ID   4HYPE_STRRD             Reviewed;         333 AA.
AC   D2AV87;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   09-FEB-2010, sequence version 1.
DT   03-AUG-2022, entry version 56.
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=Sros_6004 {ECO:0000312|EMBL:ACZ88738.1};
OS   Streptosporangium roseum (strain ATCC 12428 / DSM 43021 / JCM 3005 / NI
OS   9100).
OC   Bacteria; Actinobacteria; Streptosporangiales; Streptosporangiaceae;
OC   Streptosporangium.
OX   NCBI_TaxID=479432;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12428 / DSM 43021 / JCM 3005 / NI 9100;
RX   PubMed=21304675; DOI=10.4056/sigs.631049;
RA   Nolan M., Sikorski J., Jando M., Lucas S., Lapidus A., Glavina Del Rio T.,
RA   Chen F., Tice H., Pitluck S., Cheng J.F., Chertkov O., Sims D., Meincke L.,
RA   Brettin T., Han C., Detter J.C., Bruce D., Goodwin L., Land M., Hauser L.,
RA   Chang Y.J., Jeffries C.D., Ivanova N., Mavromatis K., Mikhailova N.,
RA   Chen A., Palaniappan K., Chain P., Rohde M., Goker M., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Streptosporangium roseum type strain (NI
RT   9100).";
RL   Stand. Genomic Sci. 2:29-37(2010).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
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}.
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=7.8 mM for trans-4-hydroxy-L-proline
CC         {ECO:0000269|PubMed:24980702};
CC         Note=kcat is 14 sec(-1) for t4LHyp epimerization.
CC         {ECO:0000269|PubMed:24980702};
CC   -!- SIMILARITY: Belongs to the proline racemase family. {ECO:0000305}.
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DR   EMBL; CP001814; ACZ88738.1; -; Genomic_DNA.
DR   RefSeq; WP_012892473.1; NC_013595.1.
DR   AlphaFoldDB; D2AV87; -.
DR   SMR; D2AV87; -.
DR   STRING; 479432.Sros_6004; -.
DR   EnsemblBacteria; ACZ88738; ACZ88738; Sros_6004.
DR   KEGG; sro:Sros_6004; -.
DR   eggNOG; COG3938; Bacteria.
DR   HOGENOM; CLU_036729_0_0_11; -.
DR   OMA; SHVLWTG; -.
DR   OrthoDB; 559014at2; -.
DR   SABIO-RK; D2AV87; -.
DR   Proteomes; UP000002029; Chromosome.
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   Isomerase; Reference proteome.
FT   CHAIN           1..333
FT                   /note="4-hydroxyproline 2-epimerase"
FT                   /id="PRO_0000432251"
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         225
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   333 AA;  35886 MW;  03A162A68D9234F5 CRC64;
     MRTKRVFHAV DSHTEGMPTR VITGGVGVIP GSTMAERREH FLAEMDHVRT LLMYEPRGHS
     AMSGAILQPP TRPDADYGVL YIEVSGCLPM CGHGTIGVAT VLVETGMVEV VEPVTTIRLD
     TPAGLVVAEV RVEDGAATAV TITNVPSFSA GLDRTVKVPG IGEVTYDLAY GGNFYAILPI
     ESVGLPFDRA HKQQILDAGL AIMDAINEQD EPVHPLDAGI RGCHHVQFTA PGSDARHSRH
     AMAIHPGWFD RSPCGTGTSA RMAQLHARGE LPLDTDFVNE SFIGTRFVGR LVEETEVTDL
     PAVVPTITGR AWVTGTAQYF LDPRDPFPEG FLL