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Database: UniProt
Entry: D7TDL2_VITVI
LinkDB: D7TDL2_VITVI
Original site: D7TDL2_VITVI 
ID   D7TDL2_VITVI            Unreviewed;      1470 AA.
AC   D7TDL2;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   RecName: Full=Pyruvate phosphate dikinase AMP/ATP-binding domain-containing protein {ECO:0000259|Pfam:PF01326};
GN   OrderedLocusNames=VIT_01s0127g00060 {ECO:0000313|EMBL:CBI28585.3};
OS   Vitis vinifera (Grape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; Vitales; Vitaceae; Viteae; Vitis.
OX   NCBI_TaxID=29760 {ECO:0000313|EMBL:CBI28585.3, ECO:0000313|Proteomes:UP000009183};
RN   [1] {ECO:0000313|Proteomes:UP000009183}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX   PubMed=17721507; DOI=10.1038/nature06148;
RG   The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA   Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA   Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA   Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA   Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA   Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA   Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA   Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA   Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA   Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA   Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA   Wincker P.;
RT   "The grapevine genome sequence suggests ancestral hexaploidization in major
RT   angiosperm phyla.";
RL   Nature 449:463-467(2007).
CC   -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007837}.
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DR   EMBL; FN595761; CBI28585.3; -; Genomic_DNA.
DR   RefSeq; XP_002270485.1; XM_002270449.3.
DR   STRING; 29760.D7TDL2; -.
DR   PaxDb; 29760-VIT_01s0127g00060-t01; -.
DR   EnsemblPlants; Vitvi01g00681_t002; Vitvi01g00681_P002; Vitvi01g00681.
DR   GeneID; 100246568; -.
DR   Gramene; Vitvi01g00681_t002; Vitvi01g00681_P002; Vitvi01g00681.
DR   KEGG; vvi:100246568; -.
DR   eggNOG; ENOG502QQ6R; Eukaryota.
DR   HOGENOM; CLU_002399_1_0_1; -.
DR   InParanoid; D7TDL2; -.
DR   OMA; IFVWIRF; -.
DR   OrthoDB; 295737at2759; -.
DR   BRENDA; 2.7.9.4; 6671.
DR   Proteomes; UP000009183; Chromosome 1.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016301; F:kinase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR002192; PPDK_AMP/ATP-bd.
DR   PANTHER; PTHR46999:SF1; ALPHA-GLUCAN WATER DIKINASE 1, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR46999; ALPHA-GLUCAN WATER DIKINASE 1, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF01326; PPDK_N; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000009183}.
FT   DOMAIN          1268..1469
FT                   /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01326"
SQ   SEQUENCE   1470 AA;  164586 MW;  EC0CC3841DDAC52A CRC64;
     MSNTIGHNLL HKSLLRHTLL EHQSKISCSG VSGNALFQAQ SPTQIKKSPI STKFRGNRLN
     LRKTKLPMGT HHLVSVIPRA VLTTDTTSEL AGKFCLDKNI ELQVDVSVPT PGSMVQVNIQ
     VTNCSNSLLL HWGAIRDTKG KWVLPSHSPD GTKVYKNKAL RTPFVKSGSK SILKIEVDDP
     AIQAIEFLIV DETQNKWFKN NGENFSVKLP VKGKMIPNAS VPEELVQIQA YLRWERKGKQ
     MYTPEQEKEE YEAARTELVE EIARGTSIED MRTRLTNESA KSEIKEQPHS ETKSKIPDEL
     VQVQAYIRWE KAGKPNYTPD QQLREFEEAR KDLQTELEKG LSLDEIRKKM IKGEIQVKVS
     KQQKSRRYFG VERIQRKKRD LMQLLHRHVT EWTEEKTPIP IKKTELTAVE QFAKLKEEQD
     SGSVLNKKIY KISDKELLVL VTKPAGKTKV YFATDSKEPL TLHWAVSKKA GEWLAPPPSV
     LPLDSISLNG AVQTQFVNSS SADPAYEVQT LKIEIEEDSF VGMPFVLLSQ GNWIKNGGSD
     FYIEFRVGPK QVKKDAGDGK GTAKALLDKI AEKESEAQKS FMHRFNIAAD LMDQAISAGK
     LGLAGIVVWM RFMATRQLVW NKNYNIKPRE ISKAQDRLTD LLQNSYKTHP QYRELLRMIM
     STVGRGGEGD VGQRIRDEIL VLQRNNDCKG AMMEEWHQKL HNNTSPDDVI ICQALIDYIK
     CDFDISAYWK TLNENGITKE RLLSYDRGIH SEPNFRKDQK DGLLRDLGKY MRTLKAVHSG
     ADLESAISNC MGYRSEGQGF MVGVKINPIP GLPSGFPELL QFVLEHVEDK NVEPLLEGLL
     EARQELQSLL IKSHDRLKDL LFLDIALDST VRTAIERGYE ELNNAGAEKI MYFITLVLEN
     LVLSSDDNED LIYCLKGWNH ALGMSKSRDG HWALYAKSVL DRTRLALTSK AEEYHQVLQP
     SAEYLGSLLG VDQWAVNIFT EEIIRAGSAA SLSSLLNRLD PVLRKTANLG SWQVISPVEA
     VGRVVVVGEL LTVQNKSYGQ PTILVVKTVK GEEEIPDGAV AVLTPDMPDV LSHVSVRARN
     GKVCFATCFD PKILADLQAN EGKLLHLKPT SADIVYSAVK EGELTDSIST KSKDNDSLPS
     VSLVRKQFGG RYAISSEEFT SEMVGAKSRN ISYLKGKVPL WVQIPTSVAL PFGVFEKVLS
     DGLNKEVSEK LRSLKGGLGK GNFAVLTEIR KTVLQLSAPS QLVQELKDKM KSSGMPWPGD
     EGEQRWEQAW MAIKKVWASK WNERAYFSTR KVKLDHDYLC MAVLVQEIIN ADYAFVIHTT
     NPSSGDSSEI YAEVVRGLGE TLVGAYPGRA LSFICKKNDL NSPQVLGYPS KPIGLFITRS
     IIFRSDSNGE DLEGYAGAGL YDSVPMDKEE KVVLDYSSDP LMIDGNFRQS ILSSIARAGN
     AIEELYGSPQ DIEGVVRDGK IYVVQTRPQM
//
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