ID   G3P1_ANAVT              Reviewed;         343 AA.
AC   P34916; Q3MFW7;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   25-NOV-2008, entry version 66.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase 1;
DE            EC=1.2.1.12;
GN   Name=gap1; OrderedLocusNames=Ava_0495;
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; L07497; AAA21995.2; -; Genomic_DNA.
DR   EMBL; CP000117; ABA20119.1; -; Genomic_DNA.
DR   PIR; I39602; I39602.
DR   RefSeq; YP_321014.1; -.
DR   HSSP; P06977; 1DC5.
DR   GeneID; 3682402; -.
DR   GenomeReviews; CP000117_GR; Ava_0495.
DR   KEGG; ava:Ava_0495; -.
DR   NMPDR; fig|240292.3.peg.1853; -.
DR   HOGENOM; P34916; -.
DR   BioCyc; AVAR240292:AVA_0495-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   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   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    343       Glyceraldehyde-3-phosphate dehydrogenase
FT                                1.
FT                                /FTId=PRO_0000145624.
FT   NP_BIND      13     14       NAD (By similarity).
FT   REGION      154    156       Glyceraldehyde 3-phosphate binding (By
FT                                similarity).
FT   REGION      214    215       Glyceraldehyde 3-phosphate binding (By
FT                                similarity).
FT   ACT_SITE    155    155       Nucleophile (By similarity).
FT   BINDING      35     35       NAD (By similarity).
FT   BINDING      79     79       NAD; via carbonyl oxygen (By similarity).
FT   BINDING     185    185       Glyceraldehyde 3-phosphate (By
FT                                similarity).
FT   BINDING     237    237       Glyceraldehyde 3-phosphate (By
FT                                similarity).
FT   BINDING     319    319       NAD (By similarity).
FT   SITE        182    182       Activates thiol group during catalysis
FT                                (By similarity).
FT   CONFLICT    240    240       T -> I (in Ref. 1; AAA21995).
SQ   SEQUENCE   343 AA;  36666 MW;  307D0703DF8D279C CRC64;
     MAKLKVGING FGRIGRLVLR AGINNPNIEF VGINDLVPPD NLAYLLKYDS THGKLRSQVE
     AKDDGIVIDG HFIPCVSVRN PAELPWGKLG ADYVVESTGL FTDSEGASKH LQAGAKRVII
     SAPTKDPDRV RTLLVGVNHD LFDPSKDVIV SNASCTTNCL APIAKVINDN FGLTEGLMTT
     VHAMTATQPT VDGPSKKDWR GGRGAAQNII PSSTGAAKAV ALVLPELKGK LTGMAFRVPT
     PDVSVVDLTF KTAKATSYKE ICAAMKQASE GSLAGILGYT DEEVVSTDFQ GDTHSSIFDA
     GAGIELNSNF FKVVAWYDNE WGYSNRVVDL MLSMIQKEQL AAV
//