4HYPE_PSEP1
ID 4HYPE_PSEP1 Reviewed; 308 AA.
AC A5VZY6;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=Pput_1285 {ECO:0000312|EMBL:ABQ77446.1};
OS Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=351746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700007 / DSM 6899 / BCRC 17059 / F1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Lykidis A., Parales R., Richardson P.;
RT "Complete sequence of Pseudomonas putida F1.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 700007 / DSM 6899 / BCRC 17059 / F1;
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 epimerization of trans-3-hydroxy-L-proline (t3LHyp)
CC to cis-3-hydroxy-D-proline (c3DHyp), albeit with 200-fold lower
CC efficiency. {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=0.54 mM for trans-4-hydroxy-L-proline
CC {ECO:0000269|PubMed:24980702};
CC KM=19 mM for trans-3-hydroxy-L-proline {ECO:0000269|PubMed:24980702};
CC KM=200 mM for L-proline {ECO:0000269|PubMed:24980702};
CC Note=kcat is 26 sec(-1) for t4LHyp epimerization. kcat is 4.8 sec(-1)
CC for t3LHyp epimerization. kcat is 2.8 sec(-1) for L-proline
CC racemization. {ECO:0000269|PubMed:24980702};
CC -!- SIMILARITY: Belongs to the proline racemase family. {ECO:0000305}.
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DR EMBL; CP000712; ABQ77446.1; -; Genomic_DNA.
DR RefSeq; WP_012051491.1; NC_009512.1.
DR PDB; 4JBD; X-ray; 1.30 A; A=1-308.
DR PDB; 4JD7; X-ray; 1.50 A; A/D=1-308.
DR PDBsum; 4JBD; -.
DR PDBsum; 4JD7; -.
DR AlphaFoldDB; A5VZY6; -.
DR SMR; A5VZY6; -.
DR STRING; 351746.Pput_1285; -.
DR EnsemblBacteria; ABQ77446; ABQ77446; Pput_1285.
DR KEGG; ppf:Pput_1285; -.
DR eggNOG; COG3938; Bacteria.
DR HOGENOM; CLU_036729_1_0_6; -.
DR OMA; SHVLWTG; -.
DR OrthoDB; 559014at2; -.
DR SABIO-RK; A5VZY6; -.
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 3D-structure; Isomerase.
FT CHAIN 1..308
FT /note="4-hydroxyproline 2-epimerase"
FT /id="PRO_0000432244"
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"
FT STRAND 2..11
FT /evidence="ECO:0007829|PDB:4JBD"
FT STRAND 14..21
FT /evidence="ECO:0007829|PDB:4JBD"
FT HELIX 31..41
FT /evidence="ECO:0007829|PDB:4JBD"
FT HELIX 43..50
FT /evidence="ECO:0007829|PDB:4JBD"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:4JBD"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:4JBD"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:4JBD"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:4JBD"
FT HELIX 89..101
FT /evidence="ECO:0007829|PDB:4JBD"
FT STRAND 107..114
FT /evidence="ECO:0007829|PDB:4JBD"
FT STRAND 117..123
FT /evidence="ECO:0007829|PDB:4JBD"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:4JBD"
FT STRAND 136..147
FT /evidence="ECO:0007829|PDB:4JBD"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:4JBD"
FT STRAND 151..168
FT /evidence="ECO:0007829|PDB:4JBD"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:4JD7"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:4JBD"
FT HELIX 179..195
FT /evidence="ECO:0007829|PDB:4JBD"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:4JBD"
FT STRAND 208..215
FT /evidence="ECO:0007829|PDB:4JBD"
FT STRAND 218..226
FT /evidence="ECO:0007829|PDB:4JBD"
FT TURN 227..229
FT /evidence="ECO:0007829|PDB:4JBD"
FT HELIX 237..249
FT /evidence="ECO:0007829|PDB:4JBD"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:4JBD"
FT STRAND 268..276
FT /evidence="ECO:0007829|PDB:4JBD"
FT STRAND 279..286
FT /evidence="ECO:0007829|PDB:4JBD"
FT STRAND 288..298
FT /evidence="ECO:0007829|PDB:4JBD"
FT TURN 303..306
FT /evidence="ECO:0007829|PDB:4JBD"
SQ SEQUENCE 308 AA; 33572 MW; 9FB724B4E11A8D11 CRC64;
MKQIHVIDSH TGGEPTRLVM KGFPQLHGRS MAEQRDELRE LHDRWRRACL LEPRGNDVLV
GALYCPPVSA DATCGVIFFN NAGYLNMCGH GTIGLVASLQ HLGLIAPGVH KIDTPVGQVS
ATLHEDGAIT VANVPSYRYR QHVAVNVPGH GVVHGDIAWG GNWFFLVAEH GQRIELDNRE
VLTEYTWAML KALEAQGITG ENGAPIDHVE LFADDPNADS RNFVMCPGKA YDRSPCGTGT
SAKLACLAAD GTLAEGQTWV QASITGSQFH GRYERDGERI RPFITGRAHM TADSTLLIDE
QDPFAWGI
