ID   T3HPD_BACC1             Reviewed;         334 AA.
AC   Q73CS0;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=BCE_0994 {ECO:0000312|EMBL:AAS39925.1};
OS   Bacillus cereus (strain ATCC 10987 / NRS 248).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=222523;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10987 / NRS 248;
RX   PubMed=14960714; DOI=10.1093/nar/gkh258;
RA   Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA   Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F.,
RA   Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.;
RT   "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT   adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL   Nucleic Acids Res. 32:977-988(2004).
RN   [2]
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). Is likely
CC       involved in a degradation pathway that converts t3LHyp to L-proline.
CC       Can also catalyze the epimerization of trans-4-hydroxy-L-proline
CC       (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp) in vitro. Displays no
CC       proline racemase activity. {ECO:0000269|PubMed:24980702,
CC       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=3.2 mM for trans-4-hydroxy-L-proline
CC         {ECO:0000269|PubMed:24980702};
CC         Note=kcat is 1.2 sec(-1) for t4LHyp epimerization. The reaction of
CC         t3LHyp dehydration is too slow to measure kinetic parameters.
CC         {ECO:0000269|PubMed:24980702};
CC   -!- SIMILARITY: Belongs to the proline racemase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE017194; AAS39925.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q73CS0; -.
DR   SMR; Q73CS0; -.
DR   EnsemblBacteria; AAS39925; AAS39925; BCE_0994.
DR   KEGG; bca:BCE_0994; -.
DR   HOGENOM; CLU_036729_0_0_9; -.
DR   OMA; ERRAYCM; -.
DR   SABIO-RK; Q73CS0; -.
DR   Proteomes; UP000002527; Chromosome.
DR   GO; GO:0050346; F:trans-L-3-hydroxyproline dehydratase 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   Lyase.
FT   CHAIN           1..334
FT                   /note="Trans-3-hydroxy-L-proline dehydratase"
FT                   /id="PRO_0000432268"
FT   ACT_SITE        91
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   BINDING         92..93
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   BINDING         250
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   BINDING         255..256
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
SQ   SEQUENCE   334 AA;  36889 MW;  EA569001FFA4FF74 CRC64;
     MKVSKVYTTI DAHVAGEPLR IITGGVPEIK GETQLERRAY CMEHLDHLRE ILMYEPRGHH
     GMYGCIITPP ASAHADFGVL FMHNEGWSTM CGHGIIAVIT VGIETGMFEV TGEKQKFIID
     SPAGEVIAYA TYRGSEVESV SFENVPSFVY KKDVPIKIDD YEFQVDIAFG GAFYAVVDSK
     EFGLKVDFND LPAIQTWGGK IKHYIESKME VKHPLEEGLK GIYGVIFSDE PKGKDATLRN
     VTIFADGQVD RSPCGTGTSA RIATLFEKGI LQKGEIFIHE CITEGKFEGE VLSVTAVHTY
     EAVVPKITGN AFITGFHQFV VDPRDDLNRG FLLG