4HYPE_AGRVS
ID 4HYPE_AGRVS Reviewed; 347 AA.
AC B9JQV3;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 63.
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=Avi_0518 {ECO:0000312|EMBL:ACM35366.1};
OS Agrobacterium vitis (strain S4 / ATCC BAA-846) (Rhizobium vitis (strain
OS S4)).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium.
OX NCBI_TaxID=311402;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S4 / ATCC BAA-846;
RX PubMed=19251847; DOI=10.1128/jb.01779-08;
RA Slater S.C., Goldman B.S., Goodner B., Setubal J.C., Farrand S.K.,
RA Nester E.W., Burr T.J., Banta L., Dickerman A.W., Paulsen I., Otten L.,
RA Suen G., Welch R., Almeida N.F., Arnold F., Burton O.T., Du Z., Ewing A.,
RA Godsy E., Heisel S., Houmiel K.L., Jhaveri J., Lu J., Miller N.M.,
RA Norton S., Chen Q., Phoolcharoen W., Ohlin V., Ondrusek D., Pride N.,
RA Stricklin S.L., Sun J., Wheeler C., Wilson L., Zhu H., Wood D.W.;
RT "Genome sequences of three Agrobacterium biovars help elucidate the
RT evolution of multichromosome genomes in bacteria.";
RL J. Bacteriol. 191:2501-2511(2009).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH
RP TRANS-4-HYDROXY-L-PROLINE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND ACTIVE SITE.
RC STRAIN=S4 / ATCC BAA-846;
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. Can also catalyze the epimerization of
CC trans-3-hydroxy-L-proline (t3LHyp) to cis-3-hydroxy-D-proline (c3DHyp)
CC in vitro. 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=5.6 mM for trans-4-hydroxy-L-proline
CC {ECO:0000269|PubMed:24980702};
CC KM=4.8 mM for trans-3-hydroxy-L-proline
CC {ECO:0000269|PubMed:24980702};
CC Note=kcat is 1.3 sec(-1) for t4LHyp epimerization. kcat is 0.75 sec(-
CC 1) for t3LHyp epimerization. {ECO:0000269|PubMed:24980702};
CC -!- SIMILARITY: Belongs to the proline racemase family. {ECO:0000305}.
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DR EMBL; CP000633; ACM35366.1; -; Genomic_DNA.
DR RefSeq; WP_015914794.1; NC_011989.1.
DR PDB; 4LB0; X-ray; 1.70 A; A/B=1-347.
DR PDBsum; 4LB0; -.
DR AlphaFoldDB; B9JQV3; -.
DR SMR; B9JQV3; -.
DR STRING; 311402.Avi_0518; -.
DR EnsemblBacteria; ACM35366; ACM35366; Avi_0518.
DR KEGG; avi:Avi_0518; -.
DR eggNOG; COG3938; Bacteria.
DR HOGENOM; CLU_036729_2_0_5; -.
DR OMA; ERRAYCM; -.
DR OrthoDB; 559014at2; -.
DR SABIO-RK; B9JQV3; -.
DR Proteomes; UP000001596; Chromosome 1.
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 3D-structure; Isomerase; Reference proteome.
FT CHAIN 1..347
FT /note="4-hydroxyproline 2-epimerase"
FT /id="PRO_0000432249"
FT ACT_SITE 93
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:24980702"
FT ACT_SITE 255
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:24980702"
FT BINDING 85
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:24980702"
FT BINDING 94..95
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:24980702"
FT BINDING 251
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:24980702"
FT BINDING 256..257
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:24980702"
FT STRAND 3..14
FT /evidence="ECO:0007829|PDB:4LB0"
FT STRAND 17..25
FT /evidence="ECO:0007829|PDB:4LB0"
FT HELIX 34..43
FT /evidence="ECO:0007829|PDB:4LB0"
FT HELIX 45..55
FT /evidence="ECO:0007829|PDB:4LB0"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:4LB0"
FT STRAND 78..84
FT /evidence="ECO:0007829|PDB:4LB0"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:4LB0"
FT HELIX 94..106
FT /evidence="ECO:0007829|PDB:4LB0"
FT STRAND 114..123
FT /evidence="ECO:0007829|PDB:4LB0"
FT STRAND 126..135
FT /evidence="ECO:0007829|PDB:4LB0"
FT STRAND 138..145
FT /evidence="ECO:0007829|PDB:4LB0"
FT STRAND 149..160
FT /evidence="ECO:0007829|PDB:4LB0"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:4LB0"
FT STRAND 164..181
FT /evidence="ECO:0007829|PDB:4LB0"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:4LB0"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:4LB0"
FT HELIX 194..211
FT /evidence="ECO:0007829|PDB:4LB0"
FT STRAND 223..233
FT /evidence="ECO:0007829|PDB:4LB0"
FT STRAND 239..245
FT /evidence="ECO:0007829|PDB:4LB0"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:4LB0"
FT HELIX 256..268
FT /evidence="ECO:0007829|PDB:4LB0"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:4LB0"
FT STRAND 287..298
FT /evidence="ECO:0007829|PDB:4LB0"
FT STRAND 301..310
FT /evidence="ECO:0007829|PDB:4LB0"
FT STRAND 312..321
FT /evidence="ECO:0007829|PDB:4LB0"
FT HELIX 335..338
FT /evidence="ECO:0007829|PDB:4LB0"
FT HELIX 340..343
FT /evidence="ECO:0007829|PDB:4LB0"
SQ SEQUENCE 347 AA; 37177 MW; 6EADF45506229AA7 CRC64;
MRWKRMMQLL DVHCEGEIGK VAIGGVPKIP GDTVADQLHW LNTDPKGREL RHFLVLEPRG
APIGSVNLLL PAKDSRADAA FIILQPDQAH ASSGSNSICV TTALLESGMI EMQEPETVVM
LETAAGLVKA VAQCRDGHCD SVTLTMVPSF VHELDAQIAT ESWGEIRFDL AYGGVFYALV
DVRQLGLTIE PGNARRLVEA GMLLKGEINQ RIQVVHPDIP AISGVAYVMF RDEDPDGAVR
TCTTMWPGRV DRSPCGTGNS ANLATLHARG RVKPGDSFLS RSIIGSQFTV GLQGLTTVAG
RSAVIPTITG RGFTYGIHQV ALDAFDPLGG GFVLTDVWGA AAETIKI
