ID   T3HPD_BURCH             Reviewed;         335 AA.
AC   A0B0B8;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Trans-3-hydroxy-L-proline dehydratase {ECO:0000250|UniProtKB:V5YXI5};
DE            Short=T3LHyp dehydratase {ECO:0000250|UniProtKB:V5YXI5};
DE            Short=t3HypD;
DE            EC=4.2.1.77 {ECO:0000250|UniProtKB:V5YXI5};
DE   AltName: Full=Trans-L-3-hydroxyproline dehydratase;
GN   Name=lhpH {ECO:0000250|UniProtKB:V5YXI5}; OrderedLocusNames=Bcen2424_4360;
OS   Burkholderia cenocepacia (strain HI2424).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=331272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HI2424;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., LiPuma J.J., Gonzalez C.F.,
RA   Konstantinidis K., Tiedje J.M., Richardson P.;
RT   "Complete sequence of chromosome 2 of Burkholderia cenocepacia HI2424.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   LACK OF ENZYMATIC ACTIVITY AS PROLINE RACEMASE AND
RP   HYDROXYPROLINE-2-EPIMERASE.
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).
CC   -!- FUNCTION: Catalyzes the dehydration of trans-3-hydroxy-L-proline
CC       (t3LHyp) to Delta(1)-pyrroline-2-carboxylate (Pyr2C) (By similarity).
CC       Does not possess neither proline racemase nor 4-hydroxyproline 2-
CC       epimerase activities (PubMed:17849014). {ECO:0000250|UniProtKB:V5YXI5,
CC       ECO:0000269|PubMed:17849014}.
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:0000250|UniProtKB:V5YXI5};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:V5YXI5}.
CC   -!- SIMILARITY: Belongs to the proline racemase family. {ECO:0000305}.
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DR   EMBL; CP000459; ABK11094.1; -; Genomic_DNA.
DR   RefSeq; WP_011547736.1; NC_008543.1.
DR   AlphaFoldDB; A0B0B8; -.
DR   SMR; A0B0B8; -.
DR   KEGG; bch:Bcen2424_4360; -.
DR   HOGENOM; CLU_036729_0_0_4; -.
DR   OMA; ERRAYCM; -.
DR   OrthoDB; 559014at2; -.
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..335
FT                   /note="Trans-3-hydroxy-L-proline dehydratase"
FT                   /id="PRO_0000354046"
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         222
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   BINDING         256..257
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
SQ   SEQUENCE   335 AA;  36329 MW;  54CD49CF5A808D1E CRC64;
     MKISRSLSTV EVHTGGEAFR IVTSGLPRLP GDTIVQRRAW LKAHADEIRR ALMFEPRGHA
     DMYGGYLTEP VSPNADFGVI FVHNEGYSDH CGHGVIALST AAVELGWVQR TVPETRVGID
     APCGFIEAFV QWDGEHAGPV RFVNVPSFIW RRDVSVDTPS FGTVTGDIAY GGAFYFYVDG
     APFDLPVRES AVEKLIRFGA EVKAAANATY PVVHPEIPEI NHIYGTIIAN APRHAGSTQA
     NCCVFADREV DRSPTGSGTG GRVAQLYQRG LLAAGDTLVN ESIVGTVFKG RVLRETTVGD
     FPAVIPEVEG SAHICGFANW IVDERDPLTY GFLVR