ID   PROD_DICDI              Reviewed;         572 AA.
AC   Q86H28; Q553B0;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Proline dehydrogenase 1, mitochondrial;
DE            EC=1.5.5.2;
DE   AltName: Full=Proline oxidase;
DE   Flags: Precursor;
GN   Name=prodh; ORFNames=DDB_G0275669;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA   Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA   Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA   Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Converts proline to delta-1-pyrroline-5-carboxylate.
CC       {ECO:0000250}.
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; Evidence={ECO:0000250};
CC   -!- PATHWAY: Amino-acid degradation; L-proline degradation into L-
CC       glutamate; L-glutamate from L-proline: step 1/2.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the proline oxidase family. {ECO:0000305}.
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DR   EMBL; AAFI02000013; EAL69585.1; -; Genomic_DNA.
DR   RefSeq; XP_643510.1; XM_638418.1.
DR   AlphaFoldDB; Q86H28; -.
DR   SMR; Q86H28; -.
DR   STRING; 44689.DDB0167252; -.
DR   PaxDb; Q86H28; -.
DR   PRIDE; Q86H28; -.
DR   EnsemblProtists; EAL69585; EAL69585; DDB_G0275669.
DR   GeneID; 8620091; -.
DR   KEGG; ddi:DDB_G0275669; -.
DR   dictyBase; DDB_G0275669; -.
DR   eggNOG; KOG0186; Eukaryota.
DR   HOGENOM; CLU_018202_3_0_1; -.
DR   InParanoid; Q86H28; -.
DR   OMA; WMQDAAD; -.
DR   PhylomeDB; Q86H28; -.
DR   Reactome; R-DDI-389661; Glyoxylate metabolism and glycine degradation.
DR   Reactome; R-DDI-70688; Proline catabolism.
DR   UniPathway; UPA00261; UER00373.
DR   PRO; PR:Q86H28; -.
DR   Proteomes; UP000002195; Chromosome 2.
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   3: Inferred from homology;
KW   FAD; Flavoprotein; Mitochondrion; Oxidoreductase; Proline metabolism;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..572
FT                   /note="Proline dehydrogenase 1, mitochondrial"
FT                   /id="PRO_0000329318"
FT   REGION          105..140
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   572 AA;  65262 MW;  3240673498631523 CRC64;
     MIKNTVRIIN KNSNTFINIR NNNNNNINSS LKSGFGTIKR FNTTLNHNSS NSNIQTPISI
     NSTIINNNNN SNNNNSNNII NNDLNVVKFS TISTPNSILD TLNENHSNQT NNVNNKNYNN
     NNNNFEKDDK FGPPNNQNNN KLDLDTSKLY VSKSTGELFF TFMILKVCSI NFISDNSQKF
     LNLFEKLGLS KPLNFFIKYS FFKQFCAGET IRETEIFTEK LNKLGIGTIL DYAIEELAGS
     SEGFDSVAEN ICETIRVAAK NPTNSFSCVK FTGLVTPSVL EKMNTLVSNV TTNVSELPIE
     SFNSPLDFYL NQSSSLMKQG SEPLLTSKDI KEIKEFFNRM DKIFQLCHQR GVPILVDAEQ
     SYYQVAIHHL TMSYSIKYNK EKPIIYNTYQ MYLVNGMNVL KQHFELSSSQ KFNFKLGAKI
     VRGAYMVTES ERSQRLSTEN PVLPTIQDTH KSYNTALDFL LNQIKSDPNS IGLMIASHNE
     DSINLGTKLI KQYKIDPTNP NIQFGQLFGM ADFLSFNLVD QHQRIFKYVP FGPVEEVLPY
     LIRRMHENKG FIGSNSDKEL FYLKKEIKRR LF