PUT1_YEAST
ID PUT1_YEAST Reviewed; 476 AA.
AC P09368; D6VYD6;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Proline dehydrogenase, mitochondrial;
DE EC=1.5.5.2;
DE AltName: Full=Proline oxidase;
DE Flags: Precursor;
GN Name=PUT1; OrderedLocusNames=YLR142W; ORFNames=L3170, L9606.2;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=3125423; DOI=10.1128/mcb.7.12.4431-4440.1987;
RA Wang S.-S., Brandriss M.C.;
RT "Proline utilization in Saccharomyces cerevisiae: sequence, regulation, and
RT 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 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
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., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA 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:
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 -!- 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 transport
CC chain aerobiosis for its activity.
CC -!- MISCELLANEOUS: Present with 184 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the proline oxidase family. {ECO:0000305}.
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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 EMBL; BK006945; DAA09452.1; -; Genomic_DNA.
DR PIR; S59339; S59339.
DR RefSeq; NP_013243.1; NM_001182029.1.
DR AlphaFoldDB; P09368; -.
DR BioGRID; 31410; 100.
DR IntAct; P09368; 6.
DR MINT; P09368; -.
DR STRING; 4932.YLR142W; -.
DR iPTMnet; P09368; -.
DR MaxQB; P09368; -.
DR PaxDb; P09368; -.
DR PRIDE; P09368; -.
DR EnsemblFungi; YLR142W_mRNA; YLR142W; YLR142W.
DR GeneID; 850833; -.
DR KEGG; sce:YLR142W; -.
DR SGD; S000004132; PUT1.
DR VEuPathDB; FungiDB:YLR142W; -.
DR eggNOG; KOG0186; Eukaryota.
DR GeneTree; ENSGT00390000006265; -.
DR HOGENOM; CLU_029274_0_0_1; -.
DR InParanoid; P09368; -.
DR OMA; HLIWAEK; -.
DR BioCyc; MetaCyc:YLR142W-MON; -.
DR BioCyc; YEAST:YLR142W-MON; -.
DR Reactome; R-SCE-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-SCE-70688; Proline catabolism.
DR UniPathway; UPA00261; UER00373.
DR PRO; PR:P09368; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P09368; protein.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0071949; F:FAD binding; IBA:GO_Central.
DR GO; GO:0004657; F:proline dehydrogenase activity; IDA:SGD.
DR GO; GO:0006537; P:glutamate biosynthetic process; IC:SGD.
DR GO; GO:0010133; P:proline catabolic process to glutamate; IDA:SGD.
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 1: Evidence at protein level;
KW FAD; Flavoprotein; Mitochondrion; Oxidoreductase; Proline metabolism;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..476
FT /note="Proline dehydrogenase, mitochondrial"
FT /id="PRO_0000025806"
FT CONFLICT 50
FT /note="A -> P (in Ref. 1; AAA16631)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="N -> T (in Ref. 1; AAA16631)"
FT /evidence="ECO:0000305"
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
