ID   HYPDH_XENLA             Reviewed;         466 AA.
AC   Q6PAY6;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Hydroxyproline dehydrogenase {ECO:0000250|UniProtKB:Q9UF12};
DE            Short=HYPDH {ECO:0000250|UniProtKB:Q9UF12};
DE            EC=1.5.5.3 {ECO:0000250|UniProtKB:Q9UF12};
DE   AltName: Full=Probable proline dehydrogenase 2 {ECO:0000250|UniProtKB:Q9UF12};
DE            EC=1.5.5.2 {ECO:0000250|UniProtKB:Q9UF12};
DE   AltName: Full=Probable proline oxidase 2;
GN   Name=prodh2; Synonyms=hypdh {ECO:0000250|UniProtKB:Q9UF12};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Dehydrogenase that converts trans-4-L-hydroxyproline to
CC       delta-1-pyrroline-3-hydroxy-5-carboxylate (Hyp) using a quinone as the
CC       terminal electron acceptor. Can also use proline as a substrate but
CC       with a very much lower efficiency. Does not react with other
CC       diastereomers of Hyp: trans-4-D-hydroxyproline and cis-4-L-
CC       hydroxyproline. {ECO:0000250|UniProtKB:Q9UF12}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + trans-4-hydroxy-L-proline = (3R,5S)-1-pyrroline-3-
CC         hydroxy-5-carboxylate + a quinol + H(+); Xref=Rhea:RHEA:52512,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:58375,
CC         ChEBI:CHEBI:62612, ChEBI:CHEBI:132124; EC=1.5.5.3;
CC         Evidence={ECO:0000250|UniProtKB:Q9UF12};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + L-proline = (S)-1-pyrroline-5-carboxylate + a
CC         quinol + H(+); Xref=Rhea:RHEA:23784, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17388, ChEBI:CHEBI:24646, ChEBI:CHEBI:60039,
CC         ChEBI:CHEBI:132124; EC=1.5.5.2;
CC         Evidence={ECO:0000250|UniProtKB:Q9UF12};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:Q9UF12};
CC   -!- PATHWAY: Amino-acid degradation; L-proline degradation into L-
CC       glutamate; L-glutamate from L-proline: step 1/2.
CC   -!- SIMILARITY: Belongs to the proline oxidase family. {ECO:0000305}.
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DR   EMBL; BC059998; AAH59998.1; -; mRNA.
DR   RefSeq; NP_001083128.1; NM_001089659.1.
DR   AlphaFoldDB; Q6PAY6; -.
DR   SMR; Q6PAY6; -.
DR   PRIDE; Q6PAY6; -.
DR   DNASU; 398760; -.
DR   GeneID; 398760; -.
DR   KEGG; xla:398760; -.
DR   CTD; 398760; -.
DR   Xenbase; XB-GENE-5784821; prodh2.L.
DR   OrthoDB; 948528at2759; -.
DR   UniPathway; UPA00261; UER00373.
DR   Proteomes; UP000186698; Chromosome 9_10L.
DR   Bgee; 398760; Expressed in pancreas and 7 other tissues.
DR   GO; GO:0016645; F:oxidoreductase activity, acting on the CH-NH group of donors; ISS:UniProtKB.
DR   GO; GO:0004657; F:proline dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0010133; P:proline catabolic process to glutamate; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR029041; FAD-linked_oxidoreductase-like.
DR   InterPro; IPR002872; Proline_DH_dom.
DR   InterPro; IPR015659; Proline_oxidase.
DR   PANTHER; PTHR13914; PTHR13914; 1.
DR   Pfam; PF01619; Pro_dh; 1.
DR   SUPFAM; SSF51730; SSF51730; 1.
PE   2: Evidence at transcript level;
KW   FAD; Flavoprotein; Oxidoreductase; Proline metabolism; Reference proteome.
FT   CHAIN           1..466
FT                   /note="Hydroxyproline dehydrogenase"
FT                   /id="PRO_0000308626"
SQ   SEQUENCE   466 AA;  52329 MW;  873A4E7B7B336E99 CRC64;
     MRLLGRYLRL GSPRLCSRVW PTLPPSCSPH STAAAAQAQG ALSFSDGGVF KLKSSWEVAR
     GLLIFRMCSF PSLVKHSEKM LSVSRRLLGR RLFEWGMKGS VYGQFVAGET LPEIRVCVDR
     LRQLGIHPML AVPIEEDLGQ AKSGERWYEQ NESIMLDCVD LSAAGGDRPM MQLKITALMS
     AELCKLLSVH LSHPSNGPQL CPRSIVSIME GKESAFSFLS EGENSHLRNS VRRLSRIAKH
     ATANRVRVLV DAEYTYMNPA LSLVTMAMMS QCNQSEPWIW NTYQCYLKDS FSLLSLDLDT
     ARSLGLCFGV KLVRGAYMDK ERKLSKQKGY ADPIQHDWEA TNRSYQRSLD KMLDLIGQNG
     QRHNLIVASH NEESVLHAVT RMAELGIDKG SGSVSFGQLL GMCDHVSLTL GQAGYLVYKS
     LPYGSVDSVL PYLIRRAQEN QSVLQGIRKE RDLLRRELKR RLFNQR