ID   T3HPD_BURCM             Reviewed;         335 AA.
AC   Q0B950;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=Bamb_3769 {ECO:0000312|EMBL:ABI89323.1};
OS   Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia
OS   (strain AMMD)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=339670;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-244 / AMMD;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K.,
RA   Ramette A., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 2 of Burkholderia cepacia AMMD.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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       Displays neither trans-4-hydroxy-L-proline (t4LHyp) epimerase nor
CC       proline racemase activity. {ECO:0000269|PubMed:24980702, ECO:0000305}.
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=13 mM for trans-4-hydroxy-L-proline {ECO:0000269|PubMed:24980702};
CC         Note=kcat is 43 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; CP000441; ABI89323.1; -; Genomic_DNA.
DR   RefSeq; WP_011658778.1; NZ_CP009799.1.
DR   AlphaFoldDB; Q0B950; -.
DR   SMR; Q0B950; -.
DR   STRING; 339670.Bamb_3769; -.
DR   EnsemblBacteria; ABI89323; ABI89323; Bamb_3769.
DR   GeneID; 44694405; -.
DR   KEGG; bam:Bamb_3769; -.
DR   PATRIC; fig|339670.21.peg.4013; -.
DR   eggNOG; COG3938; Bacteria.
DR   OMA; ERRAYCM; -.
DR   SABIO-RK; Q0B950; -.
DR   Proteomes; UP000000662; Chromosome 2.
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..335
FT                   /note="Trans-3-hydroxy-L-proline dehydratase"
FT                   /id="PRO_0000432252"
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         251
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;  36384 MW;  5D3585FE9AB13BFB CRC64;
     MKISRSLSTV EVHTGGEAFR IVTSGLPRLP GDTIVQRRAW LKENADEIRR ALMFEPRGHA
     DMYGGYLTEP VSPTADFGVI FLHNEGYSDH CGHGVIALST AAVELGWVQR TVPETRVGID
     APCGFIEAFV QWDGEHAGPV RFVNVPSFIW RRDVSVDTPS FGTVTGDIAY GGAFYFYVDG
     APFDLPVREA AVEKLIRFGA EVKAAANAKY PVVHPEIPEI NHIYGTIIAN APRHPGSTQA
     NCCVFADREV DRSPTGSGTG GRVAQLYQRG VLAAGDTLVN ESIVGTVFKG RVLRETMVGD
     IPAVIPEVEG SAHICGFANW IVDERDPLTY GFLVR