EPHA_MYCTU
ID EPHA_MYCTU Reviewed; 322 AA.
AC I6YGS0;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Epoxide hydrolase A {ECO:0000303|PubMed:16511284};
DE Short=EHB {ECO:0000303|PubMed:16511284};
DE EC=3.3.2.10 {ECO:0000250|UniProtKB:P95276};
DE AltName: Full=Epoxide hydrolase EphA {ECO:0000303|PubMed:16511284};
GN Name=ephA; OrderedLocusNames=Rv3617;
GN ORFNames=LH57_19705 {ECO:0000312|EMBL:AIR16405.1};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27294 / TMC 102 / H37Rv;
RA Hazbon M.H., Riojas M.A., Damon A.M., Alalade R.O., Cantwell B.J.,
RA Monaco A., King S., Sohrabi A.;
RT "Phylogenetic analysis of Mycobacterial species using whole genome
RT sequences.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION.
RX PubMed=16511284; DOI=10.1107/s1744309106000637;
RA Biswal B.K., Garen G., Cherney M.M., Garen C., James M.N.;
RT "Cloning, expression, purification, crystallization and preliminary X-ray
RT studies of epoxide hydrolases A and B from Mycobacterium tuberculosis.";
RL Acta Crystallogr. F 62:136-138(2006).
RN [4]
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 be involved in detoxification of extraneous host-cell
CC epoxides. Catalyzes the hydrolysis of epoxide-containing substrates.
CC {ECO:0000305|PubMed:16511284}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an epoxide + H2O = an ethanediol; Xref=Rhea:RHEA:19037,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:32955, ChEBI:CHEBI:140594;
CC EC=3.3.2.10; Evidence={ECO:0000250|UniProtKB:P95276};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P95276}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Epoxide hydrolase
CC family. {ECO:0000305}.
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DR EMBL; CP009480; AIR16405.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP46440.1; -; Genomic_DNA.
DR RefSeq; NP_218134.1; NC_000962.3.
DR RefSeq; WP_003899600.1; NZ_NVQJ01000056.1.
DR AlphaFoldDB; I6YGS0; -.
DR SMR; I6YGS0; -.
DR STRING; 83332.Rv3617; -.
DR ESTHER; myctu-ephA; Epoxide_hydrolase.
DR MEROPS; S33.973; -.
DR PaxDb; I6YGS0; -.
DR PRIDE; I6YGS0; -.
DR DNASU; 885769; -.
DR GeneID; 45427603; -.
DR GeneID; 885769; -.
DR KEGG; mtu:Rv3617; -.
DR PATRIC; fig|83332.111.peg.4023; -.
DR TubercuList; Rv3617; -.
DR eggNOG; COG2267; Bacteria.
DR HOGENOM; CLU_020336_7_2_11; -.
DR OMA; PRKHYKW; -.
DR PhylomeDB; I6YGS0; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0018742; F:epoxide hydrolase B activity; ISS:UniProtKB.
DR GO; GO:0016787; F:hydrolase activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR000639; Epox_hydrolase-like.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PRINTS; PR00412; EPOXHYDRLASE.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Detoxification; Hydrolase; Reference proteome.
FT CHAIN 1..322
FT /note="Epoxide hydrolase A"
FT /id="PRO_0000438585"
FT DOMAIN 27..131
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 103
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P95276"
FT ACT_SITE 298
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P95276"
FT SITE 152
FT /note="Contributes to the formation of an oxyanion binding
FT site for the epoxide oxygen of substrate"
FT /evidence="ECO:0000250|UniProtKB:P95276"
FT SITE 239
FT /note="Contributes to the formation of an oxyanion binding
FT site for the epoxide oxygen of substrate"
FT /evidence="ECO:0000250|UniProtKB:P95276"
FT SITE 269
FT /note="Plays an orienting role for the imidazole group of
FT His-298"
FT /evidence="ECO:0000250|UniProtKB:P95276"
SQ SEQUENCE 322 AA; 35097 MW; BA270066838AF442 CRC64;
MGAPTERLVD TNGVRLRVVE AGEPGAPVVI LAHGFPELAY SWRHQIPALA DAGYHVLAPD
QRGYGGSSRP EAIEAYDIHR LTADLVGLLD DVGAERAVWV GHDWGAVVVW NAPLLHADRV
AAVAALSVPA LPRAQVPPTQ AFRSRFGENF FYILYFQEPG IADAELNGDP ARTMRRMIGG
LRPPGDQSAA MRMLAPGPDG FIDRLPEPAG LPAWISQEEL DHYIGEFTRT GFTGGLNWYR
NFDRNWETTA DLAGKTISVP SLFIAGTADP VLTFTRTDRA AEVISGPYRE VLIDGAGHWL
QQERPGEVTA ALLEFLTGLE LR
