T3HPD_RHIME
ID T3HPD_RHIME Reviewed; 342 AA.
AC Q92WR9;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Trans-3-hydroxy-L-proline dehydratase {ECO:0000303|PubMed:24980702};
DE Short=T3LHyp dehydratase;
DE Short=t3HypD {ECO:0000303|PubMed:24980702};
DE EC=4.2.1.77 {ECO:0000269|PubMed:24980702};
DE AltName: Full=Trans-L-3-hydroxyproline dehydratase;
GN OrderedLocusNames=RB0260; ORFNames=SM_b20270 {ECO:0000312|EMBL:CAC48660.1};
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, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, 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: Catalyzes the dehydration of trans-3-hydroxy-L-proline
CC (t3LHyp) to Delta(1)-pyrroline-2-carboxylate (Pyr2C). Can also catalyze
CC the epimerization of trans-4-hydroxy-L-proline (t4LHyp) to cis-4-
CC hydroxy-D-proline (c4DHyp), albeit with 150-fold lower efficiency. May
CC be involved in the degradation pathway that converts t3LHyp to L-
CC proline, which would allow R.meliloti to grow on t3LHyp as a sole
CC carbon source. Displays no proline racemase activity.
CC {ECO:0000269|PubMed:24980702, ECO:0000305|PubMed:24980702}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=trans-3-hydroxy-L-proline = 1-pyrroline-2-carboxylate + H2O;
CC Xref=Rhea:RHEA:10320, ChEBI:CHEBI:15377, ChEBI:CHEBI:39785,
CC ChEBI:CHEBI:57938; EC=4.2.1.77;
CC Evidence={ECO:0000269|PubMed:24980702};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.8 mM for trans-3-hydroxy-L-proline
CC {ECO:0000269|PubMed:24980702};
CC KM=6.3 mM for trans-4-hydroxy-L-proline
CC {ECO:0000269|PubMed:24980702};
CC Note=kcat is 7.9 sec(-1) for t3LHyp dehydration. kcat is 0.089 sec(-
CC 1) for t4LHyp epimerization. {ECO:0000269|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; CAC48660.1; -; Genomic_DNA.
DR PIR; D95874; D95874.
DR RefSeq; NP_436800.1; NC_003078.1.
DR RefSeq; WP_010975160.1; NC_003078.1.
DR AlphaFoldDB; Q92WR9; -.
DR SMR; Q92WR9; -.
DR STRING; 266834.SM_b20270; -.
DR EnsemblBacteria; CAC48660; CAC48660; SM_b20270.
DR GeneID; 61600275; -.
DR KEGG; sme:SM_b20270; -.
DR PATRIC; fig|266834.11.peg.5184; -.
DR eggNOG; COG3938; Bacteria.
DR HOGENOM; CLU_036729_2_0_5; -.
DR OMA; IMESEEY; -.
DR SABIO-RK; Q92WR9; -.
DR Proteomes; UP000001976; Plasmid pSymB.
DR GO; GO:0050346; F:trans-L-3-hydroxyproline dehydratase 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 Lyase; Plasmid; Reference proteome.
FT CHAIN 1..342
FT /note="Trans-3-hydroxy-L-proline dehydratase"
FT /id="PRO_0000432273"
FT ACT_SITE 90
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:B9K4G4"
FT BINDING 91..92
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B9K4G4"
FT BINDING 252
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B9K4G4"
FT BINDING 257..258
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B9K4G4"
SQ SEQUENCE 342 AA; 36694 MW; C5F3F19FDC6ECF9A CRC64;
MRSTKTIHVI SAHAEGEVGD VIVGGVAPPP GDTIWEQSRW IAREQTLRNF VLNEPRGGVF
RHVNLLVPPK HPDADAAFII MEPEDTPPMS GSNSICVSTV LLDSGILPMK EPVTEITLEA
PGGLVRVRAE CRDGKAERIF VENLPSFAER LDAKLEVEGL GTLTVDTAYG GDSFVIVDAA
AMGFALKPDE AHDIARLGVR ITNAANAKLG FHHPENPDWR HFSFCLFAGP VERTAEGLRA
GAAVAIQPGK VDRSPTGTAL SARMAVLHAR GQMGLSDRLT AVSLIGSTFS GRILGTTEVG
GRPAVLPEIS GRAWITGTHQ HMLDPSDPWP EGYRLTDTWG AR
