ID   G3P2_ANASP              Reviewed;         337 AA.
AC   P58554;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 1.
DT   04-NOV-2008, entry version 45.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase 2;
DE            EC=1.2.1.12;
GN   Name=gap2; OrderedLocusNames=all5062;
OS   Anabaena sp. (strain PCC 7120).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=21595285; PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S.,
RA   Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T.,
RA   Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
RA   Nakazaki N., Shimpo S., Sugimoto M., Takazawa M., Yamada M.,
RA   Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
CC   -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate + phosphate +
CC       NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 1/5.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate
CC       dehydrogenase family.
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DR   EMBL; BA000019; BAB76761.1; -; Genomic_DNA.
DR   PIR; AF2438; AF2438.
DR   RefSeq; NP_489102.1; -.
DR   HSSP; P19866; 1NBO.
DR   SMR; P58554; 2-335.
DR   GeneID; 1108666; -.
DR   GenomeReviews; BA000019_GR; all5062.
DR   KEGG; ana:all5062; -.
DR   NMPDR; fig|103690.1.peg.5369; -.
DR   HOGENOM; P58554; -.
DR   BioCyc; NSP103690:ALL5062-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR000173; GlycerAld_3-P_DHase.
DR   InterPro; IPR006424; Glyceraldehyde-3-P_DHase_1.
DR   InterPro; IPR016040; NAD(P)-bd.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 2.
DR   PANTHER; PTHR10836; GAP_DH; 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   TIGRFAMs; TIGR01534; GAPDH-I; 1.
DR   PROSITE; PS00071; GAPDH; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Glycolysis; NAD; Oxidoreductase.
FT   CHAIN         1    337       Glyceraldehyde-3-phosphate dehydrogenase
FT                                2.
FT                                /FTId=PRO_0000145625.
FT   NP_BIND      11     12       NAD (By similarity).
FT   REGION      153    155       Glyceraldehyde 3-phosphate binding (By
FT                                similarity).
FT   REGION      212    213       Glyceraldehyde 3-phosphate binding (By
FT                                similarity).
FT   ACT_SITE    154    154       Nucleophile (By similarity).
FT   BINDING      35     35       NAD (By similarity).
FT   BINDING      80     80       NAD; via carbonyl oxygen (By similarity).
FT   BINDING     184    184       Glyceraldehyde 3-phosphate (By
FT                                similarity).
FT   BINDING     199    199       Glyceraldehyde 3-phosphate (By
FT                                similarity).
FT   BINDING     235    235       Glyceraldehyde 3-phosphate (By
FT                                similarity).
FT   BINDING     317    317       NAD (By similarity).
FT   SITE        181    181       Activates thiol group during catalysis
FT                                (By similarity).
SQ   SEQUENCE   337 AA;  36910 MW;  6671C88D5CC7E033 CRC64;
     MIRVAINGFG RIGRNFARCW LGRENTNIEL VAVNDTSDPR TNAHLLKYDS MLGKLKNVDI
     TADDNSITVN GKTIKCVSDR NPENLPWKEW EIDLIIEATG VFVSKEGATK HINAGAKKVL
     ITAPGKNEDG TFVMGVNHHD YDHNLHNIIS NASCTTNCLA PIAKVLNDKF GIIKGSMTTT
     HSYTGDQRLL DASHRDLRRA RAAAINIVPT STGAAKAVAL VIPELKGKLN GVALRVPTPN
     VSMVDFVVQV EKRTITEEVN QALKDASEGP LKGILDYSEL QLVSSDYQGT DASSIVDANL
     TLVMGNDLVK VMAWYDNEWG YSQRVLDLAE LVAEKWV
//