EPHG_MYCTU
ID EPHG_MYCTU Reviewed; 149 AA.
AC O33283; F2GPI3; L0TC43;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Epoxide hydrolase EphG;
DE Short=EH;
DE EC=3.3.2.10;
DE AltName: Full=Cholesterol-5,6-oxide hydrolase;
DE EC=3.3.2.11;
GN Name=ephG; OrderedLocusNames=Rv2740;
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).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP SUBSTRATE SPECIFICITY, KINETIC PARAMETERS, ACTIVITY REGULATION, REACTION
RP MECHANISM, ACTIVE SITES, AND SUBUNIT.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=16051262; DOI=10.1016/j.jmb.2005.06.055;
RA Johansson P., Unge T., Cronin A., Arand M., Bergfors T., Jones T.A.,
RA Mowbray S.L.;
RT "Structure of an atypical epoxide hydrolase from Mycobacterium tuberculosis
RT gives insights into its function.";
RL J. Mol. Biol. 351:1048-1056(2005).
CC -!- FUNCTION: Epoxide hydrolase capable of hydrolyzing long or bulky
CC lipophilic epoxides such as 9,10-epoxystearic acid and cholesterol 5,6-
CC oxide in vitro. The physiological substrates have yet to be identified,
CC but could be fatty acid or steroid derivatives.
CC {ECO:0000269|PubMed:16051262}.
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:0000269|PubMed:16051262};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6alpha-epoxy-5alpha-cholestan-3beta-ol + H2O = 5alpha-
CC cholestane-3beta,5,6beta-triol; Xref=Rhea:RHEA:11964,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:28082, ChEBI:CHEBI:49305; EC=3.3.2.11;
CC Evidence={ECO:0000269|PubMed:16051262};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6beta-epoxy-5beta-cholestan-3beta-ol + H2O = 5alpha-
CC cholestane-3beta,5,6beta-triol; Xref=Rhea:RHEA:15113,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:28082, ChEBI:CHEBI:28164; EC=3.3.2.11;
CC Evidence={ECO:0000269|PubMed:16051262};
CC -!- ACTIVITY REGULATION: Is inhibited by the anti-epileptic drug valpromide
CC (Ki value of about 100 uM). {ECO:0000269|PubMed:16051262}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=45 uM for cis-9,10-epoxystearate {ECO:0000269|PubMed:16051262};
CC KM=60 uM for cholesterol 5,6-oxide {ECO:0000269|PubMed:16051262};
CC Vmax=30 nmol/min/mg enzyme with cis-9,10-epoxystearate as substrate
CC {ECO:0000269|PubMed:16051262};
CC Vmax=1.1 nmol/min/mg enzyme with cholesterol 5,6-oxide as substrate
CC {ECO:0000269|PubMed:16051262};
CC -!- SUBUNIT: Homodimer. Is also present as monomer in solution.
CC {ECO:0000269|PubMed:16051262}.
CC -!- SIMILARITY: Belongs to the limonene-1,2-epoxide hydrolase family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP45539.1; -; Genomic_DNA.
DR PIR; C70878; C70878.
DR RefSeq; NP_217256.1; NC_000962.3.
DR RefSeq; WP_003414015.1; NZ_NVQJ01000017.1.
DR PDB; 2BNG; X-ray; 2.50 A; A/B/C=1-149.
DR PDBsum; 2BNG; -.
DR AlphaFoldDB; O33283; -.
DR SMR; O33283; -.
DR STRING; 83332.Rv2740; -.
DR PaxDb; O33283; -.
DR DNASU; 888365; -.
DR GeneID; 888365; -.
DR KEGG; mtu:Rv2740; -.
DR TubercuList; Rv2740; -.
DR eggNOG; COG4308; Bacteria.
DR OMA; FEVHDGR; -.
DR SABIO-RK; O33283; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0033963; F:cholesterol-5,6-oxide hydrolase activity; IDA:MTBBASE.
DR GO; GO:0004301; F:epoxide hydrolase activity; IDA:MTBBASE.
DR GO; GO:0097176; P:epoxide metabolic process; IDA:MTBBASE.
DR InterPro; IPR013100; LEH.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR Pfam; PF07858; LEH; 1.
DR SUPFAM; SSF54427; SSF54427; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Reference proteome.
FT CHAIN 1..149
FT /note="Epoxide hydrolase EphG"
FT /id="PRO_0000420415"
FT ACT_SITE 93
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:16051262"
FT ACT_SITE 122
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:16051262"
FT HELIX 14..30
FT /evidence="ECO:0007829|PDB:2BNG"
FT HELIX 33..39
FT /evidence="ECO:0007829|PDB:2BNG"
FT STRAND 40..48
FT /evidence="ECO:0007829|PDB:2BNG"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:2BNG"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:2BNG"
FT HELIX 57..65
FT /evidence="ECO:0007829|PDB:2BNG"
FT TURN 66..70
FT /evidence="ECO:0007829|PDB:2BNG"
FT STRAND 72..83
FT /evidence="ECO:0007829|PDB:2BNG"
FT STRAND 86..97
FT /evidence="ECO:0007829|PDB:2BNG"
FT STRAND 100..113
FT /evidence="ECO:0007829|PDB:2BNG"
FT STRAND 116..123
FT /evidence="ECO:0007829|PDB:2BNG"
FT HELIX 126..139
FT /evidence="ECO:0007829|PDB:2BNG"
SQ SEQUENCE 149 AA; 16593 MW; 6941EA603B942822 CRC64;
MAELTETSPE TPETTEAIRA VEAFLNALQN EDFDTVDAAL GDDLVYENVG FSRIRGGRRT
ATLLRRMQGR VGFEVKIHRI GADGAAVLTE RTDALIIGPL RVQFWVCGVF EVDDGRITLW
RDYFDVYDMF KGLLRGLVAL VVPSLKATL
