ECH14_MYCBO
ID ECH14_MYCBO Reviewed; 256 AA.
AC P64019; A0A1R3Y1Q4; O53211; X2BL76;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Probable enoyl-CoA hydratase echA14;
DE EC=4.2.1.17;
GN Name=echA14; OrderedLocusNames=BQ2027_MB2511;
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: Induced 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}.
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DR EMBL; LT708304; SIU01127.1; -; Genomic_DNA.
DR RefSeq; NP_856158.1; NC_002945.3.
DR RefSeq; WP_003412728.1; NC_002945.4.
DR AlphaFoldDB; P64019; -.
DR SMR; P64019; -.
DR EnsemblBacteria; SIU01127; SIU01127; BQ2027_MB2511.
DR PATRIC; fig|233413.5.peg.2764; -.
DR OMA; WERFEND; -.
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 InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR InterPro; IPR001753; Enoyl-CoA_hydra/iso.
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 Fatty acid metabolism; Lipid metabolism; Lyase.
FT CHAIN 1..256
FT /note="Probable enoyl-CoA hydratase echA14"
FT /id="PRO_0000109342"
FT REGION 235..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 256 AA; 26280 MW; EB314ABF51113AED CRC64;
MAQYDPVLLS VDKHVALITV NDPDRRNAVT DEMSAQLRAA IQRAEGDPDV HAVVVTGAGK
AFCAGADLSA LGAGVGDPAE PRLLRLYDGF MAVSSCNLPT IAAVNGAAVG AGLNLALAAD
VRIAGPAALF DARFQKLGLH PGGGATWMLQ RAVGPQVARA ALLFGMCFDA ESAVRHGLAL
MVADDPVTAA LELAAGPAAA PREVVLASKA TMRATASPGS LDLEQHELAK RLELGPQAKS
VQSPEFAARL AAAQHR
