ECHA8_MYCTU
ID ECHA8_MYCTU Reviewed; 257 AA.
AC P9WNN9; L0T5R3; O53418; P64016;
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 echA8;
DE EC=4.2.1.17;
GN Name=echA8; OrderedLocusNames=Rv1070c; ORFNames=MTV017.23c;
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; CCP43821.1; -; Genomic_DNA.
DR PIR; D70893; D70893.
DR RefSeq; NP_215586.1; NC_000962.3.
DR RefSeq; WP_003405712.1; NZ_NVQJ01000072.1.
DR PDB; 3H81; X-ray; 1.80 A; A/B/C=1-257.
DR PDB; 3PZK; X-ray; 2.23 A; A/B/C=1-257.
DR PDB; 3Q0G; X-ray; 2.38 A; A/B/C/D/E/F=1-257.
DR PDB; 3Q0J; X-ray; 2.40 A; A/B/C/D/E/F=1-257.
DR PDB; 4FJW; X-ray; 2.20 A; D/E/F=1-257.
DR PDBsum; 3H81; -.
DR PDBsum; 3PZK; -.
DR PDBsum; 3Q0G; -.
DR PDBsum; 3Q0J; -.
DR PDBsum; 4FJW; -.
DR AlphaFoldDB; P9WNN9; -.
DR SMR; P9WNN9; -.
DR STRING; 83332.Rv1070c; -.
DR PaxDb; P9WNN9; -.
DR DNASU; 887117; -.
DR GeneID; 45425042; -.
DR GeneID; 887117; -.
DR KEGG; mtu:Rv1070c; -.
DR TubercuList; Rv1070c; -.
DR eggNOG; COG1024; Bacteria.
DR OMA; MDMCLSA; -.
DR PhylomeDB; P9WNN9; -.
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 Gene3D; 1.10.12.10; -; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
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.
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..257
FT /note="Probable enoyl-CoA hydratase echA8"
FT /id="PRO_0000109338"
FT STRAND 4..11
FT /evidence="ECO:0007829|PDB:3H81"
FT STRAND 14..19
FT /evidence="ECO:0007829|PDB:3H81"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:3H81"
FT HELIX 30..44
FT /evidence="ECO:0007829|PDB:3H81"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:3H81"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:3H81"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:3H81"
FT HELIX 75..81
FT /evidence="ECO:0007829|PDB:3H81"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:3H81"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:3H81"
FT HELIX 88..91
FT /evidence="ECO:0007829|PDB:3H81"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:3H81"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:3H81"
FT HELIX 108..115
FT /evidence="ECO:0007829|PDB:3H81"
FT STRAND 116..122
FT /evidence="ECO:0007829|PDB:3H81"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:3H81"
FT HELIX 130..134
FT /evidence="ECO:0007829|PDB:3H81"
FT HELIX 142..150
FT /evidence="ECO:0007829|PDB:3H81"
FT HELIX 152..161
FT /evidence="ECO:0007829|PDB:3H81"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:4FJW"
FT HELIX 167..172
FT /evidence="ECO:0007829|PDB:3H81"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:3H81"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:3H81"
FT HELIX 185..197
FT /evidence="ECO:0007829|PDB:3H81"
FT HELIX 201..213
FT /evidence="ECO:0007829|PDB:3H81"
FT TURN 214..216
FT /evidence="ECO:0007829|PDB:3H81"
FT HELIX 219..233
FT /evidence="ECO:0007829|PDB:3H81"
FT HELIX 237..247
FT /evidence="ECO:0007829|PDB:3H81"
SQ SEQUENCE 257 AA; 27273 MW; C8907716969540AA CRC64;
MTYETILVER DQRVGIITLN RPQALNALNS QVMNEVTSAA TELDDDPDIG AIIITGSAKA
FAAGADIKEM ADLTFADAFT ADFFATWGKL AAVRTPTIAA VAGYALGGGC ELAMMCDVLI
AADTAKFGQP EIKLGVLPGM GGSQRLTRAI GKAKAMDLIL TGRTMDAAEA ERSGLVSRVV
PADDLLTEAR ATATTISQMS ASAARMAKEA VNRAFESSLS EGLLYERRLF HSAFATEDQS
EGMAAFIEKR APQFTHR
