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Database: UniProt
Entry: P44304
LinkDB: P44304
Original site: P44304 
ID   G3P_HAEIN               Reviewed;         339 AA.
AC   P44304;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   09-DEC-2015, entry version 116.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000250|UniProtKB:P0A9B2};
DE            Short=GAPDH {ECO:0000250|UniProtKB:P0A9B2};
DE            EC=1.2.1.12 {ECO:0000250|UniProtKB:P0A9B2};
DE   AltName: Full=NAD-dependent glyceraldehyde-3-phosphate dehydrogenase {ECO:0000250|UniProtKB:P0A9B2};
GN   Name=gapA; Synonyms=gapDH; OrderedLocusNames=HI_0001;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M.,
RA   Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D.,
RA   Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C.,
RA   Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M.,
RA   Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O.,
RA   Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
CC   -!- FUNCTION: Catalyzes the oxidative phosphorylation of
CC       glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG)
CC       using the cofactor NAD. The first reaction step involves the
CC       formation of a hemiacetal intermediate between G3P and a cysteine
CC       residue, and this hemiacetal intermediate is then oxidized to a
CC       thioester, with concomitant reduction of NAD to NADH. The reduced
CC       NADH is then exchanged with the second NAD, and the thioester is
CC       attacked by a nucleophilic inorganic phosphate to produce BPG.
CC       {ECO:0000250|UniProtKB:P0A9B2}.
CC   -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate + phosphate +
CC       NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH.
CC       {ECO:0000250|UniProtKB:P0A9B2}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 1/5. {ECO:0000305}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P0A9B2}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate
CC       dehydrogenase family. {ECO:0000305}.
DR   EMBL; L42023; AAC21680.1; -; Genomic_DNA.
DR   PIR; G64041; G64041.
DR   RefSeq; NP_438174.1; NC_000907.1.
DR   RefSeq; WP_005646416.1; NC_000907.1.
DR   ProteinModelPortal; P44304; -.
DR   SMR; P44304; 3-334.
DR   STRING; 71421.HI0001; -.
DR   PRIDE; P44304; -.
DR   EnsemblBacteria; AAC21680; AAC21680; HI_0001.
DR   GeneID; 950899; -.
DR   KEGG; hin:HI0001; -.
DR   PATRIC; 20188453; VBIHaeInf48452_0001.
DR   eggNOG; ENOG4105C17; Bacteria.
DR   eggNOG; COG0057; LUCA.
DR   KO; K00134; -.
DR   OMA; KWGEVGA; -.
DR   OrthoDB; EOG66TG3S; -.
DR   PhylomeDB; P44304; -.
DR   UniPathway; UPA00109; UER00184.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; ISS:UniProtKB.
DR   GO; GO:0051287; F:NAD binding; ISS:UniProtKB.
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   Gene3D; 3.40.50.720; -; 1.
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; IPR016040; NAD(P)-bd_dom.
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;
KW   Complete proteome; Cytoplasm; Glycolysis; NAD; Nucleotide-binding;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN         1    339       Glyceraldehyde-3-phosphate dehydrogenase.
FT                                /FTId=PRO_0000145661.
FT   NP_BIND      12     13       NAD. {ECO:0000250|UniProtKB:P00362}.
FT   REGION      149    151       Glyceraldehyde 3-phosphate binding.
FT                                {ECO:0000250|UniProtKB:P0A9B2}.
FT   REGION      209    210       Glyceraldehyde 3-phosphate binding.
FT                                {ECO:0000250|UniProtKB:P0A9B2}.
FT   ACT_SITE    150    150       Nucleophile.
FT                                {ECO:0000250|UniProtKB:P0A9B2}.
FT   BINDING      34     34       NAD. {ECO:0000250|UniProtKB:P0A9B2}.
FT   BINDING      78     78       NAD; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P0A9B2}.
FT   BINDING     120    120       NAD. {ECO:0000250|UniProtKB:P0A9B2}.
FT   BINDING     180    180       Glyceraldehyde 3-phosphate.
FT                                {ECO:0000250|UniProtKB:P0A9B2}.
FT   BINDING     232    232       Glyceraldehyde 3-phosphate.
FT                                {ECO:0000250|UniProtKB:P0A9B2}.
FT   BINDING     319    319       NAD. {ECO:0000250|UniProtKB:P0A9B2}.
FT   SITE        177    177       Activates thiol group during catalysis.
FT                                {ECO:0000250|UniProtKB:P0A9B2}.
SQ   SEQUENCE   339 AA;  36052 MW;  87119EDEB114EDF0 CRC64;
     MAIKIGINGF GRIGRIVFRA AQHRDDIEVV GINDLIDVEY MAYMLKYDST HGRFDGTVEV
     KDGNLVVNGK TIRVTAERDP ANLNWGAIGV DIAVEATGLF LTDETARKHI TAGAKKVVLT
     GPSKDATPMF VRGVNFNAYA GQDIVSNASC TTNCLAPLAR VVHETFGIKD GLMTTVHATT
     ATQKTVDGPS AKDWRGGRGA SQNIIPSSTG AAKAVGKVLP ALNGKLTGMA FRVPTPNVSV
     VDLTVNLEKP ASYDAIKQAI KDAAEGKTFN GELKGVLGYT EDAVVSTDFN GCALTSVFDA
     DAGIALTDSF VKLVSWYDNE TGYSNKVLDL VAHIYNYKG
//
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