ID   G3P_METHJ               Reviewed;         339 AA.
AC   Q2FNA2;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 27.
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=Mhun_2462;
OS   Methanospirillum hungatei (strain JF-1 / DSM 864).
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanomicrobiales;
OC   Methanospirillaceae; Methanospirillum.
OX   NCBI_TaxID=323259;
RN   [1]
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., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Ivanova N., McInerney M.J., Brockman F., Culley D.,
RA   Ferry J.G., Gunsalus R.P., Morrison M., Plugge C., Scholten J.,
RA   Stams A.J.M., Boone D.R., Richardson P.;
RT   "Complete sequence of Methanospirillum hungatei JF-1.";
RL   Submitted (JAN-2006) 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; CP000254; ABD42162.1; -; Genomic_DNA.
DR   RefSeq; YP_503881.1; -.
DR   GeneID; 3923967; -.
DR   GenomeReviews; CP000254_GR; Mhun_2462.
DR   KEGG; mhu:Mhun_2462; -.
DR   NMPDR; fig|323259.5.peg.2588; -.
DR   HOGENOM; Q2FNA2; -.
DR   OMA; Q2FNA2; AIFQGGE.
DR   BioCyc; MHUN323259:MHUN_2462-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   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   ProDom; PD004105; DapB; 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    339       Glyceraldehyde-3-phosphate dehydrogenase.
FT                                /FTId=PRO_0000300974.
FT   NP_BIND      11     12       NAD (By similarity).
FT   REGION      139    141       Glyceraldehyde 3-phosphate binding (By
FT                                similarity).
FT   REGION      194    195       Glyceraldehyde 3-phosphate binding (By
FT                                similarity).
FT   ACT_SITE    140    140       Nucleophile (By similarity).
FT   BINDING     110    110       NAD; via amide nitrogen (By similarity).
FT   BINDING     168    168       NAD (By similarity).
FT   BINDING     301    301       NAD; via carbonyl oxygen (By similarity).
SQ   SEQUENCE   339 AA;  36818 MW;  3C149595098A350B CRC64;
     MIKVAINGYG TIGKRVADAV SAQKDMEIIG VSKTKPSAEA LIAVQRGYPI YIADMSKKDA
     FAKAGIPVAG SVEDMLKKAD IVVDGTPGGV GESNKALYEK AGVKAIWQGG EDHEVAGFSF
     NAHANYKDAI GRQFVRVVSC NTTGLCRVIK AVDDAFGVVK VRAVMVRRGA DPHVVKKGPI
     DAVVLDPPTI PSHHGPDVNT VLPHIDIVTM AMIVPTTQMH MHAITIELKK EVSRDDVLAV
     MRSHNRIGLV QPKTAIKSTA ELKEYVMDMG RPRSDLWENG IFEASVNMVG KELFFFQAIH
     QEADVVIENV DAIRAMMGEV RDPETSIRMT NEAMQFTAL
//