(data stored in SCRATCH zone)

SWISSPROT: C5DCC7_LACTC

ID   C5DCC7_LACTC            Unreviewed;       332 AA.
AC   C5DCC7;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   16-JAN-2019, entry version 69.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361160};
DE            EC=1.2.1.12 {ECO:0000256|RuleBase:RU361160};
GN   OrderedLocusNames=KLTH0B01958g {ECO:0000313|EMBL:CAR21438.1};
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:CAR21438.1, ECO:0000313|Proteomes:UP000002036};
RN   [1] {ECO:0000313|EMBL:CAR21438.1, 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).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = 3-
CC         phospho-D-glyceroyl phosphate + H(+) + NADH;
CC         Xref=Rhea:RHEA:10300, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57604, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:59776; EC=1.2.1.12;
CC         Evidence={ECO:0000256|RuleBase:RU361160};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 1/5.
CC       {ECO:0000256|RuleBase:RU361160}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|RuleBase:RU361160}.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU000397}.
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DR   EMBL; CU928166; CAR21438.1; -; Genomic_DNA.
DR   RefSeq; XP_002551876.1; XM_002551830.1.
DR   STRING; 381046.XP_002551876.1; -.
DR   EnsemblFungi; CAR21438; CAR21438; KLTH0B01958g.
DR   GeneID; 8290704; -.
DR   KEGG; lth:KLTH0B01958g; -.
DR   HOGENOM; HOG000071678; -.
DR   InParanoid; C5DCC7; -.
DR   KO; K00134; -.
DR   OMA; KYDPSSM; -.
DR   OrthoDB; 945145at2759; -.
DR   UniPathway; UPA00109; UER00184.
DR   Proteomes; UP000002036; Chromosome B.
DR   GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR020831; GlycerAld/Erythrose_P_DH.
DR   InterPro; IPR020830; GlycerAld_3-P_DH_AS.
DR   InterPro; IPR020829; GlycerAld_3-P_DH_cat.
DR   InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd.
DR   InterPro; IPR006424; Glyceraldehyde-3-P_DH_1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR10836; PTHR10836; 1.
DR   Pfam; PF02800; Gp_dh_C; 1.
DR   Pfam; PF00044; Gp_dh_N; 1.
DR   PIRSF; PIRSF000149; GAP_DH; 1.
DR   PRINTS; PR00078; G3PDHDRGNASE.
DR   SMART; SM00846; Gp_dh_N; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR01534; GAPDH-I; 1.
DR   PROSITE; PS00071; GAPDH; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5DCC7.
DR   SWISS-2DPAGE; C5DCC7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002036};
KW   Glycolysis {ECO:0000256|RuleBase:RU361160};
KW   NAD {ECO:0000256|PIRSR:PIRSR000149-3, ECO:0000256|RuleBase:RU361160};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000149-3};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU361160};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002036}.
FT   DOMAIN        3    150       Gp_dh_N. {ECO:0000259|SMART:SM00846}.
FT   NP_BIND      12     13       NAD. {ECO:0000256|PIRSR:PIRSR000149-3}.
FT   REGION      149    151       Glyceraldehyde 3-phosphate binding.
FT                                {ECO:0000256|PIRSR:PIRSR000149-2}.
FT   REGION      209    210       Glyceraldehyde 3-phosphate binding.
FT                                {ECO:0000256|PIRSR:PIRSR000149-2}.
FT   ACT_SITE    150    150       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR000149-1}.
FT   BINDING      34     34       NAD. {ECO:0000256|PIRSR:PIRSR000149-3}.
FT   BINDING      79     79       NAD; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR000149-3}.
FT   BINDING     121    121       NAD. {ECO:0000256|PIRSR:PIRSR000149-3}.
FT   BINDING     180    180       Glyceraldehyde 3-phosphate.
FT                                {ECO:0000256|PIRSR:PIRSR000149-2}.
FT   BINDING     232    232       Glyceraldehyde 3-phosphate.
FT                                {ECO:0000256|PIRSR:PIRSR000149-2}.
FT   BINDING     314    314       NAD. {ECO:0000256|PIRSR:PIRSR000149-3}.
FT   SITE        177    177       Activates thiol group during catalysis.
FT                                {ECO:0000256|PIRSR:PIRSR000149-4}.
SQ   SEQUENCE   332 AA;  35670 MW;  C3692D03AE3C4AAE CRC64;
     MVTTVAINGF GRIGRLVLRI ALSRKDLKVV AINDPFISVD YAAYMFKYDS THGRYQGTVS
     HEGSDLVIDG QKIAVFQERD PAQLPWGKLN VDIAIDSTGV FKELDSAQKH IDAGAKKVVI
     TAPSSTAPMF VVGVNEDEYK GQNIVSNASC TTNCLAPLAK VINDKFGIEE GLMTTVHSLT
     ATQKTVDGPS QKDWRGGRTA SGNIIPSSTG AAKAVGKVLP VLQGKLTGMA FRVPTVDVSV
     VDLTVKLAKE TTYDEIKAAV KEASEGKMKG VLGYTEEDVV SSDFLSDSHS SIFDASAGIQ
     LSPKFVKLVS WYDNEYGYST RVVDLVEHVA KA
//

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