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Database: UniProt
Entry: A7XGB6_9STRA
LinkDB: A7XGB6_9STRA
Original site: A7XGB6_9STRA 
ID   A7XGB6_9STRA            Unreviewed;       546 AA.
AC   A7XGB6;
DT   23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   23-OCT-2007, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=Triosephosphate isomerase/glyceraldehyde-3-phosphate dehydrogenase {ECO:0000313|EMBL:ABU99205.1};
DE   Flags: Fragment;
GN   Name=tigA {ECO:0000313|EMBL:ABU99205.1};
OS   Phytophthora kelmanii.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=2805668 {ECO:0000313|EMBL:ABU99205.1};
RN   [1] {ECO:0000313|EMBL:ABU99205.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PD_00100 {ECO:0000313|EMBL:ABU99205.1};
RX   PubMed=18039586; DOI=10.1016/j.fgb.2007.10.010;
RA   Blair J.E., Coffey M.D., Park S.Y., Geiser D.M., Kang S.;
RT   "A multi-locus phylogeny for Phytophthora utilizing markers derived from
RT   complete genome sequences.";
RL   Fungal Genet. Biol. 45:266-277(2008).
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}.
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DR   EMBL; EU079611; ABU99205.1; -; Genomic_DNA.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; 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:UniProtKB-KW.
DR   CDD; cd00311; TIM; 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   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:ABU99205.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          235..383
FT                   /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT                   binding"
FT                   /evidence="ECO:0000259|SMART:SM00846"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ABU99205.1"
FT   NON_TER         546
FT                   /evidence="ECO:0000313|EMBL:ABU99205.1"
SQ   SEQUENCE   546 AA;  58666 MW;  5D4A3DE1D0BB8829 CRC64;
     QELVGMLNTA RIPADVEVVV APSQVHAATV KASLRADVRV SGQDVWKQGN GAFTGETSAE
     MLKDLGAEYT LVGHSERREK GEXNEIVAKK AAYALEKGLA VIACIGESKE TREANETVAY
     ITEQLNAYAA XIKDWTNVVI AYEPIWAIGT GLTASPEQAQ DVHASIRAWL KEKVSPEAAE
     KTRVIYGGSV GAKNAPELSQ KEDIDGFLVG GASLKPDFLQ IINAQNPTEN VGGAVNVAIN
     GFGRIGRLVL RAAAKNPLIN IVAINDPFIS TTYMEYMLEY DTVHGKFDGA LSHDEQHIFV
     NGKPIRVFNE MNPSNIKWXE EQVQYVVEST GAFTTLEKAS THLQNXVEKV VISAPSSDAP
     MFVMGVNHEL YEKNMHVVSN ASCTTNCLAP LAKVVNDKFG IKEGLMTTVH AVTATQKTVD
     GPSKKDWRGG RGACFNIIPS STGAAKAVGK VIPSLNGKLT GMSFRVPTAD VSVVDLTARL
     VNPASYDEIK AAIKDASENE MKGILGYTEK AVVSSDFIGD SHSSIFDASA GIALTDDFVK
     LVSWYD
//
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