ID   PROD_BOVIN              Reviewed;         593 AA.
AC   Q148G5;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Proline dehydrogenase 1, mitochondrial {ECO:0000250|UniProtKB:O43272};
DE            EC=1.5.5.2;
DE   AltName: Full=Proline oxidase {ECO:0000250|UniProtKB:O43272};
DE   Flags: Precursor;
GN   Name=PRODH {ECO:0000312|EMBL:AAI18354.1};
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] {ECO:0000312|EMBL:AAI18354.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford {ECO:0000312|EMBL:AAI18354.1};
RC   TISSUE=Fetal cerebellum {ECO:0000312|EMBL:AAI18354.1};
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Converts proline to delta-1-pyrroline-5-carboxylate.
CC       {ECO:0000250|UniProtKB:O43272}.
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   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:O43272};
CC   -!- PATHWAY: Amino-acid degradation; L-proline degradation into L-
CC       glutamate; L-glutamate from L-proline: step 1/2.
CC       {ECO:0000250|UniProtKB:O43272}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000250|UniProtKB:O43272}.
CC   -!- SIMILARITY: Belongs to the proline oxidase family. {ECO:0000255}.
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DR   EMBL; BC118353; AAI18354.1; -; mRNA.
DR   RefSeq; NP_001068653.1; NM_001075185.1.
DR   AlphaFoldDB; Q148G5; -.
DR   STRING; 9913.ENSBTAP00000056646; -.
DR   PaxDb; Q148G5; -.
DR   GeneID; 505094; -.
DR   KEGG; bta:505094; -.
DR   CTD; 5625; -.
DR   eggNOG; KOG0186; Eukaryota.
DR   InParanoid; Q148G5; -.
DR   UniPathway; UPA00261; UER00373.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0071949; F:FAD binding; ISS:UniProtKB.
DR   GO; GO:0004657; F:proline dehydrogenase activity; ISS:UniProtKB.
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; Mitochondrion; Oxidoreductase;
KW   Proline metabolism; Reference proteome; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000305"
FT   CHAIN           ?..593
FT                   /note="Proline dehydrogenase 1, mitochondrial"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000406783"
FT   REGION          24..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         368
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WU79"
FT   MOD_RES         479
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WU79"
SQ   SEQUENCE   593 AA;  67080 MW;  64EF00C48BDD484A CRC64;
     MGLRRTSWMH FSALCRRAPL STAPAAREQP AAGPGAEPVC GPAETARPPV PAVDFGNTQE
     AYRSRRSWEL ARSLLVLSLC ASPALLARHE QLLHLARKLL GQRLFNTLMK MTFYGQFVAG
     EDQESIRPLI QHNRAFGVGS ILDYGVEEDL TPEEAERTEM ESCSSALERD GCGVSKREKQ
     FQAHRAFGDR RDGVTSARTY FYASEAKCDS HMETFLHCIE ASGGASEDGF SAIKLTALGR
     PQFLLQFSDM LTKWRRFFHH VAAEQGKAGL AAVDTKLEVA ALQESVVKMG IASRAEIEDW
     FTAETLGVSG TLDLLDWCSL IDSRTELSRH LVVPNMQTGR LEPLLSQFTE EEERQMTRML
     QRMDVLAKKA NQVGVRLMVD AEQTYFQPAI SRLTLEMQRR FNVERPLIFN TFQCYLRDAY
     DNVILDVELA RREGWCFGAK LVRGAYMAQV GYEDPINPTY EATSAVYHRC LDYVLEELKH
     NARAAVMVAS HNEDTVRFTL RRMEELGLHP ADRQVYFGQL LGMCDHISFP LGQAGFPVYK
     YVPYGPVMEV LPYLSRRALE NSGVMKGAQR ERQLLWQELK RRLCTRSLFH QPA