EPHB_MYCTO
ID EPHB_MYCTO Reviewed; 356 AA.
AC P95276; F2GGS7; Q7D7R2;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 2.
DT 25-MAY-2022, entry version 138.
DE RecName: Full=Epoxide hydrolase B {ECO:0000303|PubMed:18585390};
DE Short=EHB {ECO:0000303|PubMed:18585390};
DE EC=3.3.2.10 {ECO:0000305|PubMed:18585390};
GN OrderedLocusNames=MT1988;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 2-356 IN COMPLEX WITH SUBSTRATE
RP ANALOG, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, SUBUNIT, SUBSTRATE
RP SPECIFICITY, AND REACTION MECHANISM.
RX PubMed=18585390; DOI=10.1016/j.jmb.2008.06.030;
RA Biswal B.K., Morisseau C., Garen G., Cherney M.M., Garen C., Niu C.,
RA Hammock B.D., James M.N.;
RT "The molecular structure of epoxide hydrolase B from Mycobacterium
RT tuberculosis and its complex with a urea-based inhibitor.";
RL J. Mol. Biol. 381:897-912(2008).
CC -!- FUNCTION: Could be involved in detoxification of extraneous host-cell
CC epoxides. Catalyzes the hydrolysis of small aromatic epoxide-containing
CC substrates such as trans-1,3-diphenylpropene oxide, trans and cis-
CC stilbene oxide, and terpenoid epoxide. {ECO:0000269|PubMed:18585390}.
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:0000305|PubMed:18585390};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18585390}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Epoxide hydrolase
CC family. {ECO:0000305}.
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DR EMBL; AE000516; AAK46260.1; -; Genomic_DNA.
DR PIR; F70636; F70636.
DR RefSeq; WP_003899091.1; NZ_KK341227.1.
DR PDB; 2E3J; X-ray; 2.10 A; A=2-356.
DR PDB; 2ZJF; X-ray; 2.40 A; A=2-356.
DR PDBsum; 2E3J; -.
DR PDBsum; 2ZJF; -.
DR AlphaFoldDB; P95276; -.
DR SMR; P95276; -.
DR BindingDB; P95276; -.
DR ChEMBL; CHEMBL1795155; -.
DR DrugBank; DB07496; 1,3-diphenylurea.
DR DrugCentral; P95276; -.
DR ESTHER; myctu-ephB; Epoxide_hydrolase.
DR MEROPS; S33.971; -.
DR EnsemblBacteria; AAK46260; AAK46260; MT1988.
DR KEGG; mtc:MT1988; -.
DR PATRIC; fig|83331.31.peg.2142; -.
DR HOGENOM; CLU_020336_7_2_11; -.
DR InParanoid; P95276; -.
DR EvolutionaryTrace; P95276; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0018742; F:epoxide hydrolase B activity; IDA:MTBBASE.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:MTBBASE.
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 3D-structure; Detoxification; Hydrolase.
FT CHAIN 1..356
FT /note="Epoxide hydrolase B"
FT /id="PRO_0000438587"
FT DOMAIN 28..129
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 104
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:18585390"
FT ACT_SITE 333
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:18585390"
FT SITE 164
FT /note="Contributes to the formation of an oxyanion binding
FT site for the epoxide oxygen of substrate"
FT /evidence="ECO:0000305|PubMed:18585390"
FT SITE 272
FT /note="Contributes to the formation of an oxyanion binding
FT site for the epoxide oxygen of substrate"
FT /evidence="ECO:0000305|PubMed:18585390"
FT SITE 302
FT /note="Plays an orienting role for the imidazole group of
FT His-333"
FT /evidence="ECO:0000305|PubMed:18585390"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:2E3J"
FT STRAND 13..20
FT /evidence="ECO:0007829|PDB:2E3J"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:2E3J"
FT HELIX 40..43
FT /evidence="ECO:0007829|PDB:2E3J"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:2E3J"
FT HELIX 47..52
FT /evidence="ECO:0007829|PDB:2E3J"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:2E3J"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:2E3J"
FT HELIX 79..92
FT /evidence="ECO:0007829|PDB:2E3J"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:2E3J"
FT HELIX 106..116
FT /evidence="ECO:0007829|PDB:2E3J"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:2E3J"
FT STRAND 121..129
FT /evidence="ECO:0007829|PDB:2E3J"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:2E3J"
FT HELIX 149..154
FT /evidence="ECO:0007829|PDB:2E3J"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:2E3J"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:2E3J"
FT HELIX 164..170
FT /evidence="ECO:0007829|PDB:2E3J"
FT HELIX 173..179
FT /evidence="ECO:0007829|PDB:2E3J"
FT HELIX 182..192
FT /evidence="ECO:0007829|PDB:2E3J"
FT HELIX 195..203
FT /evidence="ECO:0007829|PDB:2E3J"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:2E3J"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:2E3J"
FT HELIX 234..237
FT /evidence="ECO:0007829|PDB:2E3J"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:2ZJF"
FT HELIX 250..263
FT /evidence="ECO:0007829|PDB:2E3J"
FT HELIX 266..273
FT /evidence="ECO:0007829|PDB:2E3J"
FT HELIX 275..281
FT /evidence="ECO:0007829|PDB:2E3J"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:2E3J"
FT STRAND 294..299
FT /evidence="ECO:0007829|PDB:2E3J"
FT HELIX 303..307
FT /evidence="ECO:0007829|PDB:2E3J"
FT HELIX 309..313
FT /evidence="ECO:0007829|PDB:2E3J"
FT HELIX 315..318
FT /evidence="ECO:0007829|PDB:2E3J"
FT STRAND 322..330
FT /evidence="ECO:0007829|PDB:2E3J"
FT HELIX 335..338
FT /evidence="ECO:0007829|PDB:2E3J"
FT HELIX 340..352
FT /evidence="ECO:0007829|PDB:2E3J"
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
