ID   T3HPD_AZOBR             Reviewed;         335 AA.
AC   V5YXI5;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   19-FEB-2014, sequence version 1.
DT   03-AUG-2022, entry version 18.
DE   RecName: Full=Trans-3-hydroxy-L-proline dehydratase {ECO:0000303|PubMed:24649405};
DE            Short=T3LHyp dehydratase {ECO:0000303|PubMed:24649405};
DE            Short=t3HypD;
DE            EC=4.2.1.77 {ECO:0000269|PubMed:24649405};
DE   AltName: Full=Trans-L-3-hydroxyproline dehydratase;
GN   Name=lhpH {ECO:0000303|PubMed:24649405};
OS   Azospirillum brasilense.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBUNIT,
RP   BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, AND PATHWAY.
RC   STRAIN=ATCC 29145 / DSM 1690 / IMET 11303 / Sp7;
RX   PubMed=24649405; DOI=10.1016/j.fob.2014.02.010;
RA   Watanabe S., Tanimoto Y., Yamauchi S., Tozawa Y., Sawayama S., Watanabe Y.;
RT   "Identification and characterization of trans-3-hydroxy-L-proline
RT   dehydratase and Delta(1)-pyrroline-2-carboxylate reductase involved in
RT   trans-3-hydroxy-L-proline metabolism of bacteria.";
RL   FEBS Open Bio 4:240-250(2014).
CC   -!- FUNCTION: Catalyzes the dehydration of trans-3-hydroxy-L-proline
CC       (t3LHyp) to Delta(1)-pyrroline-2-carboxylate (Pyr2C). Together with
CC       LhpI, is involved in a t3LHyp degradation pathway to L-proline, which
CC       allows A.brasilense to grow on t3LHyp as a sole carbon source.
CC       {ECO:0000269|PubMed:24649405}.
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:24649405};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8.0-9.5. {ECO:0000269|PubMed:24649405};
CC   -!- PATHWAY: Amino-acid degradation. {ECO:0000269|PubMed:24649405}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:24649405}.
CC   -!- INDUCTION: Induced by T3LHyp, D-proline and D-lysine, but not by trans-
CC       4-hydroxy-L-proline (T4LHyp) and L-proline.
CC       {ECO:0000269|PubMed:24649405}.
CC   -!- SIMILARITY: Belongs to the proline racemase family. {ECO:0000305}.
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DR   EMBL; AB894494; BAO21621.1; -; Genomic_DNA.
DR   AlphaFoldDB; V5YXI5; -.
DR   SMR; V5YXI5; -.
DR   BioCyc; MetaCyc:MON-18702; -.
DR   BRENDA; 4.2.1.77; 611.
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_0000432241"
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         256..257
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
SQ   SEQUENCE   335 AA;  36325 MW;  F37E9E7DD3316831 CRC64;
     MKITRSLSTV EVHTGGEAFR IVTSGLPRAP GDTIVQRRAW LKENADEIRR ALMFEPRGHA
     DMYGGYLTEP VSPNADFGVI FVHNEGYSDH CGHGVIALST AAVELGWVQR TVPETRVGID
     APCGFIEAFV KWDGEHAGPV RFVNVPSFIW QRDVSVETPS FGTVTGDIAY GGAFYFYVDG
     APFDLPVREA AVEKLIRFGA EVKAAANAKY PVVHPEIPEI NHIYGTIIAN APRHPGSTQA
     NCCVFADREV DRSPTGSGTG GRVAQLYQRG LLAAGDTLVN ESIVGTVFKG RVLRETTVGD
     IPAVIPEVEG SAHICGFANW IVDERDPLTY GFLVR