4HYPE_BRUME
ID 4HYPE_BRUME Reviewed; 333 AA.
AC Q8YJ29;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=4-hydroxyproline epimerase;
DE EC=5.1.1.8;
DE AltName: Full=Hydroxyproline-2-epimerase;
DE Short=BmHyPRE;
GN OrderedLocusNames=BMEI0257;
OS Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=224914;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=16M / ATCC 23456 / NCTC 10094;
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=16M / ATCC 23456 / NCTC 10094;
RX PubMed=11756688; DOI=10.1073/pnas.221575398;
RA DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA Haselkorn R., Kyrpides N.C., Overbeek R.;
RT "The genome sequence of the facultative intracellular pathogen Brucella
RT melitensis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
CC -!- FUNCTION: Allows intracellular utilization of 4-hydroxyproline, one of
CC the major constituents of host collagen, by converting 4-hydroxy-L-
CC proline to 4-hydroxy-D-proline, which can be further metabolized by
CC intracellular 4-hydroxy-D-proline oxidases. Strong B-cell mitogen.
CC Plays an important role in the regulation of intra- and extracellular
CC amino acid pools, allowing the bacterium to profit from host precursors
CC and enzymatic pathways.
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 -!- 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=9.0 mM for 4-hydroxy-L-proline {ECO:0000269|PubMed:17849014};
CC KM=12.7 mM for 4-hydroxy-D-proline {ECO:0000269|PubMed:17849014};
CC Vmax=0.45 uM/sec/mg enzyme with L-proline as substrate (at 37 degrees
CC Celsius) {ECO:0000269|PubMed:17849014};
CC Vmax=0.70 uM/sec/mg enzyme with D-proline as substrate (at 37 degrees
CC 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}.
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DR EMBL; EF495342; ABS82394.1; -; Genomic_DNA.
DR EMBL; AE008917; AAL51439.1; -; Genomic_DNA.
DR PIR; AD3284; AD3284.
DR RefSeq; WP_004684253.1; NZ_GG703781.1.
DR AlphaFoldDB; Q8YJ29; -.
DR SMR; Q8YJ29; -.
DR STRING; 224914.BMEI0257; -.
DR EnsemblBacteria; AAL51439; AAL51439; BMEI0257.
DR GeneID; 29593014; -.
DR KEGG; bme:BMEI0257; -.
DR PATRIC; fig|224914.52.peg.1243; -.
DR eggNOG; COG3938; Bacteria.
DR OMA; SHVLWTG; -.
DR PhylomeDB; Q8YJ29; -.
DR BRENDA; 5.1.1.8; 995.
DR Proteomes; UP000000419; 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 epimerase"
FT /id="PRO_0000354029"
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 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; 36511 MW; 76457EF17BA72653 CRC64;
MARHSFFCVD GHTCGNPVRL VAGGGPNLNG STMMEKCAHF 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 SAA
