ID   PROD_SCHPO              Reviewed;         492 AA.
AC   O74524;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Probable proline dehydrogenase, mitochondrial;
DE            EC=1.5.5.2;
DE   AltName: Full=Probable proline oxidase;
DE   Flags: Precursor;
GN   ORFNames=SPCC70.03c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
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;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- SIMILARITY: Belongs to the proline oxidase family. {ECO:0000305}.
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DR   EMBL; CU329672; CAA19353.1; -; Genomic_DNA.
DR   PIR; T41549; T41549.
DR   RefSeq; NP_588537.1; NM_001023525.2.
DR   AlphaFoldDB; O74524; -.
DR   SMR; O74524; -.
DR   BioGRID; 276015; 29.
DR   STRING; 4896.SPCC70.03c.1; -.
DR   iPTMnet; O74524; -.
DR   MaxQB; O74524; -.
DR   PaxDb; O74524; -.
DR   PRIDE; O74524; -.
DR   EnsemblFungi; SPCC70.03c.1; SPCC70.03c.1:pep; SPCC70.03c.
DR   GeneID; 2539452; -.
DR   KEGG; spo:SPCC70.03c; -.
DR   PomBase; SPCC70.03c; -.
DR   VEuPathDB; FungiDB:SPCC70.03c; -.
DR   eggNOG; KOG0186; Eukaryota.
DR   HOGENOM; CLU_018202_0_1_1; -.
DR   InParanoid; O74524; -.
DR   OMA; YEICSRA; -.
DR   PhylomeDB; O74524; -.
DR   Reactome; R-SPO-389661; Glyoxylate metabolism and glycine degradation.
DR   Reactome; R-SPO-70688; Proline catabolism.
DR   PRO; PR:O74524; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005759; C:mitochondrial matrix; ISS:PomBase.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0071949; F:FAD binding; IBA:GO_Central.
DR   GO; GO:0004657; F:proline dehydrogenase activity; ISS:PomBase.
DR   GO; GO:0010133; P:proline catabolic process to glutamate; ISO:PomBase.
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           ?..492
FT                   /note="Probable proline dehydrogenase, mitochondrial"
FT                   /id="PRO_0000025805"
SQ   SEQUENCE   492 AA;  55813 MW;  6710836E021D9D95 CRC64;
     MRAFRLASGV LRNRKVILGI GAGSLITAGN IKIRNDSKFD AFFAKGFPDE LQHRSLFSVL
     RSAFVYEICS RAWLVKLSLG AMSLCDVFHL SFLYNPFCRY TFYKHFCGGE TPQAVMATMD
     TLQAAGITSC LNYSREVDLD GDMDVNKIAS QGVVPPQVPV PSEKNQKVLR QIADKAFESN
     MHIIDMATYK PGTVCAVKLT PFINPLVLQR YNSILNQYPV ESACNYLEHL KSPELSTYEV
     SELKKFWEYA DKLCQFAKEK QIPLFIDAEQ TYFQDCMHAV TVDLMRKYNK EVAIVHNTYQ
     LYLKKSRKIM DDHIKKCVAE GWLMGAKLVR GAYLNSEPRF LIHDTKAETD KDFDSAVEAI
     IAAAAKFAPG DPASASDPIA SRKGKWGIMV ASHNKKTMFE SVNLAETKKV DFTKTSFYLA
     QLLGMADDIT YALAYSQRNQ QPNFCIVKYV SCGPISEVLP YLVRRARENI DALDRCKEER
     AYYRQALRRR IF