4HYPE_BRUSU
ID 4HYPE_BRUSU Reviewed; 333 AA.
AC Q8FYS0; A8DEY2; G0K7C9;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=4-hydroxyproline 2-epimerase {ECO:0000303|PubMed:24980702};
DE Short=4Hyp 2-epimerase;
DE Short=4HypE {ECO:0000303|PubMed:24980702};
DE EC=5.1.1.8 {ECO:0000269|PubMed:17849014, ECO:0000269|PubMed:24980702};
DE AltName: Full=Hydroxyproline-2-epimerase {ECO:0000303|PubMed:17849014};
DE Short=BsHyPRE {ECO:0000303|PubMed:17849014};
GN OrderedLocusNames=BR1792, BS1330_I1786;
OS Brucella suis biovar 1 (strain 1330).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=204722;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=1330;
RX PubMed=17849014; DOI=10.1371/journal.pone.0000885;
RA Goytia M., Chamond N., Cosson A., Coatnoan N., Hermant D., Berneman A.,
RA Minoprio P.;
RT "Molecular and structural discrimination of proline racemase and
RT hydroxyproline-2-epimerase from nosocomial and bacterial pathogens.";
RL PLoS ONE 2:E885-E885(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=12271122; DOI=10.1073/pnas.192319099;
RA Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT "The Brucella suis genome reveals fundamental similarities between animal
RT and plant pathogens and symbionts.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=22038969; DOI=10.1128/jb.06181-11;
RA Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT "Revised genome sequence of Brucella suis 1330.";
RL J. Bacteriol. 193:6410-6410(2011).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=24980702; DOI=10.7554/elife.03275;
RA Zhao S., Sakai A., Zhang X., Vetting M.W., Kumar R., Hillerich B.,
RA San Francisco B., Solbiati J., Steves A., Brown S., Akiva E., Barber A.,
RA Seidel R.D., Babbitt P.C., Almo S.C., Gerlt J.A., Jacobson M.P.;
RT "Prediction and characterization of enzymatic activities guided by sequence
RT similarity and genome neighborhood networks.";
RL Elife 3:E03275-E03275(2014).
CC -!- FUNCTION: Allows intracellular utilization of 4-hydroxyproline, one of
CC the major constituents of host collagen, by converting trans-4-hydroxy-
CC L-proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp), which can be
CC further metabolized by intracellular 4-hydroxy-D-proline oxidases.
CC Strong B-cell mitogen. Plays an important role in the regulation of
CC intra- and extracellular amino acid pools, allowing the bacterium to
CC profit from host precursors and enzymatic pathways. Displays no proline
CC racemase activity. {ECO:0000269|PubMed:17849014,
CC ECO:0000269|PubMed:24980702}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=trans-4-hydroxy-L-proline = cis-4-hydroxy-D-proline;
CC Xref=Rhea:RHEA:21152, ChEBI:CHEBI:57690, ChEBI:CHEBI:58375;
CC EC=5.1.1.8; Evidence={ECO:0000269|PubMed:17849014,
CC ECO:0000269|PubMed:24980702};
CC -!- ACTIVITY REGULATION: Inhibited by iodoacetate, iodoacetamide and by
CC high amounts (10 mM) of pyrrole-2-carboxylic acid (PYC). Not inhibited
CC by PYC at 1 mM. {ECO:0000269|PubMed:17849014}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.6 mM for 4-hydroxy-L-proline {ECO:0000269|PubMed:17849014};
CC KM=10.8 mM for 4-hydroxy-D-proline {ECO:0000269|PubMed:17849014};
CC Vmax=0.50 uM/sec/mg enzyme with 4-hydroxy-L-proline as substrate (at
CC 37 degrees Celsius) {ECO:0000269|PubMed:17849014};
CC Vmax=0.75 uM/sec/mg enzyme with 4-hydroxy-D-proline as substrate (at
CC 37 degrees Celsius) {ECO:0000269|PubMed:17849014};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- MISCELLANEOUS: This enzyme does not require pyridoxal phosphate (PLP)
CC as a cofactor.
CC -!- SIMILARITY: Belongs to the proline racemase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EF495343; ABS82395.1; -; Genomic_DNA.
DR EMBL; AE014291; AAN30688.1; -; Genomic_DNA.
DR EMBL; CP002997; AEM19105.1; -; Genomic_DNA.
DR RefSeq; WP_004690494.1; NZ_KN046804.1.
DR AlphaFoldDB; Q8FYS0; -.
DR SMR; Q8FYS0; -.
DR EnsemblBacteria; AEM19105; AEM19105; BS1330_I1786.
DR GeneID; 45125077; -.
DR GeneID; 55591392; -.
DR KEGG; bms:BR1792; -.
DR KEGG; bsi:BS1330_I1786; -.
DR PATRIC; fig|204722.22.peg.66; -.
DR HOGENOM; CLU_036729_0_0_5; -.
DR OMA; SHVLWTG; -.
DR PhylomeDB; Q8FYS0; -.
DR BRENDA; 5.1.1.8; 8693.
DR Proteomes; UP000007104; Chromosome I.
DR GO; GO:0047580; F:4-hydroxyproline epimerase activity; IEA:UniProtKB-EC.
DR InterPro; IPR008794; Pro_racemase_fam.
DR PANTHER; PTHR33442; PTHR33442; 1.
DR Pfam; PF05544; Pro_racemase; 1.
DR PIRSF; PIRSF029792; Pro_racemase; 1.
DR SFLD; SFLDS00028; Proline_Racemase; 1.
PE 1: Evidence at protein level;
KW Isomerase.
FT CHAIN 1..333
FT /note="4-hydroxyproline 2-epimerase"
FT /id="PRO_0000354032"
FT ACT_SITE 90
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT ACT_SITE 253
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT BINDING 91..92
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT BINDING 223
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT BINDING 249
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT BINDING 254..255
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q4KGU2"
SQ SEQUENCE 333 AA; 36592 MW; 320E7AA563495FBD CRC64;
MARHSFFCVD GHTCGNPVRL VAGGGPNLNG STMMEKRAHF LAEYDWIRTG LMFEPRGHDM
MSGSILYPPT RPDCDVAVLF IETSGCLPMC GHGTIGTVTM AIEQGLVTPK TPGKLNLDTP
AGLVAIEYEQ DGQYVERVRL TNVPAFLYAE GLEVECPDLG PIKVDVAYGG NFYAIVEPQE
NYTDMDDYSA LQLIAWSPVL RQRLNEKYKF QHPELPDINR LSHILWTGKP KHPQAHARNA
VFYGDKAIDR SPCGTGTSAR MAQLAAKGKL KPGDEFIHES IIGSLFHGRV ERAAEVAGRP
AIVPSIAGWA RMTGYNTIFI DDRDPFAHGF SVA
