4HYPE_ROSAD
ID 4HYPE_ROSAD Reviewed; 327 AA.
AC B9R4E3;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 44.
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=SADFL11_2813 {ECO:0000312|EMBL:EEE45524.1};
OS Roseibium alexandrii (strain DSM 17067 / NCIMB 14079 / DFL-11) (Labrenzia
OS alexandrii).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Stappiaceae; Roseibium.
OX NCBI_TaxID=244592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17067 / NCIMB 14079 / DFL-11;
RA Wagner-Dobler I., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
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). Displays no proline
CC 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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.1 mM for trans-4-hydroxy-L-proline
CC {ECO:0000269|PubMed:24980702};
CC Note=kcat is 67 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; EQ973121; EEE45524.1; -; Genomic_DNA.
DR RefSeq; WP_008193519.1; NZ_CM011002.1.
DR AlphaFoldDB; B9R4E3; -.
DR SMR; B9R4E3; -.
DR HOGENOM; CLU_036729_1_0_5; -.
DR OrthoDB; 559014at2; -.
DR SABIO-RK; B9R4E3; -.
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..327
FT /note="4-hydroxyproline 2-epimerase"
FT /id="PRO_0000432259"
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 327 AA; 35075 MW; B2A5B3440A62EE31 CRC64;
MRVIDSHTAG EPTRLVVEGG PDLGPGSLIE KAACLEAEHM DFCASVVLEP RGHDAIIGAL
LLPPSQPDCA AAVIYFNNLQ NLGMCGHATI GLAVTLAHMG RIDPGRHKFE TPVGIVEVDL
QDANTVSVVN VESYRLHKDV TVEVPGHGKV TGDVAWGGNW FFLVKESPFD LTLENVPALT
AYTKTIRQAL ENAGVTGTDC AWIDHIELFG PPKDPFAQSR NFVLCPGGAY DRSPCGTGCS
AKLACLAEDG VLAPGEDWIQ ESVIGSTYRI SYQPGTTKGV IPTITGQAFV TSDAHLIFNP
ADPYRFGIRP QNWTTSWITR TLSVEHG
