ID   G3P2_METBF              Reviewed;         338 AA.
AC   Q465K9;
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 2;
DE            Short=GAPDH 2;
DE            EC=1.2.1.59;
DE   AltName: Full=NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase 2;
GN   Name=gap2; OrderedLocusNames=Mbar_A3564;
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; AAZ72433.1; -; Genomic_DNA.
DR   RefSeq; YP_307013.1; -.
DR   GeneID; 3626493; -.
DR   GenomeReviews; CP000099_GR; Mbar_A3564.
DR   KEGG; mba:Mbar_A3564; -.
DR   NMPDR; fig|269797.3.peg.2568; -.
DR   HOGENOM; Q465K9; -.
DR   OMA; Q465K9; ESHPIAG.
DR   BioCyc; MBAR269797:MBAR_A3564-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                                2.
FT                                /FTId=PRO_0000232391.
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;  36868 MW;  B1610F59B57B7710 CRC64;
     MAKAKIAVNG YGTIGKRVAD AVRAQDDMEV VGISKTKPNY EAAVAHRLGY DIYAPAANLE
     AFEKAGMPAA GSIEEMLEKA DLVVDCTPGG IGEKNKPIYE KVGIKAIWQG GESHPIAGFS
     FNAESNYEQA VGRDLTRVVS CNTTALCRAI STIDRELGVN KVRASLSRRA VDPNEIKKGP
     VDAIVLNPVK LPSHHGPDVR SVLPHINITT AAIKVPTTLM HVHTVNMEVN KDCTAEDVKN
     IFGSQSRIRL VGQGITSTAE IIEFARDIGR PRHDMWELCI WPESITVTDK ELYFFHAVHQ
     ESIVVPENVD AIRAMMELES DGAKSIEKTN KAIGLYNK
//