4HYPE_PSEPK
ID 4HYPE_PSEPK Reviewed; 308 AA.
AC Q88NF3;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=4-hydroxyproline 2-epimerase {ECO:0000305|PubMed:23995642};
DE Short=4-hydroxyproline epimerase {ECO:0000303|PubMed:23995642};
DE Short=4Hyp 2-epimerase;
DE Short=4HypE;
DE EC=5.1.1.8 {ECO:0000269|PubMed:23995642};
GN Name=proR {ECO:0000303|PubMed:23995642};
GN Synonyms=prpA {ECO:0000312|EMBL:AAN66882.1};
GN OrderedLocusNames=PP_1258 {ECO:0000312|EMBL:AAN66882.1};
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=23995642; DOI=10.1128/jb.00761-13;
RA Radkov A.D., Moe L.A.;
RT "Amino acid racemization in Pseudomonas putida KT2440.";
RL J. Bacteriol. 195:5016-5024(2013).
CC -!- FUNCTION: Catalyzes the reversible epimerization of cis-4-hydroxy-D-
CC proline (c4DHyp) to trans-4-hydroxy-L-proline (t4LHyp). May be involved
CC in a degradation pathway that allows P.putida strain KT2440 to grow on
CC either epimer of 4-hydroxyproline, c4DHyp and t4LHyp, as the sole
CC carbon and nitrogen source. Does not exhibit measureable racemase
CC activity in vitro with any of the 19 natural chiral amino acid
CC enantiomers. {ECO:0000269|PubMed:23995642}.
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:23995642};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.26 mM for cis-4-hydroxy-D-proline {ECO:0000269|PubMed:23995642};
CC KM=15.04 mM for trans-4-hydroxy-L-proline
CC {ECO:0000269|PubMed:23995642};
CC Note=kcat is 69.63 sec(-1) for c4DHyp epimerization. kcat is 7.74
CC sec(-1) for t4LHyp epimerization. {ECO:0000269|PubMed:23995642};
CC -!- SIMILARITY: Belongs to the proline racemase family. {ECO:0000305}.
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DR EMBL; AE015451; AAN66882.1; -; Genomic_DNA.
DR RefSeq; NP_743418.1; NC_002947.4.
DR RefSeq; WP_010952392.1; NC_002947.4.
DR AlphaFoldDB; Q88NF3; -.
DR SMR; Q88NF3; -.
DR STRING; 160488.PP_1258; -.
DR EnsemblBacteria; AAN66882; AAN66882; PP_1258.
DR KEGG; ppu:PP_1258; -.
DR PATRIC; fig|160488.4.peg.1334; -.
DR eggNOG; COG3938; Bacteria.
DR HOGENOM; CLU_036729_1_0_6; -.
DR OMA; SHVLWTG; -.
DR PhylomeDB; Q88NF3; -.
DR BioCyc; MetaCyc:G1G01-1345-MON; -.
DR BioCyc; PPUT160488:G1G01-1345-MON; -.
DR Proteomes; UP000000556; Chromosome.
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; Reference proteome.
FT CHAIN 1..308
FT /note="4-hydroxyproline 2-epimerase"
FT /id="PRO_0000446939"
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 308 AA; 33663 MW; 5338B28A1D1B0BED CRC64;
MKQIHVIDSH TGGEPTRLVM KGFPQLRGRS MAEQRDELRE LHDRWRRACL LEPRGNDVLV
GALYCPPVSA DATCGVIFFN NAGYLNMCGH GTIGLVASLQ HMGLITPGVH KIDTPVGQVS
ATLHEDGAIT VANVPSYRYR QQVAVDVPGH GVVRGDIAWG GNWFFLVSEH GQRIELDNRE
ALTEYTWAML KALETQGVTG ENGAPIDHIE LFADDPNADS RNFVMCPGKA YDRSPCGTGT
SAKLACLAAD GKLAEGQTWV QASITGSQFH GRYARDGERI RPFITGRAYM TADSTLLIDE
QDPFAWGI
