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   27-MAR-2024, entry version 86.
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; Pseudomonadota; 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   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   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; TRANS-3-HYDROXY-L-PROLINE DEHYDRATASE; 1.
DR   PANTHER; PTHR33442:SF5; TRANS-3-HYDROXY-L-PROLINE DEHYDRATASE-RELATED; 1.
DR   Pfam; PF05544; Pro_racemase; 1.
DR   PIRSF; PIRSF029792; Pro_racemase; 1.
DR   SFLD; SFLDS00028; Proline_Racemase; 1.
DR   SUPFAM; SSF54506; Diaminopimelate epimerase-like; 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
//