ID Q9M7R8_ACHBI Unreviewed; 596 AA. AC Q9M7R8; DT 01-OCT-2000, integrated into UniProtKB/TrEMBL. DT 01-OCT-2000, sequence version 1. DT 27-NOV-2024, entry version 89. DE SubName: Full=Triosephosphate isomerase + glyceraldehyde-3-phosphate dehydrogenase {ECO:0000313|EMBL:AAF44720.1}; GN Name=TigA {ECO:0000313|EMBL:AAF44720.1}; OS Achlya bisexualis (Water mold). OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae; OC Achlya. OX NCBI_TaxID=4766 {ECO:0000313|EMBL:AAF44720.1}; RN [1] {ECO:0000313|EMBL:AAF44720.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=10677844; RA Liaud M.F., Lichtle C., Apt K., Martin W., Cerff R.; RT "Compartment-specific isoforms of TPI and GAPDH are imported into diatom RT mitochondria as a fusion protein: evidence in favor of a mitochondrial RT origin of the eukaryotic glycolytic pathway."; RL Mol. Biol. Evol. 17:213-223(2000). CC -!- PATHWAY: Carbohydrate biosynthesis. {ECO:0000256|ARBA:ARBA00024331}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}. CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase CC family. {ECO:0000256|ARBA:ARBA00007406, ECO:0000256|RuleBase:RU000397}. CC -!- SIMILARITY: Belongs to the triosephosphate isomerase family. CC {ECO:0000256|ARBA:ARBA00007422}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF063107; AAF44720.1; -; mRNA. DR AlphaFoldDB; Q9M7R8; -. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IEA:TreeGrafter. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0004807; F:triose-phosphate isomerase activity; IEA:InterPro. DR GO; GO:0006006; P:glucose metabolic process; IEA:InterPro. DR GO; GO:0006096; P:glycolytic process; IEA:InterPro. DR CDD; cd00311; TIM; 1. DR FunFam; 3.30.360.10:FF:000001; Glyceraldehyde-3-phosphate dehydrogenase; 1. DR FunFam; 3.40.50.720:FF:000266; Glyceraldehyde-3-phosphate dehydrogenase; 1. DR FunFam; 3.20.20.70:FF:000025; Triosephosphate isomerase; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR HAMAP; MF_00147_B; TIM_B; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020831; GlycerAld/Erythrose_P_DH. DR InterPro; IPR020830; GlycerAld_3-P_DH_AS. DR InterPro; IPR020829; GlycerAld_3-P_DH_cat. DR InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd. DR InterPro; IPR006424; Glyceraldehyde-3-P_DH_1. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR035990; TIM_sf. DR InterPro; IPR022896; TrioseP_Isoase_bac/euk. DR InterPro; IPR000652; Triosephosphate_isomerase. DR InterPro; IPR020861; Triosephosphate_isomerase_AS. DR NCBIfam; TIGR01534; GAPDH-I; 1. DR NCBIfam; TIGR00419; tim; 1. DR PANTHER; PTHR10836; GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE; 1. DR PANTHER; PTHR10836:SF134; TRIOSEPHOSPHATE ISOMERASE_GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE; 1. DR Pfam; PF02800; Gp_dh_C; 1. DR Pfam; PF00044; Gp_dh_N; 1. DR Pfam; PF00121; TIM; 1. DR PRINTS; PR00078; G3PDHDRGNASE. DR SMART; SM00846; Gp_dh_N; 1. DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR SUPFAM; SSF51351; Triosephosphate isomerase (TIM); 1. DR PROSITE; PS00071; GAPDH; 1. DR PROSITE; PS00171; TIM_1; 1. DR PROSITE; PS51440; TIM_2; 1. PE 2: Evidence at transcript level; KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:AAF44720.1}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}. FT DOMAIN 263..411 FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P) FT binding" FT /evidence="ECO:0000259|SMART:SM00846" SQ SEQUENCE 596 AA; 64255 MW; D4CA852D53F8AD31 CRC64; MQVRRFSSVA RKFFVGGNWK CNGSLSQAQS LVDTLNTATI PKNVEVVVAP ASIHALSVKS SLRKDIGVSG QDTWSRGNGA FTGEVSAEML KDAGINYTII GHSERRQKGE TNEEVASKAG YALSKGVSVI ACIGETKIER EAQKTMQVVT EQLAAYAKNI TDWSNVVIAY EPVWAIGTGL TATPEQAQEV HAGIRSWLKQ NVSSAVADAT RIIYGGSVTA GNAAELSKKA DIDGFLVGGA SLKPDFLSII NCQNDKAHQG GPVNIAINGF GRIGRLVLRA AQTNPLLNVV AVNDPFIPTE YMEYMLKHDT VHGHFDGTVR HEGDHIIVND RKIRVFGEKD PKAIKWGESD VEYVVESTGA FTTKEKASAH LLNGPRKVVI SAPSADAPMF VVGVNHDKYD PSMNIVSNAS CTTNCLAPLA KVVNDKFGII EGLMTTVHAV TATQLTVDGP SKKDWRGGRA ACFNIIPSST GAAKAVGKVI PELNGKLTGM SFRVPTANVS VVDLTVRLRN KASYEDIKAA IKYASENELR GILGYTDTAV VSSDFISDPR SSIFDADAGI VLTDDFVKLV SWYDNEWGYS NRVLDLITHM VHTERQ //