4HYPE_CERS1
ID 4HYPE_CERS1 Reviewed; 337 AA.
AC A3PPJ8;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=Rsph17029_3164 {ECO:0000312|EMBL:ABN78264.1};
OS Cereibacter sphaeroides (strain ATCC 17029 / ATH 2.4.9) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=349101;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17029 / ATH 2.4.9;
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 Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.,
RA Mackenzie C., Choudhary M., Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome 2 of Rhodobacter sphaeroides ATCC 17029.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
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 ECO:0000305|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; CP000578; ABN78264.1; -; Genomic_DNA.
DR RefSeq; WP_011842139.1; NC_009050.1.
DR AlphaFoldDB; A3PPJ8; -.
DR SMR; A3PPJ8; -.
DR EnsemblBacteria; ABN78264; ABN78264; Rsph17029_3164.
DR GeneID; 57471827; -.
DR KEGG; rsh:Rsph17029_3164; -.
DR HOGENOM; CLU_036729_0_0_5; -.
DR OMA; ERRAYCM; -.
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.
FT CHAIN 1..337
FT /note="4-hydroxyproline 2-epimerase"
FT /id="PRO_0000432256"
FT ACT_SITE 91
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT BINDING 92..93
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT BINDING 252
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT BINDING 257..258
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q4KGU2"
SQ SEQUENCE 337 AA; 36862 MW; 03E1CBBC2F0FEB7C CRC64;
MRVQDVYNVI YTHTEGEPLC IIYSGVPYPA GSTILEKRAF LEENYDWLRK ALMREPRGHA
DMFGVFLTPP SSRDYDAGLI YIDGKEYSHM CGHGTIAVAM AMVANGLVAR DPSGLTRIRF
ETTAGLVVAE VAHEDDRVLW TRFENVPAYV AAQDIAFELP GYGPLKADLV WGGNYFGIID
LRGTSLRIAP ENGSELSRMG LIAREEIRKK VTVQHPTEAH INNLNFVTFW HEPTIEGCLY
KNVHVFSAGQ LDRSPGGTGT SAMMAYFEAR GVIGLNQPIT SEGLLGSGTF EGCLIGETTL
GTVRAVRPTV KGTAGMLGTA SWTINREDPV DAGFLVL
