ID   4HYPE_BURCM             Reviewed;         311 AA.
AC   Q0B9R9;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=Bamb_3550 {ECO:0000312|EMBL:ABI89104.1};
OS   Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia
OS   (strain AMMD)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=339670;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-244 / AMMD;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K.,
RA   Ramette A., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 2 of Burkholderia cepacia AMMD.";
RL   Submitted (AUG-2006) 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; CP000441; ABI89104.1; -; Genomic_DNA.
DR   RefSeq; WP_011658573.1; NC_008391.1.
DR   AlphaFoldDB; Q0B9R9; -.
DR   SMR; Q0B9R9; -.
DR   STRING; 339670.Bamb_3550; -.
DR   EnsemblBacteria; ABI89104; ABI89104; Bamb_3550.
DR   GeneID; 44694190; -.
DR   KEGG; bam:Bamb_3550; -.
DR   eggNOG; COG3938; Bacteria.
DR   OMA; SHVLWTG; -.
DR   Proteomes; UP000000662; Chromosome 2.
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..311
FT                   /note="4-hydroxyproline 2-epimerase"
FT                   /id="PRO_0000432281"
FT   ACT_SITE        89
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   ACT_SITE        237
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   BINDING         90..91
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   BINDING         209
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   BINDING         233
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   BINDING         238..239
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
SQ   SEQUENCE   311 AA;  32880 MW;  D200CE7D66D8DD52 CRC64;
     MMKRIQIIDS HTGGEPTRLV VSGFPSLGNG TMAERRDVLA REHNRYRTAC ILEPRGSDVM
     VGALLCEPVS PEAAAGVIFF NNSGYLGMCG HGTIGVVRTL HHMGRIEPGV HRIETPVGTV
     EATLHDDLSV SVRNVLAYRH AKAVAVDVPG YGPVKGDIAW GGNWFFLISD HGQRVAGDNV
     AALTAYSSAV REGLERAGIT GANGGEIDHI ELFADDAEHD SRSFVLCPGH AYDRSPCGTG
     TSAKLACLAA DGKLEPGVVW RQASVIGSVF QASYAQADGG IVPTIRGSAH LSAEATLLIE
     EDDPFGWGIV S