ID   G3P1_METBF              Reviewed;         338 AA.
AC   Q46AH5;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 31.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase 1;
DE            Short=GAPDH 1;
DE            EC=1.2.1.59;
DE   AltName: Full=NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase 1;
GN   Name=gap1; OrderedLocusNames=Mbar_A2189;
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC   Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16980466; DOI=10.1128/JB.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P.,
RA   Han C.S., Lapidus A., Metcalf W.W., Saunders E., Tapia R.,
RA   Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(2006).
CC   -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate + phosphate +
CC       NAD(P)(+) = 3-phospho-D-glyceroyl phosphate + NAD(P)H.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 1/5.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate
CC       dehydrogenase family.
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DR   EMBL; CP000099; AAZ71117.1; -; Genomic_DNA.
DR   RefSeq; YP_305697.1; -.
DR   GeneID; 3626065; -.
DR   GenomeReviews; CP000099_GR; Mbar_A2189.
DR   KEGG; mba:Mbar_A2189; -.
DR   NMPDR; fig|269797.3.peg.1766; -.
DR   HOGENOM; Q46AH5; -.
DR   BioCyc; MBAR269797:MBAR_A2189-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0043891; F:glyceraldehyde-3-phosphate dehydrogenase (N...; IEA:EC.
DR   GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (p...; IEA:HAMAP.
DR   GO; GO:0051287; F:NAD or NADH binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP or NADPH binding; IEA:InterPro.
DR   GO; GO:0006096; P:glycolysis; IEA:HAMAP.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   HAMAP; MF_00559; -; 1.
DR   InterPro; IPR000173; GlycerAld_3-P_DH.
DR   InterPro; IPR006436; Glyceraldehyde-3-P_DH_2_arc.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF02800; Gp_dh_C; 1.
DR   Pfam; PF00044; Gp_dh_N; 1.
DR   PIRSF; PIRSF000149; GAP_DH; 1.
DR   ProDom; PD007761; GAPDH_like; 1.
DR   TIGRFAMs; TIGR01546; GAPDH-II_archae; 1.
DR   PROSITE; PS00071; GAPDH; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Glycolysis; NAD; NADP; Oxidoreductase.
FT   CHAIN         1    338       Glyceraldehyde-3-phosphate dehydrogenase
FT                                1.
FT                                /FTId=PRO_0000232390.
FT   NP_BIND      13     14       NAD (By similarity).
FT   REGION      140    142       Glyceraldehyde 3-phosphate binding (By
FT                                similarity).
FT   REGION      195    196       Glyceraldehyde 3-phosphate binding (By
FT                                similarity).
FT   ACT_SITE    141    141       Nucleophile (By similarity).
FT   BINDING     111    111       NAD; via amide nitrogen (By similarity).
FT   BINDING     169    169       NAD (By similarity).
FT   BINDING     300    300       NAD; via carbonyl oxygen (By similarity).
SQ   SEQUENCE   338 AA;  36958 MW;  0C51D7380992EA43 CRC64;
     MVKAKIAVNG YGTIGKRVAD AVRAQDDMEV IGISKTKPNY EAAVAHQIGY DIYAPAANLE
     AFEKAGMPAA GTIEEMVEKA DLVVDCTPGG IGEKNKPMYE KAGVKAIWQG GEDHSLAGFS
     FNAICNYEQA VGRDLVRVVS CNTTALCRAI YPIDKELGVK KARVVLARRA TDPNDVKKGP
     INAIVPDPIK LPSHHGPDVK SVLPQINITS AALKIPTTLM HVHTVNMEVE KDCTVDDVKN
     IFGSQPRIRF VGQGMSSTAE IMEFARDMKR PRNDMWENCI WPESITVGDK ELYFFQAVHQ
     ESIVVPENVD AIRAMMEFES DGAKSIEKTN KAIGLSKK
//