ID G3P2_RHIRA Reviewed; 338 AA. AC Q96UF2; DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 25-NOV-2008, entry version 39. DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase 2; DE Short=GAPDH 2; DE EC=1.2.1.12; GN Name=GPD2; OS Rhizomucor racemosus (Mucor circinelloides f. lusitanicus). OC Eukaryota; Fungi; Fungi incertae sedis; Basal fungal lineages; OC Mucoromycotina; Mucorales; Mucoraceae; Mucor. OX NCBI_TaxID=4841; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 90680 / R7B; RX PubMed=11860262; DOI=10.1006/fgbi.2001.1313; RA Wolff A.M., Arnau J.; RT "Cloning of glyceraldehyde-3-phosphate dehydrogenase-encoding genes in RT Mucor circinelloides (Syn. racemosus) and use of the gpd1 promoter for RT recombinant protein production."; RL Fungal Genet. Biol. 35:21-29(2002). 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 (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate CC dehydrogenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ293013; CAC37404.1; -; Genomic_DNA. DR HSSP; P56649; 1DSS. DR SMR; Q96UF2; 4-331. 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 1 338 Glyceraldehyde-3-phosphate dehydrogenase FT 2. FT /FTId=PRO_0000145577. FT NP_BIND 12 13 NAD (By similarity). FT REGION 150 152 Glyceraldehyde 3-phosphate binding (By FT similarity). FT REGION 210 211 Glyceraldehyde 3-phosphate binding (By FT similarity). FT ACT_SITE 151 151 Nucleophile (By similarity). FT BINDING 34 34 NAD (By similarity). FT BINDING 79 79 NAD; via carbonyl oxygen (By similarity). FT BINDING 181 181 Glyceraldehyde 3-phosphate (By FT similarity). FT BINDING 233 233 Glyceraldehyde 3-phosphate (By FT similarity). FT BINDING 315 315 NAD (By similarity). FT SITE 178 178 Activates thiol group during catalysis FT (By similarity). SQ SEQUENCE 338 AA; 35864 MW; DE0D19A20D797AEF CRC64; MVTQVGINGF GRIGRIVLRA SLSNPEVQVV AINDPFIPLE YMVYMFKYDS VHGRFQGTVE AKDGKLVVNG KEISVFSERD PAQIPWGSVE AAYVVESTGV FTSIDAASAH LQGGAKKVII SAPSGDAPMF VCGVNLEKYT SDLKVISNAS CTTNCLAPLA KVINDNFGIV EGLMTTVHAT TATQKTVDGP SNKDWRGGRG AGANIIPSST GAAKAVGKVI PELNGKLTGM AFRVPTPDVS VVDLTVRLEK GATYEEIKAV IKKASENELK GILGYTNDQV VSTDFVGDAQ SSIFDAAAGI ALNDKFVKLV SWYDNEFGYS NRVIDLLAYA AKVDAAAQ //