(data stored in ACNUC7421 zone)

SWISSPROT: Q750V4_ASHGO

ID   Q750V4_ASHGO            Unreviewed;       463 AA.
AC   Q750V4;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 87.
DE   RecName: Full=Proline dehydrogenase {ECO:0000256|RuleBase:RU364054};
DE            EC=1.5.5.2 {ECO:0000256|RuleBase:RU364054};
GN   ORFNames=AGOS_AGL165W {ECO:0000313|EMBL:AAS54326.1};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS54326.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS54326.1, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: Converts proline to delta-1-pyrroline-5-carboxylate.
CC       {ECO:0000256|RuleBase:RU364054}.
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         Evidence={ECO:0000256|RuleBase:RU364054};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|RuleBase:RU364054};
CC   -!- SIMILARITY: Belongs to the proline oxidase family.
CC       {ECO:0000256|RuleBase:RU364054}.
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DR   EMBL; AE016820; AAS54326.1; -; Genomic_DNA.
DR   RefSeq; NP_986502.1; NM_211564.1.
DR   STRING; 33169.AAS54326; -.
DR   EnsemblFungi; AAS54326; AAS54326; AGOS_AGL165W.
DR   GeneID; 4622795; -.
DR   KEGG; ago:AGOS_AGL165W; -.
DR   HOGENOM; HOG000248390; -.
DR   InParanoid; Q750V4; -.
DR   KO; K00318; -.
DR   OMA; IIKYVPW; -.
DR   Proteomes; UP000000591; Chromosome VII.
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; IBA:GO_Central.
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;
DR   PRODOM; Q750V4.
DR   SWISS-2DPAGE; Q750V4.
KW   FAD {ECO:0000256|RuleBase:RU364054};
KW   Flavoprotein {ECO:0000256|RuleBase:RU364054};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU364054};
KW   Proline metabolism {ECO:0000256|RuleBase:RU364054};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591}.
FT   DOMAIN          116..444
FT                   /note="Pro_dh"
FT                   /evidence="ECO:0000259|Pfam:PF01619"
SQ   SEQUENCE   463 AA;  51126 MW;  A5D1CAB0A436B9F8 CRC64;
     MNSRLGQVLR QAVRVQTGLR GPARSMRGYV SQTQTKQNTV AVVAGAAERF VAPAADAHLK
     TLSQRELVAL GVIGCVTTNA RLLKLVTQAF PYVPTPVAKL LISALYCGGD TMAEVRETGR
     ALARRGVGNM MLSLTVEDSE GTKNIDIDYI VEETVRSLHG VLLPHMEEQL ARAADVNSVP
     PGYLALKPSA LVSDPANTLL HFADPAWREK RDALVANFSR IVGEVYKLNQ EMLARYPGRK
     SPFFVATIDA EKYEVQCAGV YELQRLMFAK YNPVSSPIVS CIGTWQLYLR DAAADLVAQA
     ERAEREGYKL GLKLVRGAYL HSEPNRDVIH PTKEATDEHY NEVMAKVIQD LLANGEHSVF
     GHLVVASHNY QSQMLATMLL QAHGESVGKS NVVLGQLLGM ADNVTYDLIH NHGARNIIKY
     VPWGPPKETK DYMHRRLQEN GDAVRADNGW PLVKAVCRAL FYR
//

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