(data stored in SCRATCH zone)

SWISSPROT: Q6BN30_DEBHA

ID   Q6BN30_DEBHA            Unreviewed;       439 AA.
AC   Q6BN30;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   08-MAY-2019, entry version 81.
DE   SubName: Full=DEHA2F00682p {ECO:0000313|EMBL:CAG88694.1};
GN   OrderedLocusNames=DEHA2F00682g {ECO:0000313|EMBL:CAG88694.1};
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC
OS   0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG88694.1, ECO:0000313|Proteomes:UP000000599};
RN   [1] {ECO:0000313|EMBL:CAG88694.1, ECO:0000313|Proteomes:UP000000599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968
RC   {ECO:0000313|Proteomes:UP000000599};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.F., Straub M.L., Suleau A.,
RA   Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; CR382138; CAG88694.1; -; Genomic_DNA.
DR   RefSeq; XP_460390.1; XM_460390.1.
DR   STRING; 4959.XP_460390.1; -.
DR   EnsemblFungi; CAG88694; CAG88694; DEHA2F00682g.
DR   GeneID; 2903875; -.
DR   KEGG; dha:DEHA2F00682g; -.
DR   HOGENOM; HOG000020206; -.
DR   InParanoid; Q6BN30; -.
DR   OMA; YTTHVND; -.
DR   OrthoDB; 145181at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6BN30.
DR   SWISS-2DPAGE; Q6BN30.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000599};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000599}.
SQ   SEQUENCE   439 AA;  47574 MW;  6285C3D23BB972DF CRC64;
     MSLYSSIDEK EFWLKSKSLL PYGGVFTPAI ITKAKGVYIY THDGKRILDF TSGQMSCLLG
     HGHPEISKTI TEHAFNLDHL FSGMICPPVV NLAHMLTGIL PDGLDKAMFL STGGEANEAA
     IKLAKICTGN FEVVGLSLSW HGMTGASNAT TYQSGRSGQG PMIPGNLVLP APNGYRSIFR
     KPDGSYDWET ELDYGWSLID SASVGSLAAV IVEPILSSGG MLVLPDGYLR AMKKHCEKRG
     MLLIVDEAQT ALGRCGSMFA FGDSGVIPDI LSLSKTLGNG IPLSAIVTSE QLSERGNKKG
     FLFYTTHVND PLPAAVGLKV LEVIIRDNLV DKARIMGNIF KSELDKFKQE YNFIGDIRGK
     GLMVGIEIVK NRQTKESDPD LAKVLADKMM ELGLSANLIA VASFGGIFRI APPITITEEE
     LRHGLSIMND AFRAIRNQL
//

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