;  27178 MW;  40BF00216BEF9DC1 CRC64;
     MAAVTPTVPE FVNVVVSDGS QDAGLAMLLL SRPPTNAMTR QVYREVVAAA NELGRRDDVA
     AVILYGGHEI FSAGDDMPEL RTLSAQEADT AARIRQQAVD AVAAIPKPTV AAITGYALGA
     GLTLALAADW RVSGDNVKFG ATEILAGLIP SGDGMARLTR AAGPSRAKEL VFSGRFFDAE
     EALALGLIDD MVAPDDVYDA AAAWARRFLD GPPHALAAAK AGISDVYELA PAERIAAERR
     RYVEVFAAGQ GGGSKGDRGG R