ID   G3P2_RHOSH              Reviewed;         333 AA.
AC   P29272;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   25-NOV-2008, entry version 52.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase B;
DE            Short=GAPDH;
DE            EC=1.2.1.12;
GN   Name=gapB;
OS   Rhodobacter sphaeroides (Rhodopseudomonas sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=1063;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=92041881; PubMed=1939098;
RA   Chen J.-H., Gibson J.L., McCue L.A., Tabita F.R.;
RT   "Identification, expression, and deduced primary structure of
RT   transketolase and other enzymes encoded within the form II CO2
RT   fixation operon of Rhodobacter sphaeroides.";
RL   J. Biol. Chem. 266:20447-20452(1991).
CC   -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate + phosphate +
CC       NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 1/5.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MISCELLANEOUS: This protein is encoded within the form II
CC       ribulose-bisphosphate carboxylase operon.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate
CC       dehydrogenase family.
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DR   EMBL; M68914; AAA26156.1; -; Genomic_DNA.
DR   PIR; C41080; C41080.
DR   HSSP; P00362; 1NQO.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (p...; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR000173; GlycerAld_3-P_DHase.
DR   InterPro; IPR006424; Glyceraldehyde-3-P_DHase_1.
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   PRINTS; PR00078; G3PDHDRGNASE.
DR   TIGRFAMs; TIGR01534; GAPDH-I; 1.
DR   PROSITE; PS00071; GAPDH; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Glycolysis; NAD; Oxidoreductase.
FT   CHAIN         1    333       Glyceraldehyde-3-phosphate dehydrogenase
FT                                B.
FT                                /FTId=PRO_0000145675.
FT   NP_BIND      12     13       NAD (By similarity).
FT   REGION      150    152       Glyceraldehyde 3-phosphate binding (By
FT                                similarity).
FT   REGION      209    210       Glyceraldehyde 3-phosphate binding (By
FT                                similarity).
FT   ACT_SITE    151    151       Nucleophile (By similarity).
FT   BINDING      36     36       NAD (By similarity).
FT   BINDING      80     80       NAD; via carbonyl oxygen (By similarity).
FT   BINDING     181    181       Glyceraldehyde 3-phosphate (By
FT                                similarity).
FT   BINDING     196    196       Glyceraldehyde 3-phosphate (By
FT                                similarity).
FT   BINDING     232    232       Glyceraldehyde 3-phosphate (By
FT                                similarity).
FT   BINDING     314    314       NAD (By similarity).
FT   SITE        178    178       Activates thiol group during catalysis
FT                                (By similarity).
SQ   SEQUENCE   333 AA;  35679 MW;  B072F443A20C3AFD CRC64;
     MTIRVAINGF GRIGRNVLRA IVESGRTDIE VVAINDLGQV ETNAHLLRFD SVHGRFPAKV
     TSGDDWIDVG RGPIKVTAIR NPAELPWAGV DMAMECTGIF TTKEKAAAHL QNGAKRVLVS
     APCDGADRTI VYGVNHATLT ADDLVVSNAS CTTNCLSPVA KVLHDAIGIA KGFMTTIHSY
     TGDQPTLDTM HKDLYRARAA ALSMIPTSTG AAKAVGLVLP ELKGRLDGVS IRVPTPNVSV
     VDLVFEAARD TTVEEVNAAI EAAACGPLKG VLGFTTEPNV SSDFNHDPHS SVFHMDQTKV
     MEGRMVRILS WYDNEWGFSN RMADTAVAMG RLL
//