ID   G3P2_ANAVT              Reviewed;         337 AA.
AC   P34917; Q3MAQ0;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 2.
DT   25-NOV-2008, entry version 67.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase 2;
DE            EC=1.2.1.12;
GN   Name=gap2; OrderedLocusNames=Ava_2318;
OS   Anabaena variabilis (strain ATCC 29413 / PCC 7937).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena.
OX   NCBI_TaxID=240292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=93391421; PubMed=8378350;
RA   Martin W., Brinkmann H., Savona C., Cerff R.;
RT   "Evidence for a chimeric nature of nuclear genomes: eubacterial origin
RT   of eukaryotic glyceraldehyde-3-phosphate dehydrogenase genes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:8692-8696(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.;
RT   "Complete sequence of Anabaena variabilis ATCC 29413.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate
CC       dehydrogenase family.
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DR   EMBL; L07498; AAA21996.1; -; Genomic_DNA.
DR   EMBL; CP000117; ABA21936.1; -; Genomic_DNA.
DR   PIR; I39603; I39603.
DR   RefSeq; YP_322831.1; -.
DR   HSSP; P19866; 1NBO.
DR   SMR; P34917; 2-335.
DR   GeneID; 3683588; -.
DR   GenomeReviews; CP000117_GR; Ava_2318.
DR   KEGG; ava:Ava_2318; -.
DR   NMPDR; fig|240292.3.peg.198; -.
DR   HOGENOM; P34917; -.
DR   BioCyc; AVAR240292:AVA_2318-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (p...; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
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_0000145626.
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).
FT   CONFLICT     47     47       K -> N (in Ref. 1; AAA21996).
FT   CONFLICT     51     51       M -> S (in Ref. 1; AAA21996).
FT   CONFLICT     54     57       KLKN -> VKK (in Ref. 1; AAA21996).
FT   CONFLICT    114    114       A -> V (in Ref. 1; AAA21996).
FT   CONFLICT    217    217       A -> R (in Ref. 1; AAA21996).
SQ   SEQUENCE   337 AA;  36876 MW;  4FDCBD856B858863 CRC64;
     MIRVAINGFG RIGRNFARCW LGRENSNIEL VAVNDTSDPR TNAHLLKYDS MLGKLKNVDI
     TADDNSITVN GKTIKCVSDR NPENLPWKEW EIDLIIESTG VFTSKEGALK HVNAGAKKVL
     ITAPGKNEDG TFVIGVNHHD YDHNVHHIIS NASCTTNCLA PIAKVLNDKF GIIKGSMTTT
     HSYTGDQRLL DASHRDLRRA RAAAINIVPT STGAAKAVAL VIPELKGKLN GVALRVPTPN
     VSMVDFVVQV EKRTITEEVN QALKDASEGP LKGILDYSEL QLVSSDYQGT DASSIVDASL
     TLVMGNDLVK VMAWYDNEWG YSQRVLDLAE LVAEKWV
//