4HYPE_BRUC2
ID 4HYPE_BRUC2 Reviewed; 333 AA.
AC A9M832;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=4-hydroxyproline epimerase;
DE EC=5.1.1.8;
DE AltName: Full=Hydroxyproline-2-epimerase;
DE Short=HyPRE;
GN OrderedLocusNames=BCAN_A1830;
OS Brucella canis (strain ATCC 23365 / NCTC 10854).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=483179;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23365 / NCTC 10854;
RA Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J., Dharmanolla C.,
RA Gillespie J.J., Kenyon R.W., Lu J., Mane S., Mohapatra S., Nagrani S.,
RA Purkayastha A., Rajasimha H.K., Shallom J.M., Shallom S., Shukla M.,
RA Snyder E.E., Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H.,
RA Bruce D., Detter C., Munk C., Brettin T.S.;
RT "Brucella canis ATCC 23365 whole genome shotgun sequencing project.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
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;
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the proline racemase family. {ECO:0000305}.
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DR EMBL; CP000872; ABX62830.1; -; Genomic_DNA.
DR RefSeq; WP_004690494.1; NC_010103.1.
DR AlphaFoldDB; A9M832; -.
DR SMR; A9M832; -.
DR EnsemblBacteria; ABX62830; ABX62830; BCAN_A1830.
DR GeneID; 45125077; -.
DR GeneID; 55591392; -.
DR KEGG; bcs:BCAN_A1830; -.
DR HOGENOM; CLU_036729_0_0_5; -.
DR OMA; SHVLWTG; -.
DR PhylomeDB; A9M832; -.
DR Proteomes; UP000001385; 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 3: Inferred from homology;
KW Isomerase.
FT CHAIN 1..333
FT /note="4-hydroxyproline epimerase"
FT /id="PRO_0000354028"
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; 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
