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Database: UniProt
Entry: A0A161YIU5_DAUCS
LinkDB: A0A161YIU5_DAUCS
Original site: A0A161YIU5_DAUCS 
ID   A0A161YIU5_DAUCS        Unreviewed;       288 AA.
AC   A0A161YIU5;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Glyceraldehyde 3-phosphate dehydrogenase NAD(P) binding domain-containing protein {ECO:0000259|SMART:SM00846};
GN   ORFNames=DCAR_016414 {ECO:0000313|EMBL:KZM93169.1};
OS   Daucus carota subsp. sativus (Carrot).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; Daucinae;
OC   Daucus; Daucus sect. Daucus.
OX   NCBI_TaxID=79200 {ECO:0000313|EMBL:KZM93169.1, ECO:0000313|Proteomes:UP000077755};
RN   [1] {ECO:0000313|EMBL:KZM93169.1, ECO:0000313|Proteomes:UP000077755}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DH1 {ECO:0000313|Proteomes:UP000077755};
RC   TISSUE=Leaf {ECO:0000313|EMBL:KZM93169.1};
RX   PubMed=27158781; DOI=10.1038/ng.3565;
RA   Iorizzo M., Ellison S., Senalik D., Zeng P., Satapoomin P., Huang J.,
RA   Bowman M., Iovene M., Sanseverino W., Cavagnaro P., Yildiz M.,
RA   Macko-Podgorni A., Moranska E., Grzebelus E., Grzebelus D., Ashrafi H.,
RA   Zheng Z., Cheng S., Spooner D., Van Deynze A., Simon P.;
RT   "A high-quality carrot genome assembly provides new insights into
RT   carotenoid accumulation and asterid genome evolution.";
RL   Nat. Genet. 48:657-666(2016).
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00007406, ECO:0000256|RuleBase:RU000397}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KZM93169.1}.
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DR   EMBL; LNRQ01000005; KZM93169.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A161YIU5; -.
DR   STRING; 79200.A0A161YIU5; -.
DR   EnsemblPlants; KZM93169; KZM93169; DCAR_016414.
DR   Gramene; KZM93169; KZM93169; DCAR_016414.
DR   OMA; ITYMYSK; -.
DR   Proteomes; UP000077755; Chromosome 5.
DR   GO; GO:0051287; F:NAD 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:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR020831; GlycerAld/Erythrose_P_DH.
DR   InterPro; IPR020829; GlycerAld_3-P_DH_cat.
DR   InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR10836; GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR10836:SF76; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF02800; Gp_dh_C; 1.
DR   Pfam; PF00044; Gp_dh_N; 1.
DR   PIRSF; PIRSF000149; GAP_DH; 2.
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.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000149-3};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000149-3};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077755}.
FT   DOMAIN          4..118
FT                   /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT                   binding"
FT                   /evidence="ECO:0000259|SMART:SM00846"
FT   BINDING         13..14
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT   BINDING         35
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT   BINDING         82
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT   BINDING         269
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT   SITE            132
FT                   /note="Activates thiol group during catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-4"
SQ   SEQUENCE   288 AA;  31534 MW;  29DCF385A54E1A9F CRC64;
     MAPIKIGING FGRIGRLVAR VALQRDDVEL VAVNDPFIST DYMTYMFKYD SVHGAWKHHE
     LKVKDEKTLL FGEKPVAVFG CRNPEEIPWA STGAEYIVES TGVFTDKDKA AAHLKVINDR
     FGIVEGLMTT VHSITATQKT VDGPSAKDWR GGRAASFNII PSSTGAAKAV GKVLPQLNGK
     LTGMSFRVPT VDVSVVDLTV RLEKKATYDQ IKAAIKEESE GKLKGILGYT EDDVVSTDFV
     GDSRSSIFDA KAGIALNDNF VKLVSWYDNE WGYSTRVVDL IVHMASVQ
//
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