ID   4HYPE_SPILD             Reviewed;         334 AA.
AC   D2QN44;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   02-MAR-2010, sequence version 1.
DT   03-AUG-2022, entry version 55.
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=Slin_1478 {ECO:0000312|EMBL:ADB37528.1};
OS   Spirosoma linguale (strain ATCC 33905 / DSM 74 / LMG 10896).
OC   Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae;
OC   Spirosoma.
OX   NCBI_TaxID=504472;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33905 / DSM 74 / LMG 10896;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA   Mikhailova N., Ovchinnikova G., Saunders E., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA   Hugenholtz P., Woyke T., Wu D., Tindal B., Schutze A., Schneider S.,
RA   Goker M., Klenk H.-P., Eisen J.A.;
RT   "The complete chromosome of Spirosoma linguale DSM 74.";
RL   Submitted (SEP-2009) 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   -!- 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; CP001769; ADB37528.1; -; Genomic_DNA.
DR   AlphaFoldDB; D2QN44; -.
DR   SMR; D2QN44; -.
DR   STRING; 504472.Slin_1478; -.
DR   EnsemblBacteria; ADB37528; ADB37528; Slin_1478.
DR   KEGG; sli:Slin_1478; -.
DR   eggNOG; COG3938; Bacteria.
DR   HOGENOM; CLU_036729_0_0_10; -.
DR   OMA; SHVLWTG; -.
DR   Proteomes; UP000002028; 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.
FT   CHAIN           1..334
FT                   /note="4-hydroxyproline 2-epimerase"
FT                   /id="PRO_0000432278"
FT   ACT_SITE        91
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   ACT_SITE        254
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   BINDING         92..93
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   BINDING         224
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   BINDING         250
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   BINDING         255..256
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
SQ   SEQUENCE   334 AA;  36998 MW;  08ABD30E1FF02F00 CRC64;
     MAEFHFFCID AHTCGNPVRV VTGGSIPFLQ GNSMSEKRQH FLREFDWIRK GLMFEPRGHD
     MMSGSILYPP TDPANDAGVL FIETSGCLPM CGHGTIGTVT VAIEQNLIRP KTPGVLNLEV
     PAGLVRAEYQ QEGKKVTSVK ITNIKSYLAA EKLTVDCPDL GLLTVDVAYG GNFYAIVDPQ
     PNFPGLEHYK AEQLIGWARV MRERMNEQYT FVHPENPTIN GLSHILWTGK PIAETSTARN
     AVFYGDKAID RSPCGTGTSA RMAQWYAQGR LKPGETFVHE SIIGSIFNGR IEAETELANQ
     PAIVPSIEGW ARIHGYNHLI LDEEDPYVFG FQVI