ECH14_MYCTU
ID ECH14_MYCTU Reviewed; 256 AA.
AC P9WNN5; L0T9S3; O53211; P64018;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 40.
DE RecName: Full=Probable enoyl-CoA hydratase echA14;
DE EC=4.2.1.17;
GN Name=echA14; OrderedLocusNames=Rv2486; ORFNames=MTV008.42;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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 -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP45280.1; -; Genomic_DNA.
DR PIR; E70868; E70868.
DR RefSeq; NP_217002.1; NC_000962.3.
DR RefSeq; WP_003412728.1; NZ_NVQJ01000067.1.
DR AlphaFoldDB; P9WNN5; -.
DR SMR; P9WNN5; -.
DR STRING; 83332.Rv2486; -.
DR PaxDb; P9WNN5; -.
DR DNASU; 887894; -.
DR GeneID; 887894; -.
DR KEGG; mtu:Rv2486; -.
DR TubercuList; Rv2486; -.
DR eggNOG; COG1024; Bacteria.
DR OMA; WERFEND; -.
DR PhylomeDB; P9WNN5; -.
DR Proteomes; UP000001584; 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; Reference proteome.
FT CHAIN 1..256
FT /note="Probable enoyl-CoA hydratase echA14"
FT /id="PRO_0000109343"
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