4HYPE_BURP1
ID 4HYPE_BURP1 Reviewed; 320 AA.
AC Q3JHA9;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, 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=BURPS1710b_A1887 {ECO:0000312|EMBL:ABA51537.1};
OS Burkholderia pseudomallei (strain 1710b).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=320372;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1710b;
RX PubMed=20333227; DOI=10.1093/gbe/evq003;
RA Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA Nierman W.C.;
RT "Continuing evolution of Burkholderia mallei through genome reduction and
RT large-scale rearrangements.";
RL Genome Biol. Evol. 2:102-116(2010).
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; CP000125; ABA51537.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3JHA9; -.
DR SMR; Q3JHA9; -.
DR EnsemblBacteria; ABA51537; ABA51537; BURPS1710b_A1887.
DR KEGG; bpm:BURPS1710b_A1887; -.
DR HOGENOM; CLU_036729_1_0_4; -.
DR OMA; SHVLWTG; -.
DR Proteomes; UP000002700; Chromosome II.
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..320
FT /note="4-hydroxyproline 2-epimerase"
FT /id="PRO_0000432288"
FT ACT_SITE 98
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT ACT_SITE 246
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT BINDING 99..100
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT BINDING 218
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT BINDING 242
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT BINDING 247..248
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q4KGU2"
SQ SEQUENCE 320 AA; 33363 MW; 4365AF6F0196E6F2 CRC64;
MRISTLDRRD MKHIHIIDSH TGGEPTRVVV SGFPALGGGT MAERLAVLAR EHDRYRAACI
LEPRGSDVLV GALLCEPVSA GAAAGVIFFN NAGYLGMCGH GTIGLVRTLH HMGRIGPGVH
RIETPVGDVE ATLHDDLSVS VRNVLAYRHA KDVVVDVPGH GAVTGDVAWG GNWFFLVSDH
GQRVAGENVA ALAAYASAVR AALERAGVTG RDGAPIDHIE LFADDPEYDS RSFVLCPGHA
YDRSPCGTGT SAKLACLAAD GKLAAGVTWR QASVIGSVFS ASYAAAEGGV VPTIRGSAHL
SAEATLVIED DDPFGWGIAS
