T3HPD_BRUSU
ID T3HPD_BRUSU Reviewed; 342 AA.
AC Q8G2I3; G0K693;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=BR0337, BS1330_I0338;
OS Brucella suis biovar 1 (strain 1330).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=204722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=12271122; DOI=10.1073/pnas.192319099;
RA Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT "The Brucella suis genome reveals fundamental similarities between animal
RT and plant pathogens and symbionts.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=22038969; DOI=10.1128/jb.06181-11;
RA Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT "Revised genome sequence of Brucella suis 1330.";
RL J. Bacteriol. 193:6410-6410(2011).
RN [3]
RP LACK OF ENZYMATIC ACTIVITY AS PROLINE RACEMASE AND HYDROXYPROLINE
RP 2-EPIMERASE.
RC STRAIN=1330;
RX PubMed=17849014; DOI=10.1371/journal.pone.0000885;
RA Goytia M., Chamond N., Cosson A., Coatnoan N., Hermant D., Berneman A.,
RA Minoprio P.;
RT "Molecular and structural discrimination of proline racemase and
RT hydroxyproline-2-epimerase from nosocomial and bacterial pathogens.";
RL PLoS ONE 2:E885-E885(2007).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
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) (PubMed:24980702).
CC Displays neither proline racemase activity nor 4-hydroxyproline 2-
CC epimerase activity (PubMed:17849014, PubMed:24980702).
CC {ECO:0000269|PubMed:17849014, ECO:0000269|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=5.1 mM for trans-3-hydroxy-L-proline
CC {ECO:0000269|PubMed:24980702};
CC Note=kcat is 17 sec(-1) for t3LHyp dehydration.
CC {ECO:0000269|PubMed:24980702};
CC -!- SIMILARITY: Belongs to the proline racemase family. {ECO:0000305}.
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DR EMBL; AE014291; AAN29286.1; -; Genomic_DNA.
DR EMBL; CP002997; AEM17699.1; -; Genomic_DNA.
DR RefSeq; WP_002966688.1; NZ_KN046804.1.
DR AlphaFoldDB; Q8G2I3; -.
DR SMR; Q8G2I3; -.
DR EnsemblBacteria; AEM17699; AEM17699; BS1330_I0338.
DR GeneID; 45051462; -.
DR KEGG; bms:BR0337; -.
DR KEGG; bsi:BS1330_I0338; -.
DR PATRIC; fig|204722.21.peg.2497; -.
DR HOGENOM; CLU_036729_2_0_5; -.
DR OMA; IMESEEY; -.
DR PhylomeDB; Q8G2I3; -.
DR SABIO-RK; Q8G2I3; -.
DR Proteomes; UP000007104; Chromosome I.
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.
FT CHAIN 1..342
FT /note="Trans-3-hydroxy-L-proline dehydratase"
FT /id="PRO_0000354045"
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 251
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B9K4G4"
FT BINDING 256..257
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B9K4G4"
SQ SEQUENCE 342 AA; 36941 MW; 1982D458A78AAE8A CRC64;
MRSTKVIHIV GCHAEGEVGD VIVGGVAPPP GETVWEQSRF IANDETLRNF VLNEPRGGVF
RHVNLLVPPK DPRAQMGFII MEPADTPPMS GSNSICVSTV LLDSGIIAMQ EPVTHMVLEA
PGGIIEVEAE CRNGKAERIS VRNVPSFADR LDAPLDVTGL GTIMVDTAYG GDSFVIVDAA
QIGMKIEPGQ ARELAEIGVK ITKAANEQLG FRHPERDWRH ISFCQITEPV TREGDVLTGV
NTVAIRPAKL DRSPTGTGCS ARMAVLHAKG QMKAGERFIG KSVLGTEFHC RLDKVLELGG
KPAISPIISG RAWVTGTSQL MLDPSDPFPH GYRLSDTWPR DE
