ID   4HYPE_ROSAI             Reviewed;         310 AA.
AC   A0NXQ7;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 64.
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   ORFNames=SIAM614_28492 {ECO:0000312|EMBL:EAV42584.1};
OS   Roseibium aggregatum (strain ATCC 25650 / DSM 13394 / JCM 20685 / NBRC
OS   16684 / NCIMB 2208 / IAM 12614 / B1) (Stappia aggregata).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Stappiaceae; Roseibium.
OX   NCBI_TaxID=384765;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25650 / DSM 13394 / JCM 20685 / NBRC 16684 / NCIMB 2208 / IAM
RC   12614 / B1;
RA   King G., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION.
RC   STRAIN=ATCC 25650 / DSM 13394 / JCM 20685 / NBRC 16684 / NCIMB 2208 / IAM
RC   12614 / B1;
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). May be involved in a
CC       degradation pathway of t4LHyp, which would allow L.aggregata to grow on
CC       t4LHyp as a sole carbon source. Displays no proline racemase activity.
CC       {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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=3.2 mM for trans-4-hydroxy-L-proline
CC         {ECO:0000269|PubMed:24980702};
CC         Note=kcat is 55 sec(-1) for t4LHyp epimerization.
CC         {ECO:0000269|PubMed:24980702};
CC   -!- INDUCTION: Is up-regulated when the bacterium is grown on t4LHyp or
CC       t3LHyp as sole carbon source. {ECO:0000269|PubMed:24980702}.
CC   -!- SIMILARITY: Belongs to the proline racemase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AAUW01000014; EAV42584.1; -; Genomic_DNA.
DR   RefSeq; WP_006937102.1; NZ_AAUW01000014.1.
DR   AlphaFoldDB; A0NXQ7; -.
DR   SMR; A0NXQ7; -.
DR   eggNOG; COG3938; Bacteria.
DR   OrthoDB; 559014at2; -.
DR   SABIO-RK; A0NXQ7; -.
DR   Proteomes; UP000004848; Unassembled WGS sequence.
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.
FT   CHAIN           1..310
FT                   /note="4-hydroxyproline 2-epimerase"
FT                   /id="PRO_0000432258"
FT   ACT_SITE        85
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   ACT_SITE        235
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   BINDING         86..87
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   BINDING         205
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   BINDING         231
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   BINDING         236..237
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
SQ   SEQUENCE   310 AA;  32363 MW;  84AC6189EF659B3B CRC64;
     MRVIDSHTAG EPTRVVLDGG PDLGSGTLAE RAARLEAEHL DFCASVVLEP RGHDAIIGAL
     LVPPSDPACA AGVIYFNNLQ NLGMCGHATI GLGVTLAHLG RIRPGRHRFE TPVGVVEIDL
     IDANTVSVVN IESYRLAKDV TVEVEGVGPV TGDVAWGGNW FFLVKNSPIA LTGANIRPLT
     DLTLKIRTAL EKAGVTGKDG AWIDHIELFG PAEDPAAQSR NFVLCPGGAY DRSPCGTGCS
     AKLACLAADG ALAPGQDYLQ ESVIGSTYKI SYQPGPGGGV IPTITGQAFV TSDATLIFNP
     ADPYRSGIRL