HYPDH_RAT
ID HYPDH_RAT Reviewed; 456 AA.
AC Q2V057;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 80.
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;
DE AltName: Full=Proline oxidase-like protein;
GN Name=Prodh2 {ECO:0000312|RGD:1306761};
GN Synonyms=Hypdh {ECO:0000250|UniProtKB:Q9UF12};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Yang Q., Tian Y., Wallner E.I., Kanwar Y.S.;
RL Submitted (JAN-2000) 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 -!- 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; AF222852; AAQ13908.1; -; mRNA.
DR AlphaFoldDB; Q2V057; -.
DR SMR; Q2V057; -.
DR STRING; 10116.ENSRNOP00000028392; -.
DR iPTMnet; Q2V057; -.
DR PhosphoSitePlus; Q2V057; -.
DR PaxDb; Q2V057; -.
DR UCSC; RGD:1306761; rat.
DR RGD; 1306761; Prodh2.
DR eggNOG; KOG0186; Eukaryota.
DR InParanoid; Q2V057; -.
DR PhylomeDB; Q2V057; -.
DR Reactome; R-RNO-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-RNO-70688; Proline catabolism.
DR PRO; PR:Q2V057; -.
DR Proteomes; UP000002494; 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..456
FT /note="Hydroxyproline dehydrogenase"
FT /id="PRO_0000308625"
FT MOD_RES 310
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VCZ9"
FT MOD_RES 320
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VCZ9"
SQ SEQUENCE 456 AA; 51002 MW; 03DA662B133B5857 CRC64;
MIWTRLPLYG HSKPSTGGWQ PLRFDGGAFH LKRTAELARA LLVLRLCAWP PLVTHGLAFQ
AWSQRLLGSR LSGALLRASI YGQFVAGETA EEVRGCVQQL QAIGLQPLLA VPTEEEPDSA
AKTSEAWYEG NLSAMLHCVD LSRAVADAHG PARNSLMQLK VTALTSPRLC KELSAWIQRP
RGSSELRPER LAEAMESGRN LQLSCLSTEQ NQHLQASLSR LHRVAQHARA QDVRLLVDAE
YTFINPALSL LVAALAMRLD SSEEEGPWVW NTYQAYLKDT HERLERDAKA AHEAGLAFGV
KLVRGAYLDK ERSVTQLHGK EDCTQPDYEA TSRSYSRCLE LMLRRVSNHG PRCHLMVASH
NEESIRQATR RMWELGIPLD GPVCFGQLLG MCDHVSLALG QAGYMVYKSI PYGCLEEVIP
YLIRRAQENR SVLQGARREQ ALLSQELWRR LLGRTA
