(data stored in SCRATCH zone)

SWISSPROT: Q6BM39_DEBHA

ID   Q6BM39_DEBHA            Unreviewed;       420 AA.
AC   Q6BM39;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   08-MAY-2019, entry version 82.
DE   SubName: Full=DEHA2F08514p {ECO:0000313|EMBL:CAG89072.1};
GN   OrderedLocusNames=DEHA2F08514g {ECO:0000313|EMBL:CAG89072.1};
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:CAG89072.1, ECO:0000313|Proteomes:UP000000599};
RN   [1] {ECO:0000313|EMBL:CAG89072.1, 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 alpha-IPM synthase/homocitrate synthase
CC       family. {ECO:0000256|RuleBase:RU003523}.
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DR   EMBL; CR382138; CAG89072.1; -; Genomic_DNA.
DR   RefSeq; XP_460732.1; XM_460732.1.
DR   STRING; 4959.XP_460732.1; -.
DR   EnsemblFungi; CAG89072; CAG89072; DEHA2F08514g.
DR   GeneID; 2903354; -.
DR   KEGG; dha:DEHA2F08514g; -.
DR   HOGENOM; HOG000046858; -.
DR   InParanoid; Q6BM39; -.
DR   KO; K01655; -.
DR   OMA; SNMFAHE; -.
DR   OrthoDB; 928619at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0004410; F:homocitrate synthase activity; IEA:InterPro.
DR   GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IEA:InterPro.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR011872; Homocitrate_synth_fun/arc.
DR   InterPro; IPR000891; PYR_CT.
DR   Pfam; PF00682; HMGL-like; 1.
DR   TIGRFAMs; TIGR02146; LysS_fung_arch; 1.
DR   PROSITE; PS00815; AIPM_HOMOCIT_SYNTH_1; 1.
DR   PROSITE; PS00816; AIPM_HOMOCIT_SYNTH_2; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6BM39.
DR   SWISS-2DPAGE; Q6BM39.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000599};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000599};
KW   Transferase {ECO:0000256|RuleBase:RU003523}.
FT   DOMAIN       22    281       Pyruvate carboxyltransferase.
FT                                {ECO:0000259|PROSITE:PS50991}.
SQ   SEQUENCE   420 AA;  46392 MW;  E95D4B2B94A2C28B CRC64;
     MSIQSNPYGP NPSDFLSNVN KFEVIESTLR EGEQFANAFF STEKKIEIAK ALDDFGVDYI
     ELTSPVASEQ SRSDCEAICK LGLKAKILTH IRCHMDDARV AVETGVDGVD VVIGTSQFLR
     QYSHGKDMNY IAQSAIEVIE FVKSKGIEIR FSSEDSFRSD IVDLLNIYRT VDKIGVNRVG
     IADTVGCANP RQVYELVKTL KSVVSCDIEC HFHNDTGCAI ANAYTALEAG AKLIDVSVLG
     IGERNGITPL GALMARMITA DRDYVLSKYK LHKLRDLENL VADAVQVNVP FNNPITGFCA
     FTHKAGIHAK AILANPSTYE ILNPSDFGLT RYIHFANRLT GWNAIKSRVD QLNLHLTDDQ
     CKEVTTKIKI MGDVRQLNID DVDSIIKDFH ADLSTPLLKP QAEGDKDVTE EPVSKKQKSG
//

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