(data stored in ACNUC8465 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   11-DEC-2019, entry version 72.
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; Saccharomycetes;
OC   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., Jubin C.,
RA   Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA   Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA   Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA   Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA   Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA   Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA   Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA   Ozanne C., Richard G.-F., Sacerdot C., 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 = (2R)-3-
CC         phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, 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. {ECO:0000256|RuleBase:RU361160}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|RuleBase:RU361160}.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC       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; NAKVLAW; -.
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   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
FT                   /note="Gp_dh_N"
FT                   /evidence="ECO:0000259|SMART:SM00846"
FT   NP_BIND         12..13
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT   REGION          149..151
FT                   /note="Glyceraldehyde 3-phosphate binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT   REGION          209..210
FT                   /note="Glyceraldehyde 3-phosphate binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT   ACT_SITE        150
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-1"
FT   BINDING         34
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT   BINDING         79
FT                   /note="NAD; via carbonyl oxygen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT   BINDING         121
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT   BINDING         180
FT                   /note="Glyceraldehyde 3-phosphate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT   BINDING         232
FT                   /note="Glyceraldehyde 3-phosphate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT   BINDING         314
FT                   /note="NAD"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT   SITE            177
FT                   /note="Activates thiol group during catalysis"
FT                   /evidence="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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