(data stored in SCRATCH zone)

SWISSPROT: C5DD59_LACTC

ID   C5DD59_LACTC            Unreviewed;       437 AA.
AC   C5DD59;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   08-MAY-2019, entry version 63.
DE   SubName: Full=KLTH0B08514p {ECO:0000313|EMBL:CAR21720.1};
GN   OrderedLocusNames=KLTH0B08514g {ECO:0000313|EMBL:CAR21720.1};
OS   Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS   (Yeast) (Kluyveromyces thermotolerans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=559295 {ECO:0000313|EMBL:CAR21720.1, ECO:0000313|Proteomes:UP000002036};
RN   [1] {ECO:0000313|EMBL:CAR21720.1, ECO:0000313|Proteomes:UP000002036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284
RC   {ECO:0000313|Proteomes:UP000002036};
RX   PubMed=19525356; DOI=10.1101/gr.091546.109;
RG   The Genolevures Consortium;
RA   Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA   Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P.,
RA   Jubin C., Poulain J., Barbe V., Segurens B., Artiguenave F.,
RA   Anthouard V., Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R.,
RA   Durrens P., Jean G., Marck C., Martin T., Nikolski M., Rolland T.,
RA   Seret M.-L., Casaregola S., Despons L., Fairhead C., Fischer G.,
RA   Lafontaine I., Leh V., Lemaire M., de Montigny J., Neuveglise C.,
RA   Thierry A., Blanc-Lenfle I., Bleykasten C., Diffels J., Fritsch E.,
RA   Frangeul L., Goeffon A., Jauniaux N., Kachouri-Lafond R., Payen C.,
RA   Potier S., Pribylova L., Ozanne C., Richard G.-F., Sacerdot C.,
RA   Straub M.-L., Talla E.;
RT   "Comparative genomics of protoploid Saccharomycetaceae.";
RL   Genome Res. 19:1696-1709(2009).
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DR   EMBL; CU928166; CAR21720.1; -; Genomic_DNA.
DR   RefSeq; XP_002552158.1; XM_002552112.1.
DR   SMR; C5DD59; -.
DR   STRING; 381046.XP_002552158.1; -.
DR   EnsemblFungi; CAR21720; CAR21720; KLTH0B08514g.
DR   GeneID; 8290998; -.
DR   KEGG; lth:KLTH0B08514g; -.
DR   HOGENOM; HOG000072174; -.
DR   InParanoid; C5DD59; -.
DR   KO; K01689; -.
DR   OMA; EFMIIPV; -.
DR   OrthoDB; 773373at2759; -.
DR   Proteomes; UP000002036; Chromosome B.
DR   GO; GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004634; F:phosphopyruvate hydratase activity; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:InterPro.
DR   CDD; cd03313; enolase; 1.
DR   Gene3D; 3.20.20.120; -; 1.
DR   Gene3D; 3.30.390.10; -; 1.
DR   HAMAP; MF_00318; Enolase; 1.
DR   InterPro; IPR000941; Enolase.
DR   InterPro; IPR036849; Enolase-like_C_sf.
DR   InterPro; IPR029017; Enolase-like_N.
DR   InterPro; IPR020810; Enolase_C.
DR   InterPro; IPR020809; Enolase_CS.
DR   InterPro; IPR020811; Enolase_N.
DR   PANTHER; PTHR11902; PTHR11902; 1.
DR   Pfam; PF00113; Enolase_C; 1.
DR   Pfam; PF03952; Enolase_N; 1.
DR   PIRSF; PIRSF001400; Enolase; 1.
DR   PRINTS; PR00148; ENOLASE.
DR   SMART; SM01192; Enolase_C; 1.
DR   SMART; SM01193; Enolase_N; 1.
DR   SUPFAM; SSF51604; SSF51604; 1.
DR   TIGRFAMs; TIGR01060; eno; 1.
DR   PROSITE; PS00164; ENOLASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5DD59.
DR   SWISS-2DPAGE; C5DD59.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002036};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002036}.
FT   DOMAIN        3    134       Enolase_N. {ECO:0000259|SMART:SM01193}.
FT   DOMAIN      144    434       Enolase_C. {ECO:0000259|SMART:SM01192}.
FT   REGION      373    376       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR001400-2}.
FT   ACT_SITE    212    212       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR001400-1}.
FT   ACT_SITE    346    346       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR001400-1}.
FT   BINDING     160    160       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001400-2}.
FT   BINDING     169    169       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001400-2}.
FT   BINDING     296    296       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001400-2}.
FT   BINDING     321    321       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001400-2}.
FT   BINDING     397    397       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001400-2}.
SQ   SEQUENCE   437 AA;  46707 MW;  60FBD8F3A7802ACB CRC64;
     MAISKVHARQ VYDSRGNPTV EVELTTEKGT FRSIVPSGAS TGAYEAIELR DGDKSKWLGK
     GVLKAVDNVN SVIAPALVKA NVDVKNQKAV DELLLSLDGT PNKSKLGANA VLGVSMAAAK
     AAAAEKNVPL YKHLADLSNS KQDSYVLPVP FLNVLNGGSH AGGALALQEF MIAPTGAESF
     SEAMRMGSEV YHNLKSLTKK RYGPSAGNVG DEGGVAPNIQ TAEEALDLIV DAIKAAGYEG
     KISIGLDSAS SEFYKDGLYD LDFKNPDSDK SKWLTGKQMA EMYASLVSKY PIVSIEDPFA
     EDDWEAWSHY YKTAGIQIVA DDLTVTNPLR IKTAIEKKAA DALLLKVNQI GSLSESIEAA
     QDSFAAGWGV MVSHRSGETE DTFIADLVVG LRTGQIKTGA PARSERLAKL NQLLRIEEEL
     GSKAVFAGKK FHNGQNL
//

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