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SCRK7_ARATH
ID   SCRK7_ARATH             Reviewed;         343 AA.
AC   Q9FLH8;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=Probable fructokinase-7;
DE            EC=2.7.1.4;
GN   OrderedLocusNames=At5g51830 {ECO:0000312|Araport:AT5G51830};
GN   ORFNames=MIO24.3 {ECO:0000312|EMBL:BAB11252.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA   Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT   features of the regions of 1,456,315 bp covered by nineteen physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:41-54(1998).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC   -!- FUNCTION: May play an important role in maintaining the flux of carbon
CC       towards starch formation. {ECO:0000250|UniProtKB:Q6XZ79}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-fructose = ADP + D-fructose 6-phosphate + H(+);
CC         Xref=Rhea:RHEA:16125, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:37721, ChEBI:CHEBI:61527, ChEBI:CHEBI:456216; EC=2.7.1.4;
CC   -!- PATHWAY: Glycan biosynthesis; starch biosynthesis.
CC   -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC       {ECO:0000255|RuleBase:RU003704}.
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DR   EMBL; AB010074; BAB11252.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED96132.1; -; Genomic_DNA.
DR   EMBL; CP002688; ANM70527.1; -; Genomic_DNA.
DR   EMBL; AF370289; AAK44104.1; -; mRNA.
DR   EMBL; AY063037; AAL34211.1; -; mRNA.
DR   RefSeq; NP_001318782.1; NM_001344963.1.
DR   RefSeq; NP_199996.1; NM_124562.3.
DR   AlphaFoldDB; Q9FLH8; -.
DR   SMR; Q9FLH8; -.
DR   STRING; 3702.AT5G51830.1; -.
DR   iPTMnet; Q9FLH8; -.
DR   MetOSite; Q9FLH8; -.
DR   PaxDb; Q9FLH8; -.
DR   PRIDE; Q9FLH8; -.
DR   ProteomicsDB; 232921; -.
DR   EnsemblPlants; AT5G51830.1; AT5G51830.1; AT5G51830.
DR   EnsemblPlants; AT5G51830.2; AT5G51830.2; AT5G51830.
DR   GeneID; 835258; -.
DR   Gramene; AT5G51830.1; AT5G51830.1; AT5G51830.
DR   Gramene; AT5G51830.2; AT5G51830.2; AT5G51830.
DR   KEGG; ath:AT5G51830; -.
DR   Araport; AT5G51830; -.
DR   TAIR; locus:2165361; AT5G51830.
DR   eggNOG; KOG2855; Eukaryota.
DR   HOGENOM; CLU_027634_6_1_1; -.
DR   InParanoid; Q9FLH8; -.
DR   OMA; YIFYKDH; -.
DR   OrthoDB; 918144at2759; -.
DR   PhylomeDB; Q9FLH8; -.
DR   BioCyc; ARA:AT5G51830-MON; -.
DR   BRENDA; 2.7.1.4; 399.
DR   UniPathway; UPA00152; -.
DR   PRO; PR:Q9FLH8; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FLH8; baseline and differential.
DR   Genevisible; Q9FLH8; AT.
DR   GO; GO:0005829; C:cytosol; IDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008865; F:fructokinase activity; IDA:TAIR.
DR   GO; GO:0016051; P:carbohydrate biosynthetic process; IGI:TAIR.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IGI:TAIR.
DR   GO; GO:0006000; P:fructose metabolic process; IDA:TAIR.
DR   GO; GO:0019252; P:starch biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.1190.20; -; 1.
DR   InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS.
DR   InterPro; IPR011611; PfkB_dom.
DR   InterPro; IPR002139; Ribo/fructo_kinase.
DR   InterPro; IPR029056; Ribokinase-like.
DR   Pfam; PF00294; PfkB; 1.
DR   PRINTS; PR00990; RIBOKINASE.
DR   SUPFAM; SSF53613; SSF53613; 1.
DR   PROSITE; PS00583; PFKB_KINASES_1; 1.
DR   PROSITE; PS00584; PFKB_KINASES_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Carbohydrate metabolism; Kinase;
KW   Nucleotide-binding; Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   CHAIN           2..343
FT                   /note="Probable fructokinase-7"
FT                   /id="PRO_0000430867"
FT   MOD_RES         2
FT                   /note="N-acetylglycine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
SQ   SEQUENCE   343 AA;  37028 MW;  5CCD5320725E6396 CRC64;
     MGEDAISGNL KNLTIDTRDS ETLVVCFGEM LIDFVPTVGG VSLAEAPAFK KAPGGAPANV
     AVGVSRLGGS SAFIGKVGDD EFGRMLADIL RLNNVDNSGM RFDHNARTAL AFVTLRGDGE
     REFLFFRHPS ADMLLLESEL DKNLIQKAKI FHYGSISLIE EPCRSTQLVA MKIAKAAGSL
     LSYDPNLRLP LWPSEEAARK EIMSIWNLAD VIKISEDEIT FLTGGDDPYD DDVVLQKLFH
     PNLKLLVVSE GPNGCRYYTQ EFKGRVGGVK VKPVDTTGAG DAFVSGLLNS LASDLTLLKD
     EKKLREALLF ANACGAITVT ERGAIPAMPS MDAVQDLLSS TRS
 
 
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