EPHB_MYCTU
ID EPHB_MYCTU Reviewed; 356 AA.
AC I6YC03;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Epoxide hydrolase B {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 EphB {ECO:0000303|PubMed:16511284};
GN Name=ephB; OrderedLocusNames=Rv1938;
GN ORFNames=LH57_10545 {ECO:0000312|EMBL:AIR14683.1};
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 INDUCTION.
RX PubMed=19389781; DOI=10.1099/mic.0.027086-0;
RA de la Paz Santangelo M., Klepp L., Nunez-Garcia J., Blanco F.C., Soria M.,
RA Garcia-Pelayo M.C., Bianco M.V., Cataldi A.A., Golby P., Jackson M.,
RA Gordon S.V., Bigi F.;
RT "Mce3R, a TetR-type transcriptional repressor, controls the expression of a
RT regulon involved in lipid metabolism in Mycobacterium tuberculosis.";
RL Microbiology 155:2245-2255(2009).
RN [5]
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 -!- INDUCTION: Repressed by Mce3R. {ECO:0000269|PubMed:19389781}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Epoxide hydrolase
CC family. {ECO:0000305}.
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DR EMBL; CP009480; AIR14683.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP44705.1; -; Genomic_DNA.
DR RefSeq; NP_216454.1; NC_000962.3.
DR RefSeq; WP_003899091.1; NZ_NVQJ01000034.1.
DR AlphaFoldDB; I6YC03; -.
DR SMR; I6YC03; -.
DR IntAct; I6YC03; 5.
DR MINT; I6YC03; -.
DR STRING; 83332.Rv1938; -.
DR ESTHER; myctu-ephB; Epoxide_hydrolase.
DR MEROPS; S33.971; -.
DR PaxDb; I6YC03; -.
DR PRIDE; I6YC03; -.
DR DNASU; 885392; -.
DR GeneID; 885392; -.
DR KEGG; mtu:Rv1938; -.
DR PATRIC; fig|83332.111.peg.2156; -.
DR TubercuList; Rv1938; -.
DR eggNOG; COG0596; Bacteria.
DR HOGENOM; CLU_020336_7_2_11; -.
DR OMA; FYVSYFQ; -.
DR PhylomeDB; I6YC03; -.
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; PR00111; ABHYDROLASE.
DR PRINTS; PR00412; EPOXHYDRLASE.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Detoxification; Hydrolase; Reference proteome.
FT CHAIN 1..356
FT /note="Epoxide hydrolase B"
FT /id="PRO_0000438586"
FT DOMAIN 28..129
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 104
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P95276"
FT ACT_SITE 333
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P95276"
FT SITE 164
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 272
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 302
FT /note="Plays an orienting role for the imidazole group of
FT His-333"
FT /evidence="ECO:0000250|UniProtKB:P95276"
SQ SEQUENCE 356 AA; 39297 MW; 64D10EA23A0D57AF CRC64;
MSQVHRILNC RGTRIHAVAD SPPDQQGPLV VLLHGFPESW YSWRHQIPAL AGAGYRVVAI
DQRGYGRSSK YRVQKAYRIK ELVGDVVGVL DSYGAEQAFV VGHDWGAPVA WTFAWLHPDR
CAGVVGISVP FAGRGVIGLP GSPFGERRPS DYHLELAGPG RVWYQDYFAV QDGIITEIEE
DLRGWLLGLT YTVSGEGMMA ATKAAVDAGV DLESMDPIDV IRAGPLCMAE GARLKDAFVY
PETMPAWFTE ADLDFYTGEF ERSGFGGPLS FYHNIDNDWH DLADQQGKPL TPPALFIGGQ
YDVGTIWGAQ AIERAHEVMP NYRGTHMIAD VGHWIQQEAP EETNRLLLDF LGGLRP
