ECHA6_MYCTU
ID ECHA6_MYCTU Reviewed; 243 AA.
AC P9WNP1; L0T7V5; P64014; Q10533;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Probable enoyl-CoA hydratase echA6;
DE EC=4.2.1.17;
GN Name=echA6; OrderedLocusNames=Rv0905; ORFNames=MTCY31.33;
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; CCP43653.1; -; Genomic_DNA.
DR PIR; F70783; F70783.
DR RefSeq; NP_215420.1; NC_000962.3.
DR RefSeq; WP_003404702.1; NZ_NVQJ01000001.1.
DR PDB; 3HE2; X-ray; 2.30 A; A/B/C=1-243.
DR PDB; 5DTP; X-ray; 1.91 A; A/B/C=1-243.
DR PDB; 5DTW; X-ray; 2.44 A; A/B/C/D/E/F=1-243.
DR PDB; 5DU4; X-ray; 1.70 A; A=1-243.
DR PDB; 5DU6; X-ray; 2.61 A; A/B/C=1-243.
DR PDB; 5DU8; X-ray; 2.23 A; A/B/C=1-243.
DR PDB; 5DUC; X-ray; 2.70 A; A/B/C=1-243.
DR PDB; 5DUF; X-ray; 1.50 A; A=1-243.
DR PDBsum; 3HE2; -.
DR PDBsum; 5DTP; -.
DR PDBsum; 5DTW; -.
DR PDBsum; 5DU4; -.
DR PDBsum; 5DU6; -.
DR PDBsum; 5DU8; -.
DR PDBsum; 5DUC; -.
DR PDBsum; 5DUF; -.
DR AlphaFoldDB; P9WNP1; -.
DR SMR; P9WNP1; -.
DR STRING; 83332.Rv0905; -.
DR PaxDb; P9WNP1; -.
DR DNASU; 885825; -.
DR GeneID; 885825; -.
DR KEGG; mtu:Rv0905; -.
DR TubercuList; Rv0905; -.
DR eggNOG; COG1024; Bacteria.
DR OMA; MHALPRI; -.
DR PhylomeDB; P9WNP1; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0004300; F:enoyl-CoA hydratase activity; IBA:GO_Central.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
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 3D-structure; Fatty acid metabolism; Lipid metabolism; Lyase;
KW Reference proteome.
FT CHAIN 1..243
FT /note="Probable enoyl-CoA hydratase echA6"
FT /id="PRO_0000109335"
FT STRAND 1..7
FT /evidence="ECO:0007829|PDB:5DUF"
FT STRAND 10..15
FT /evidence="ECO:0007829|PDB:5DUF"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:5DUF"
FT HELIX 26..37
FT /evidence="ECO:0007829|PDB:5DUF"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:5DUF"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:5DUF"
FT STRAND 46..54
FT /evidence="ECO:0007829|PDB:5DUF"
FT TURN 62..67
FT /evidence="ECO:0007829|PDB:5DTW"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:5DUF"
FT HELIX 71..84
FT /evidence="ECO:0007829|PDB:5DUF"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:5DUF"
FT HELIX 100..107
FT /evidence="ECO:0007829|PDB:5DUF"
FT STRAND 108..113
FT /evidence="ECO:0007829|PDB:5DUF"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:5DUF"
FT HELIX 123..126
FT /evidence="ECO:0007829|PDB:5DUF"
FT HELIX 132..142
FT /evidence="ECO:0007829|PDB:5DUF"
FT HELIX 144..153
FT /evidence="ECO:0007829|PDB:5DUF"
FT HELIX 159..165
FT /evidence="ECO:0007829|PDB:5DUF"
FT STRAND 166..171
FT /evidence="ECO:0007829|PDB:5DUF"
FT HELIX 174..184
FT /evidence="ECO:0007829|PDB:5DUF"
FT HELIX 189..200
FT /evidence="ECO:0007829|PDB:5DUF"
FT TURN 201..204
FT /evidence="ECO:0007829|PDB:5DTW"
FT HELIX 210..220
FT /evidence="ECO:0007829|PDB:5DUF"
FT HELIX 223..233
FT /evidence="ECO:0007829|PDB:5DUF"
SQ SEQUENCE 243 AA; 26029 MW; 23BD1153F0159991 CRC64;
MIGITQAEAV LTIELQRPER RNALNSQLVE ELTQAIRKAG DGSARAIVLT GQGTAFCAGA
DLSGDAFAAD YPDRLIELHK AMDASPMPVV GAINGPAIGA GLQLAMQCDL RVVAPDAFFQ
FPTSKYGLAL DNWSIRRLSS LVGHGRARAM LLSAEKLTAE IALHTGMANR IGTLADAQAW
AAEIARLAPL AIQHAKRVLN DDGAIEEAWP AHKELFDKAW GSQDVIEAQV ARMEKRPPKF
QGA
