ID   T3HPD_BOVIN             Reviewed;         354 AA.
AC   Q3SX04;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 90.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2005) 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; BC104573; AAI04574.1; -; mRNA.
DR   RefSeq; NP_001029558.1; NM_001034386.1.
DR   AlphaFoldDB; Q3SX04; -.
DR   SMR; Q3SX04; -.
DR   STRING; 9913.ENSBTAP00000004371; -.
DR   PaxDb; Q3SX04; -.
DR   PRIDE; Q3SX04; -.
DR   Ensembl; ENSBTAT00000004371; ENSBTAP00000004371; ENSBTAG00000030824.
DR   GeneID; 510525; -.
DR   KEGG; bta:510525; -.
DR   CTD; 112849; -.
DR   VEuPathDB; HostDB:ENSBTAG00000030824; -.
DR   VGNC; VGNC:30762; L3HYPDH.
DR   eggNOG; ENOG502QRPF; Eukaryota.
DR   GeneTree; ENSGT00390000002032; -.
DR   HOGENOM; CLU_036729_0_1_1; -.
DR   InParanoid; Q3SX04; -.
DR   OMA; SHVLWTG; -.
DR   OrthoDB; 894373at2759; -.
DR   TreeFam; TF329167; -.
DR   Proteomes; UP000009136; Chromosome 10.
DR   Bgee; ENSBTAG00000030824; Expressed in biceps femoris and 103 other tissues.
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_0000288948"
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;  37957 MW;  997C31A237A82510 CRC64;
     MAGPLTVPWM PPHDPGTPAL SVVDMHTGGE PLRIVLAGCP EVVGPTLLAK RRYMRQHLDH
     VRRRLMFEPR GHRDMYGAVL VPSELPDAHL GVLFLNNEGY SSMCGHAVLA LGRFALDFGL
     VPAPPSDAQE ALVNIHCPCG LVAAFVECEG CRSRGPVRFH SVPAFVLATD FLVDVPGRGK
     VVVDIAYGGA FYAFVSAEKL GLDVCSAKMG DLVAAASAVT EAVKAQFKIS HPDSEDLAFL
     YGTILTDGKD TYNEEPTTNI CVFADEQVDR SPTGSGVTAR IALQYHKGLL ELNQTRAFKS
     SATGSVFTGK AVREAKCGDF KAVIVEVSGQ AHYTGTASFI VEDDDPLRDG FLLK