ID   HYPDH_BOVIN             Reviewed;         461 AA.
AC   A6QQ74;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 73.
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 {ECO:0000250|UniProtKB:Q9UF12};
GN   Synonyms=HYPDH {ECO:0000250|UniProtKB:Q9UF12};
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=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUL-2007) 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 ubiquinone-10 as
CC       the 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. Ubiquininone analogs such as menadione, duroquinone and
CC       ubiquinone-1 react more efficiently than oxygen as the terminal
CC       electron acceptor during catalysis. {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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC149682; AAI49683.1; -; mRNA.
DR   RefSeq; NP_001098437.1; NM_001104967.2.
DR   AlphaFoldDB; A6QQ74; -.
DR   SMR; A6QQ74; -.
DR   STRING; 9913.ENSBTAP00000042469; -.
DR   PaxDb; A6QQ74; -.
DR   PRIDE; A6QQ74; -.
DR   GeneID; 508542; -.
DR   KEGG; bta:508542; -.
DR   CTD; 58510; -.
DR   eggNOG; KOG0186; Eukaryota.
DR   InParanoid; A6QQ74; -.
DR   OrthoDB; 948528at2759; -.
DR   UniPathway; UPA00261; UER00373.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0071949; F:FAD binding; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0010133; P:proline catabolic process to glutamate; IBA:GO_Central.
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   Acetylation; FAD; Flavoprotein; Oxidoreductase; Proline metabolism;
KW   Reference proteome.
FT   CHAIN           1..461
FT                   /note="Hydroxyproline dehydrogenase"
FT                   /id="PRO_0000308622"
FT   MOD_RES         310
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VCZ9"
SQ   SEQUENCE   461 AA;  51262 MW;  DF3E394E3AF6356E CRC64;
     MLQACRVLRS RAGPSPGSWQ PLSFDGGAFH LKSIGELTRA LLVLRLCAWP PLVTHGLALQ
     AWSQRLLGSR LSGALLRASI YGQFVAGETA EEVRSCVLQL QNLGLRPLLA VPTEEEPDSA
     VKTGEAWYEG NLSAMLRCVD LSRGLLETPD PTGNALMQLK MTALMSTRLC KQLTSWVRRP
     GDSLELSPER LAEAMDSGQD LQVSCLNTEQ TRHLQASLSR LHRVVQHARA QRVRLLVDAE
     YTSLNPALSL LVAALATRWN SSGEGGPWVW NTYQAYLKDT YERLRWDAEA ADRAGLAFGV
     KLVRGAYLDK ERETARLQGT EDPTQPDYEA TSQSYSRCLE LMLTQVSHRG PMCHLMVASH
     NEDSVRQATK RMWELGIPPD GPVCFGQLLG MCDHVSLALG QAGYAVYKSI PYGSLEEVIP
     YLIRRAQENR SVLRGARREQ ELLSQELRRR LLGRGLRVSP H