4HYPE_PSEF5
ID 4HYPE_PSEF5 Reviewed; 310 AA.
AC Q4KGU2;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=PFL_1412 {ECO:0000312|EMBL:AAY90697.1};
OS Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=220664;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5;
RX PubMed=15980861; DOI=10.1038/nbt1110;
RA Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.A.,
RA Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A., Rosovitz M.J.,
RA Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W., Nelson W.C.,
RA Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A., Pierson L.S. III,
RA Thomashow L.S., Loper J.E.;
RT "Complete genome sequence of the plant commensal Pseudomonas fluorescens
RT Pf-5.";
RL Nat. Biotechnol. 23:873-878(2005).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEXES WITH
RP PYRROLE-2-CARBOXYLATE AND WITH TRANS-4-HYDROXY-L-PROLINE, FUNCTION,
RP CATALYTIC ACTIVITY, AND ACTIVE SITE.
RC STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5;
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.
CC Displays no proline racemase activity. {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 -!- SIMILARITY: Belongs to the proline racemase family. {ECO:0000305}.
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DR EMBL; CP000076; AAY90697.1; -; Genomic_DNA.
DR RefSeq; WP_011059754.1; NC_004129.6.
DR PDB; 4J9W; X-ray; 1.60 A; A/B=1-310.
DR PDB; 4J9X; X-ray; 1.70 A; A/B=1-310.
DR PDBsum; 4J9W; -.
DR PDBsum; 4J9X; -.
DR AlphaFoldDB; Q4KGU2; -.
DR SMR; Q4KGU2; -.
DR STRING; 220664.PFL_1412; -.
DR EnsemblBacteria; AAY90697; AAY90697; PFL_1412.
DR KEGG; pfl:PFL_1412; -.
DR PATRIC; fig|220664.5.peg.1446; -.
DR eggNOG; COG3938; Bacteria.
DR HOGENOM; CLU_036729_1_0_6; -.
DR OMA; SHVLWTG; -.
DR OrthoDB; 559014at2; -.
DR Proteomes; UP000008540; 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 3D-structure; Isomerase; Reference proteome.
FT CHAIN 1..310
FT /note="4-hydroxyproline 2-epimerase"
FT /id="PRO_0000432243"
FT ACT_SITE 88
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:24980702"
FT ACT_SITE 236
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:24980702"
FT BINDING 89..90
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:24980702"
FT BINDING 208
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:24980702"
FT BINDING 232
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:24980702"
FT BINDING 237..238
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:24980702"
FT STRAND 2..11
FT /evidence="ECO:0007829|PDB:4J9W"
FT STRAND 14..21
FT /evidence="ECO:0007829|PDB:4J9W"
FT HELIX 31..50
FT /evidence="ECO:0007829|PDB:4J9W"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:4J9W"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:4J9W"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:4J9W"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:4J9W"
FT HELIX 89..101
FT /evidence="ECO:0007829|PDB:4J9W"
FT STRAND 107..114
FT /evidence="ECO:0007829|PDB:4J9W"
FT STRAND 117..123
FT /evidence="ECO:0007829|PDB:4J9W"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:4J9W"
FT STRAND 136..145
FT /evidence="ECO:0007829|PDB:4J9W"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:4J9X"
FT STRAND 153..168
FT /evidence="ECO:0007829|PDB:4J9W"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:4J9W"
FT HELIX 179..196
FT /evidence="ECO:0007829|PDB:4J9W"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:4J9W"
FT STRAND 208..215
FT /evidence="ECO:0007829|PDB:4J9W"
FT STRAND 218..225
FT /evidence="ECO:0007829|PDB:4J9W"
FT HELIX 237..249
FT /evidence="ECO:0007829|PDB:4J9W"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:4J9W"
FT STRAND 268..276
FT /evidence="ECO:0007829|PDB:4J9W"
FT STRAND 279..286
FT /evidence="ECO:0007829|PDB:4J9W"
FT STRAND 288..298
FT /evidence="ECO:0007829|PDB:4J9W"
FT TURN 303..306
FT /evidence="ECO:0007829|PDB:4J9W"
SQ SEQUENCE 310 AA; 33442 MW; B22441B593765962 CRC64;
MKKITVIDSH TGGEPTRLVI DGFPDLGRGS MAERLQILER EHDQWRRACV LEPRGSDVLV
GALLCQPQAG DACAGVIFFN NSGYLGMCGH GTIGLVRSLY HLGRIDQGVH RIETPVGTVE
ATLHEDLSVS VRNVPAYRYR TQVMLQLPGH GKVHGDIAWG GNWFFLISDH GQRIALDNVE
ALTHYTRDVR QALEAAGITG AEGGVIDHIE LFADDPQADS RNFVLCPGKA YDRSPCGTGT
SAKLACLAAD GKLAPGQAWR QASVIGSQFS AHYEKVGEQL IPILRGSAHI SAEATLLLDD
SDPFVWGIGS
