4HPE2_AGRRK
ID 4HPE2_AGRRK Reviewed; 332 AA.
AC B9JHU6;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=4-hydroxyproline 2-epimerase 2 {ECO:0000303|PubMed:24980702};
DE Short=4Hyp 2-epimerase 2;
DE Short=4HypE 2 {ECO:0000303|PubMed:24980702};
DE EC=5.1.1.8 {ECO:0000269|PubMed:24980702};
GN OrderedLocusNames=Arad_8151 {ECO:0000312|EMBL:ACM29488.1};
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).
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; CP000629; ACM29488.1; -; Genomic_DNA.
DR RefSeq; WP_012649794.1; NC_011983.1.
DR AlphaFoldDB; B9JHU6; -.
DR SMR; B9JHU6; -.
DR STRING; 311403.Arad_8151; -.
DR EnsemblBacteria; ACM29488; ACM29488; Arad_8151.
DR KEGG; ara:Arad_8151; -.
DR eggNOG; COG3938; Bacteria.
DR HOGENOM; CLU_036729_0_0_5; -.
DR OMA; SHVLWTG; -.
DR OrthoDB; 559014at2; -.
DR Proteomes; UP000001600; 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; Reference proteome.
FT CHAIN 1..332
FT /note="4-hydroxyproline 2-epimerase 2"
FT /id="PRO_0000432279"
FT ACT_SITE 89
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT BINDING 222
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT BINDING 248
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT BINDING 253..254
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q4KGU2"
SQ SEQUENCE 332 AA; 35677 MW; 504ADA031A9B2867 CRC64;
MRRSFFCIDS HTCGNPVRVV AGGGPLLPHV SMAERREIFV RDHDWVRKAL MFEPRGHDIM
SGAIIYPSVR EDCDFAALFI EVSGCLPMCG AGTIGLATVA IEEGLITPRV PGRLSIETPA
GKVDVDYQLK DGFVEAVRLF NVASYLHSRD VVVDVSGLGS LSVDIAYGGN FYAVIEPQEN
WSGLDGMSAS DIVTLSQRLR DALSVVCDPV HPDDERIRGV HHAIWCDAAG SENADGRGAV
FYGDKAIDRS PGGTGTSARM AQLYGRGRLG IGDSFRNESL IGTVFEGRIE GAALVGGIPG
ILPSIGGWAR VIGHNTIFVD ERDPLAHGFQ IR