ID   PUT1_YEAST              Reviewed;         476 AA.
AC   P09368;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   16-JUN-2009, entry version 79.
DE   RecName: Full=Proline dehydrogenase, mitochondrial;
DE            EC=1.5.99.8;
DE   AltName: Full=Proline oxidase;
DE   Flags: Precursor;
GN   Name=PUT1; OrderedLocusNames=YLR142W; ORFNames=L3170, L9606.2;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=88142835; PubMed=3125423;
RA   Wang S.-S., Brandriss M.C.;
RT   "Proline utilization in Saccharomyces cerevisiae: sequence,
RT   regulation, and mitochondrial localization of the PUT1 gene product.";
RL   Mol. Cell. Biol. 7:4431-4440(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204511 / S288c / AB972;
RX   MEDLINE=97313267; PubMed=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B.,
RA   Ansorge W., Benes V., Brueckner M., Delius H., Dubois E.,
RA   Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U.,
RA   Heumann K., Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K.,
RA   Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T.,
RA   Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E.,
RA   Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M.,
RA   Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C.,
RA   Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M.,
RA   Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H.,
RA   Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A.,
RA   Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
RA   Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
RA   Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
RA   Kolodner R.D., LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-
RT   encoding clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [4]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
CC   -!- FUNCTION: Converts proline to delta-1-pyrroline-5-carboxylate.
CC   -!- CATALYTIC ACTIVITY: L-proline + acceptor = (S)-1-pyrroline-5-
CC       carboxylate + reduced acceptor.
CC   -!- COFACTOR: FAD.
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.
CC   -!- MISCELLANEOUS: The expression of proline oxidase is controlled by
CC       proline and oxygen.
CC   -!- MISCELLANEOUS: Proline oxidase requires a functional electron
CC       transport chain aerobiosis for its activity.
CC   -!- MISCELLANEOUS: Present with 184 molecules/cell in log phase SD
CC       medium.
CC   -!- SIMILARITY: Belongs to the proline oxidase family.
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DR   EMBL; M18107; AAA16631.1; -; Unassigned_DNA.
DR   EMBL; X91258; CAA62662.1; -; Genomic_DNA.
DR   EMBL; Z73314; CAA97714.1; -; Genomic_DNA.
DR   EMBL; U53881; AAB82390.1; -; Genomic_DNA.
DR   EMBL; AY692906; AAT92925.1; -; Genomic_DNA.
DR   PIR; S59339; S59339.
DR   RefSeq; NP_013243.1; -.
DR   Ensembl; YLR142W; Saccharomyces cerevisiae.
DR   GeneID; 850833; -.
DR   GenomeReviews; Y13138_GR; YLR142W.
DR   KEGG; sce:YLR142W; -.
DR   NMPDR; fig|4932.3.peg.4236; -.
DR   CYGD; YLR142w; -.
DR   SGD; S000004132; PUT1.
DR   HOGENOM; P09368; -.
DR   OMA; P09368; KYVPWGP.
DR   BioCyc; MetaCyc:MON-645; -.
DR   BRENDA; 1.5.99.8; 250.
DR   NextBio; 967103; -.
DR   GermOnline; YLR142W; Saccharomyces cerevisiae.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0004657; F:proline dehydrogenase activity; IMP:SGD.
DR   GO; GO:0006537; P:glutamate biosynthetic process; TAS:SGD.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0010133; P:proline catabolic process to glutamate; IMP:SGD.
DR   InterPro; IPR002872; Proline_DH.
DR   InterPro; IPR015659; Proline_oxidase.
DR   PANTHER; PTHR13914; Proline_oxidase; 1.
DR   Pfam; PF01619; Pro_dh; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; FAD; Flavoprotein; Mitochondrion; Oxidoreductase;
KW   Proline metabolism; Transit peptide.
FT   TRANSIT       1      ?       Mitochondrion (Potential).
FT   CHAIN         ?    476       Proline dehydrogenase, mitochondrial.
FT                                /FTId=PRO_0000025806.
FT   CONFLICT     50     50       A -> P (in Ref. 1; AAA16631).
FT   CONFLICT    185    185       N -> T (in Ref. 1; AAA16631).
SQ   SEQUENCE   476 AA;  53271 MW;  12FEE55F86E1707D CRC64;
     MIASKSSLLV TKSRIPSLCF PLIKRSYVSK TPTHSNTAAN LMVETPAANA NGNSVMAPPN
     SINFLQTLPK KELFQLGFIG IATLNSFFLN TIIKLFPYIP IPVIKFFVSS LYCGGENFKE
     VIECGKRLQK RGISNMMLSL TIENSEGTKS LSSTPVDQIV KETISSVHNI LLPNIIGQLE
     SKPINDIAPG YIALKPSALV DNPHEVLYNF SNPAYKAQRD QLIENCSKIT KEIFELNQSL
     LKKYPERKAP FMVSTIDAEK YDLQENGVYE LQRILFQKFN PTSSKLISCV GTWQLYLRDS
     GDHILHELKL AQENGYKLGL KLVRGAYIHS EKNRNQIIFG DKTGTDENYD RIITQVVNDL
     IINGEDSYFG HLVVASHNYQ SQMLVTNLLK STQDNSYAKS NIVLGQLLGM ADNVTYDLIT
     NHGAKNIIKY VPWGPPLETK DYLLRRLQEN GDAVRSDNGW PLIKAIAKSI PKRVGL
//