ID   G3P_METM5               Reviewed;         340 AA.
AC   A4FZL2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   16-JUN-2009, entry version 21.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase;
DE            Short=GAPDH;
DE            EC=1.2.1.59;
DE   AltName: Full=NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase;
GN   Name=gap; OrderedLocusNames=MmarC5_1348;
OS   Methanococcus maripaludis (strain C5 / ATCC BAA-1333).
OC   Archaea; Euryarchaeota; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=402880;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Han C., Detter J.C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Whitman W.B.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Methanococcus maripaludis C5.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000609; ABO35646.1; -; Genomic_DNA.
DR   RefSeq; YP_001097860.1; -.
DR   GeneID; 4928002; -.
DR   GenomeReviews; CP000609_GR; MmarC5_1348.
DR   KEGG; mmq:MmarC5_1348; -.
DR   OMA; A4FZL2; AIFQGGE.
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   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    340       Glyceraldehyde-3-phosphate dehydrogenase.
FT                                /FTId=PRO_1000061117.
FT   NP_BIND      11     12       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     303    303       NAD; via carbonyl oxygen (By similarity).
SQ   SEQUENCE   340 AA;  37373 MW;  1D70580433C5764B CRC64;
     MVNVLINGYG SIGKRVADAV AKQDDMKVIG VTKTKPDFEA RMAVEKGYKL FAAIPERKHL
     FEEAGIPVEG TLDDIIEDAD IVVDGAPKKI GKANLENVYK KHGVKAILQG GEKAGDAQDS
     FNSLWSYDRC YGKDYIRLVS CNTTGLCRSM YAINSVADIL KARIVLIRRA ADPNDIKTGP
     VNAIVPNPVT VPSHHGPDVV SVIPQLDGKI MTSAVIVPTT LMHMHSIMVE TSGTNRDEII
     DALAKTPRIL TLKASEGFDS TAKIIEYSRD LGRSRYDLNE IAVWEESVNV VDNEVYMMQA
     IHQESDVIPE NVDCIRAMLE MESDNLKSIE KTNKAMGLIK
//