4HYPE_BURTA
ID 4HYPE_BURTA Reviewed; 310 AA.
AC Q2T3J4;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 83.
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:24980702};
GN OrderedLocusNames=BTH_II2067 {ECO:0000312|EMBL:ABC36078.1};
GN ORFNames=DR63_1264 {ECO:0000312|EMBL:AIP24752.1};
OS Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS E264).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=271848;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA DeShazer D.;
RT "Bacterial genome adaptation to niches: divergence of the potential
RT virulence genes in three Burkholderia species of different survival
RT strategies.";
RL BMC Genomics 6:174-174(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RA Bishop-Lilly K.A., Broomall S.M., Chain P.S., Chertkov O., Coyne S.R.,
RA Daligault H.E., Davenport K.W., Erkkila T., Frey K.G., Gibbons H.S., Gu W.,
RA Jaissle J., Johnson S.L., Koroleva G.I., Ladner J.T., Lo C.-C.,
RA Minogue T.D., Munk C., Palacios G.F., Redden C.L., Rosenzweig C.N.,
RA Scholz M.B., Teshima H., Xu Y.;
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
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: Catalyzes the epimerization of trans-4-hydroxy-L-proline
CC (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp). Is likely involved in a
CC degradation pathway that converts t4LHyp to alpha-ketoglutarate. Can
CC also catalyze the dehydration of trans-3-hydroxy-L-proline (t3LHyp) to
CC Delta(1)-pyrroline-2-carboxylate (Pyr2C), albeit with 42-fold lower
CC efficiency. Displays no proline racemase activity.
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:24980702};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.4 mM for trans-4-hydroxy-L-proline
CC {ECO:0000269|PubMed:24980702};
CC KM=26 mM for trans-3-hydroxy-L-proline {ECO:0000269|PubMed:24980702};
CC Note=kcat is 40 sec(-1) for t4LHyp epimerization. kcat is 17 sec(-1)
CC for t3LHyp dehydration. {ECO:0000269|PubMed:24980702};
CC -!- SIMILARITY: Belongs to the proline racemase family. {ECO:0000305}.
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DR EMBL; CP000085; ABC36078.1; -; Genomic_DNA.
DR EMBL; CP008785; AIP24752.1; -; Genomic_DNA.
DR RefSeq; WP_009894007.1; NZ_CP008785.1.
DR AlphaFoldDB; Q2T3J4; -.
DR SMR; Q2T3J4; -.
DR EnsemblBacteria; ABC36078; ABC36078; BTH_II2067.
DR KEGG; bte:BTH_II2067; -.
DR HOGENOM; CLU_036729_1_0_4; -.
DR OMA; SHVLWTG; -.
DR OrthoDB; 559014at2; -.
DR SABIO-RK; Q2T3J4; -.
DR Proteomes; UP000001930; Chromosome II.
DR GO; GO:0047580; F:4-hydroxyproline epimerase activity; IDA:CACAO.
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..310
FT /note="4-hydroxyproline 2-epimerase"
FT /id="PRO_0000432283"
FT ACT_SITE 88
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT ACT_SITE 236
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT BINDING 89..90
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT BINDING 208
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT BINDING 232
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT BINDING 237..238
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q4KGU2"
SQ SEQUENCE 310 AA; 32387 MW; 228149579B06842B CRC64;
MKHLHIIDSH TGGEPTRVVV SGFPPLGDGP MAERLAALAR DHDRYRTACI LEPRGSDVLV
GALLCEPVSA GAAAGVIFFN NAGYLGMCGH GTIGLVRTLH HMGRIAPGVH RIETPVGDVE
ATLHDDLSVS VRNVLAYRHA KDVVVEVPGH GSVTGDVAWG GNWFFLVSDH GQRIAGENVA
ALAAYASAVR AGLERAGVTG RDGAPIDHIE LFADDPEHDS RSFVLCPGHA YDRSPCGTGT
SAKLACLAAD GKLAPGAAWR QASVIGSVFS ASYERAESGV VPTIRGSAHL SAEATLLIED
DDPFGWGIVS
