4HPE1_AGRRK
ID 4HPE1_AGRRK Reviewed; 345 AA.
AC B9J8G8;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=4-hydroxyproline 2-epimerase 1 {ECO:0000303|PubMed:24980702};
DE Short=4Hyp 2-epimerase 1;
DE Short=4HypE 1 {ECO:0000303|PubMed:24980702};
DE EC=5.1.1.8 {ECO:0000269|PubMed:24980702};
GN OrderedLocusNames=Arad_0731 {ECO:0000312|EMBL:ACM25355.1};
OS Agrobacterium radiobacter (strain K84 / ATCC BAA-868).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=311403;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K84 / ATCC BAA-868;
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 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).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS).
RG Enzyme Function Initiative (EFI);
RA Patskovsky Y., Toro R., Bhosle R., Al Obaidi N.F., Morisco L.L.,
RA Wasserman S.R., Sojitra S., Stead M., Washington E., Glenn A.S.,
RA Chowdhury S., Evans B., Hammonds J., Hillerich B., Love J., Seidel R.D.,
RA Gerlt J.A., Almo S.C.;
RT "Crystal structure of proline racemase Arad_0731 from Agrobacterium
RT radiobacter, target Efi-506561.";
RL Submitted (APR-2014) to the PDB data bank.
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 -!- SIMILARITY: Belongs to the proline racemase family. {ECO:0000305}.
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DR EMBL; CP000628; ACM25355.1; -; Genomic_DNA.
DR RefSeq; WP_012650895.1; NC_011985.1.
DR PDB; 4Q2H; X-ray; 1.80 A; A/B=1-345.
DR PDBsum; 4Q2H; -.
DR AlphaFoldDB; B9J8G8; -.
DR SMR; B9J8G8; -.
DR STRING; 311403.Arad_0731; -.
DR EnsemblBacteria; ACM25355; ACM25355; Arad_0731.
DR KEGG; ara:Arad_0731; -.
DR eggNOG; COG3938; Bacteria.
DR HOGENOM; CLU_036729_2_0_5; -.
DR OMA; ERRAYCM; -.
DR OrthoDB; 559014at2; -.
DR Proteomes; UP000001600; 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..345
FT /note="4-hydroxyproline 2-epimerase 1"
FT /id="PRO_0000432266"
FT ACT_SITE 93
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:B9JQV3"
FT ACT_SITE 255
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:B9JQV3"
FT BINDING 85
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B9JQV3"
FT BINDING 94..95
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B9JQV3"
FT BINDING 251
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B9JQV3"
FT BINDING 256..257
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B9JQV3"
FT STRAND 6..14
FT /evidence="ECO:0007829|PDB:4Q2H"
FT STRAND 17..24
FT /evidence="ECO:0007829|PDB:4Q2H"
FT HELIX 34..43
FT /evidence="ECO:0007829|PDB:4Q2H"
FT HELIX 45..55
FT /evidence="ECO:0007829|PDB:4Q2H"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:4Q2H"
FT STRAND 78..84
FT /evidence="ECO:0007829|PDB:4Q2H"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:4Q2H"
FT HELIX 94..106
FT /evidence="ECO:0007829|PDB:4Q2H"
FT STRAND 114..123
FT /evidence="ECO:0007829|PDB:4Q2H"
FT STRAND 126..135
FT /evidence="ECO:0007829|PDB:4Q2H"
FT STRAND 138..145
FT /evidence="ECO:0007829|PDB:4Q2H"
FT STRAND 149..160
FT /evidence="ECO:0007829|PDB:4Q2H"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:4Q2H"
FT STRAND 164..181
FT /evidence="ECO:0007829|PDB:4Q2H"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:4Q2H"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:4Q2H"
FT HELIX 194..211
FT /evidence="ECO:0007829|PDB:4Q2H"
FT STRAND 223..233
FT /evidence="ECO:0007829|PDB:4Q2H"
FT STRAND 239..245
FT /evidence="ECO:0007829|PDB:4Q2H"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:4Q2H"
FT HELIX 256..268
FT /evidence="ECO:0007829|PDB:4Q2H"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:4Q2H"
FT STRAND 287..298
FT /evidence="ECO:0007829|PDB:4Q2H"
FT STRAND 301..310
FT /evidence="ECO:0007829|PDB:4Q2H"
FT STRAND 312..321
FT /evidence="ECO:0007829|PDB:4Q2H"
FT TURN 327..330
FT /evidence="ECO:0007829|PDB:4Q2H"
FT HELIX 335..338
FT /evidence="ECO:0007829|PDB:4Q2H"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:4Q2H"
SQ SEQUENCE 345 AA; 36792 MW; F6C0BC5DF3E5DDE3 CRC64;
MRWKRTIQLL DVHCEGEIGR VAIGGVPKIP GNTVAEQLHW LNTDPKGEEL RRFLVLEPRG
APIGSVNLLL PARHPDADAA FIILQPDQAH ASSGSNSICV TTALLESGIV EMKEPETVVT
LETAAGLVRA TATCRDGRCE KVRLTMVPSF VHELDVGIDT PQWGRIKLDL CYGGIFYALV
DVGQIGLTIG KANAASLVQA GMVLKELINR TVPVVHPEIP AISGVAYVMF RDIDADGAIR
TCTTMWPGRA DRSPCGTGNS ANLATLHARG KARVGDVFKS RSIIGSEFEV GLQAETEVAG
KPAIIPTITG RGFTFGLSQV ALDPFDPMAN GFALTDVWGP LAGDI
