4HYPE_CHRSD
ID 4HYPE_CHRSD Reviewed; 311 AA.
AC Q1QU06;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=Csal_2705 {ECO:0000312|EMBL:ABE60052.1};
OS Chromohalobacter salexigens (strain ATCC BAA-138 / DSM 3043 / CIP 106854 /
OS NCIMB 13768 / 1H11).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Chromohalobacter.
OX NCBI_TaxID=290398;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-138 / DSM 3043 / CIP 106854 / NCIMB 13768 / 1H11;
RX PubMed=22675587; DOI=10.4056/sigs.2285059;
RA Copeland A., O'Connor K., Lucas S., Lapidus A., Berry K.W., Detter J.C.,
RA Del Rio T.G., Hammon N., Dalin E., Tice H., Pitluck S., Bruce D.,
RA Goodwin L., Han C., Tapia R., Saunders E., Schmutz J., Brettin T.,
RA Larimer F., Land M., Hauser L., Vargas C., Nieto J.J., Kyrpides N.C.,
RA Ivanova N., Goker M., Klenk H.P., Csonka L.N., Woyke T.;
RT "Complete genome sequence of the halophilic and highly halotolerant
RT Chromohalobacter salexigens type strain (1H11(T)).";
RL Stand. Genomic Sci. 5:379-388(2011).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS), FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC BAA-138 / DSM 3043 / CIP 106854 / NCIMB 13768 / 1H11;
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; CP000285; ABE60052.1; -; Genomic_DNA.
DR RefSeq; WP_011507998.1; NC_007963.1.
DR PDB; 4JCI; X-ray; 1.70 A; A/B=1-311.
DR PDBsum; 4JCI; -.
DR AlphaFoldDB; Q1QU06; -.
DR SMR; Q1QU06; -.
DR STRING; 290398.Csal_2705; -.
DR EnsemblBacteria; ABE60052; ABE60052; Csal_2705.
DR KEGG; csa:Csal_2705; -.
DR eggNOG; COG3938; Bacteria.
DR HOGENOM; CLU_036729_1_0_6; -.
DR OMA; SHVLWTG; -.
DR OrthoDB; 559014at2; -.
DR Proteomes; UP000000239; 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..311
FT /note="4-hydroxyproline 2-epimerase"
FT /id="PRO_0000432245"
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 1..11
FT /evidence="ECO:0007829|PDB:4JCI"
FT STRAND 14..23
FT /evidence="ECO:0007829|PDB:4JCI"
FT HELIX 31..41
FT /evidence="ECO:0007829|PDB:4JCI"
FT HELIX 43..50
FT /evidence="ECO:0007829|PDB:4JCI"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:4JCI"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:4JCI"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:4JCI"
FT HELIX 89..101
FT /evidence="ECO:0007829|PDB:4JCI"
FT STRAND 107..113
FT /evidence="ECO:0007829|PDB:4JCI"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:4JCI"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:4JCI"
FT STRAND 136..147
FT /evidence="ECO:0007829|PDB:4JCI"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:4JCI"
FT STRAND 151..168
FT /evidence="ECO:0007829|PDB:4JCI"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:4JCI"
FT HELIX 179..195
FT /evidence="ECO:0007829|PDB:4JCI"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:4JCI"
FT STRAND 208..213
FT /evidence="ECO:0007829|PDB:4JCI"
FT STRAND 218..226
FT /evidence="ECO:0007829|PDB:4JCI"
FT TURN 227..229
FT /evidence="ECO:0007829|PDB:4JCI"
FT HELIX 237..249
FT /evidence="ECO:0007829|PDB:4JCI"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:4JCI"
FT STRAND 268..276
FT /evidence="ECO:0007829|PDB:4JCI"
FT STRAND 279..286
FT /evidence="ECO:0007829|PDB:4JCI"
FT STRAND 288..298
FT /evidence="ECO:0007829|PDB:4JCI"
FT TURN 303..306
FT /evidence="ECO:0007829|PDB:4JCI"
SQ SEQUENCE 311 AA; 33726 MW; 14C7BCB33B41906C CRC64;
MKRVHVIDSH TAGEPTRLVM EGMPALSGRT IAEKCDDFRD NHDAWRRAIM LEPRGHDVLV
GALYCAPESS DASCGVIFFN NSGYLGMCGH GTIGLVASLH HLGQLTPGCH KIDTPAGPVS
ATLHDDGAVT VRNVLSYRHR RRVPVEVPGY GTVHGDIAWG GNWFFLVSDH DMTLELDNVE
ALTDYTWAIR QALEAQSITG ENGGVIDHIE LFCDDREADS RNFVLCPGKA YDRSPCGTGT
SAKLACLAAD GKLAPGQVWT QASICGSRFE AFYEREGDGI RPSIKGRAYL SADATLLIDE
RDPFAWGIAS P
