ID   T3HPD_PONAB             Reviewed;         354 AA.
AC   Q5RC28;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Trans-L-3-hydroxyproline dehydratase;
DE            EC=4.2.1.77;
DE   AltName: Full=Trans-3-hydroxy-L-proline dehydratase;
GN   Name=L3HYPDH;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the dehydration of trans-3-hydroxy-L-proline to
CC       delta-1-pyrroline-2-carboxylate (Pyr2C). {ECO:0000250}.
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   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- MISCELLANEOUS: In contrast to the T.cruzi proline racemase enzyme,
CC       lacks the conserved Cys at position 273 which is replaced by a Thr
CC       residue, transforming the racemase activity into dehydratase activity.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the proline racemase family. {ECO:0000305}.
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DR   EMBL; CR858454; CAH90682.1; -; mRNA.
DR   RefSeq; NP_001125373.1; NM_001131901.2.
DR   AlphaFoldDB; Q5RC28; -.
DR   SMR; Q5RC28; -.
DR   GeneID; 100172276; -.
DR   KEGG; pon:100172276; -.
DR   CTD; 112849; -.
DR   InParanoid; Q5RC28; -.
DR   OrthoDB; 894373at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0016836; F:hydro-lyase activity; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   Lyase; Reference proteome.
FT   CHAIN           1..354
FT                   /note="Trans-L-3-hydroxyproline dehydratase"
FT                   /id="PRO_0000288951"
FT   ACT_SITE        104
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         105..106
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         269
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         274..275
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   354 AA;  38091 MW;  4CDC5502284E5B65 CRC64;
     MESALALPRL PPHDPGTPVL SVVDMHTGGE PLRIVLAGCP EVSGPTLLAK RRYMRQHLDH
     VRRRLMFEPR GHRDMYGAVL VPSELPDAHL GVLFLHNEGY SSMCGHAVLA LGRFALDFGL
     VPATPAGTRE ARVNIHCPCG LVTAFVACED GRSHGPVRFH SVPAFVLATD LMVDVPGHGK
     VVVDIAYGGA FYAFVTAEKL GLDICSAKTR DLVDAASAVT KAVKAQFKIN HPDSEDLAFL
     YGTILTDGKD AYTKEPTTNI CVFADEQVDR SPTGSGVIAR IALQYHKGLL ELNQTRAFKS
     SATGSVFTGK AVREAKCGDF KAVIVEVSGQ AHYTGTASFI VEDDDPLRDG FLLK