ID   G3P_METMA               Reviewed;         335 AA.
AC   Q8PTD3;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 54.
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=MM_2782;
OS   Methanosarcina mazei (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC   Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=2209;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11883 / OCM 88;
RX   MEDLINE=22120827; PubMed=12125824;
RA   Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA   Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA   Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA   Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA   Fritz H.-J., Gottschalk G.;
RT   "The genome of Methanosarcina mazei: evidence for lateral gene
RT   transfer between Bacteria and Archaea.";
RL   J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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; AE008384; AAM32478.1; -; Genomic_DNA.
DR   RefSeq; NP_634806.1; -.
DR   HSSP; P10618; 1CF2.
DR   GeneID; 1481124; -.
DR   GenomeReviews; AE008384_GR; MM_2782.
DR   KEGG; mma:MM_2782; -.
DR   NMPDR; fig|192952.1.peg.2782; -.
DR   HOGENOM; Q8PTD3; -.
DR   OMA; Q8PTD3; AIFQGGE.
DR   BioCyc; MMAZ192952:MM2782-MON; -.
DR   BRENDA; 1.2.1.59; 261165.
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    335       Glyceraldehyde-3-phosphate dehydrogenase.
FT                                /FTId=PRO_0000145725.
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     171    171       Glyceraldehyde 3-phosphate (By
FT                                similarity).
FT   BINDING     300    300       NAD; via carbonyl oxygen (By similarity).
SQ   SEQUENCE   335 AA;  36611 MW;  2AA26758A387D46E CRC64;
     MVKAKIAVNG YGTIGKRVAD AVQAQDDMEI IGVSKTKPNY EAAVAHQKGY DLFAPASNSG
     AFEKAGIPLA GTIEEMVEKA DLVVDCTPGG IGEANKPMYE KAGVKAIWQG GEDHELAGFS
     FNAASNYEGA LGRDLVRVVS CNTTGLCRVI YPIDRELGVK KVRVTLARRA TDPNDIKKGP
     INAIVPDPIK LPSHHGPDIK SVLPHINITT AALKIPTTLM HLHTVNMEVN TDCTAEDINR
     IFSSQSRIRF MSQGINSTAE IIELARDMGR PRNDMWENCI WPESITVHER EFYFFQAIHQ
     ESIVVPETVD AIRAMMELES DGAKSIQKTN KAIGL
//