4HYPE_RHIME
ID 4HYPE_RHIME Reviewed; 333 AA.
AC Q92WS1;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Probable 4-hydroxyproline 2-epimerase {ECO:0000305|PubMed:24980702};
DE Short=4Hyp 2-epimerase;
DE Short=4HypE {ECO:0000303|PubMed:24980702};
DE EC=5.1.1.8 {ECO:0000305|PubMed:24980702};
GN OrderedLocusNames=RB0258; ORFNames=SM_b20268 {ECO:0000312|EMBL:CAC48658.1};
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OG Plasmid pSymB (megaplasmid 2).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481431; DOI=10.1073/pnas.161294698;
RA Finan T.M., Weidner S., Wong K., Buhrmester J., Chain P., Vorhoelter F.J.,
RA Hernandez-Lucas I., Becker A., Cowie A., Gouzy J., Golding B., Puehler A.;
RT "The complete sequence of the 1,683-kb pSymB megaplasmid from the N2-fixing
RT endosymbiont Sinorhizobium meliloti.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9889-9894(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
RN [3]
RP FUNCTION, AND INDUCTION.
RC STRAIN=1021;
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: Likely catalyzes the epimerization of trans-4-hydroxy-L-
CC proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp). May be involved
CC in the degradation pathway that converts t4LHyp to alpha-ketoglutarate,
CC which would allow R.meliloti to grow on t4LHyp as a sole carbon source.
CC {ECO:0000305|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:0000305|PubMed:24980702};
CC -!- INDUCTION: Is slightly up-regulated when the bacterium is grown on
CC t4LHyp or t3LHyp as sole carbon source. {ECO:0000269|PubMed:24980702}.
CC -!- SIMILARITY: Belongs to the proline racemase family. {ECO:0000305}.
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DR EMBL; AL591985; CAC48658.1; -; Genomic_DNA.
DR PIR; B95874; B95874.
DR RefSeq; NP_436798.1; NC_003078.1.
DR RefSeq; WP_010975158.1; NC_003078.1.
DR AlphaFoldDB; Q92WS1; -.
DR SMR; Q92WS1; -.
DR STRING; 266834.SM_b20268; -.
DR EnsemblBacteria; CAC48658; CAC48658; SM_b20268.
DR GeneID; 61600273; -.
DR KEGG; sme:SM_b20268; -.
DR PATRIC; fig|266834.11.peg.5182; -.
DR eggNOG; COG3938; Bacteria.
DR HOGENOM; CLU_036729_0_0_5; -.
DR OMA; SHVLWTG; -.
DR Proteomes; UP000001976; Plasmid pSymB.
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 2: Evidence at transcript level;
KW Isomerase; Plasmid; Reference proteome.
FT CHAIN 1..333
FT /note="Probable 4-hydroxyproline 2-epimerase"
FT /id="PRO_0000432274"
FT ACT_SITE 90
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT ACT_SITE 253
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT BINDING 91..92
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT BINDING 223
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT BINDING 249
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT BINDING 254..255
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q4KGU2"
SQ SEQUENCE 333 AA; 36243 MW; C27C39B216956B51 CRC64;
MATHTFSCID GHTCGNPVRL VSGGGPRLEG ANMLEKRAHF LKEFDWIRTG LMFEPRGHDM
MSGSILYPPT RPDCDVAVLF IETSGCLPMC GHGTIGTITM GIENGLITPR EPGKLSIDAP
AGKVDITYRQ EGRFVEEVRL TNVPSFLYAE GLAAEVEGLG EIVVDVAYGG NFYAIVEPQK
NFRDMADHTA GELVGWSPKL RAALNAKYEF VHPEHPEIRG LSHIQWTGKP TQPEAHARNA
VFYGEKAIDR SPCGTGTSAR IAQLAAKGKL KVGDEFVHES IIGSLFKGRV EAAAKVADRD
AIIPSIAGWA RMTGINTIFI DDRDPFAHGF VVR
