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SCRK6_ARATH
ID   SCRK6_ARATH             Reviewed;         384 AA.
AC   Q9C524; Q8H119; Q94K38;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Probable fructokinase-6, chloroplastic;
DE            EC=2.7.1.4;
DE   Flags: Precursor;
GN   OrderedLocusNames=At1g66430 {ECO:0000312|Araport:AT1G66430};
GN   ORFNames=F28G11.11 {ECO:0000312|EMBL:AAG51160.1},
GN   T27F4.17 {ECO:0000312|EMBL:AAG52172.1};
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=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
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=14993207; DOI=10.1101/gr.1515604;
RA   Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA   Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA   Weissenbach J., Salanoubat M.;
RT   "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT   combined approach to evaluate and improve Arabidopsis genome annotation.";
RL   Genome Res. 14:406-413(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 142-384.
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).
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   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC       {ECO:0000255|RuleBase:RU003704}.
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DR   EMBL; AC020665; AAG52172.1; -; Genomic_DNA.
DR   EMBL; AC074025; AAG51160.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE34508.1; -; Genomic_DNA.
DR   EMBL; BX816698; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AF370329; AAK44144.2; -; mRNA.
DR   EMBL; BT000889; AAN41289.1; -; mRNA.
DR   PIR; G96689; G96689.
DR   RefSeq; NP_564875.2; NM_105314.5.
DR   AlphaFoldDB; Q9C524; -.
DR   SMR; Q9C524; -.
DR   BioGRID; 28182; 1.
DR   IntAct; Q9C524; 2.
DR   STRING; 3702.AT1G66430.1; -.
DR   PaxDb; Q9C524; -.
DR   PRIDE; Q9C524; -.
DR   ProteomicsDB; 232963; -.
DR   EnsemblPlants; AT1G66430.1; AT1G66430.1; AT1G66430.
DR   GeneID; 842961; -.
DR   Gramene; AT1G66430.1; AT1G66430.1; AT1G66430.
DR   KEGG; ath:AT1G66430; -.
DR   Araport; AT1G66430; -.
DR   TAIR; locus:2028987; AT1G66430.
DR   eggNOG; KOG2855; Eukaryota.
DR   HOGENOM; CLU_027634_6_1_1; -.
DR   InParanoid; Q9C524; -.
DR   OMA; NWRPTFW; -.
DR   OrthoDB; 918144at2759; -.
DR   PhylomeDB; Q9C524; -.
DR   BioCyc; ARA:AT1G66430-MON; -.
DR   BRENDA; 2.7.1.4; 399.
DR   UniPathway; UPA00152; -.
DR   PRO; PR:Q9C524; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9C524; baseline and differential.
DR   Genevisible; Q9C524; AT.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   ATP-binding; Carbohydrate metabolism; Chloroplast; Kinase;
KW   Nucleotide-binding; Plastid; Reference proteome; Transferase;
KW   Transit peptide.
FT   TRANSIT         1..46
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           47..384
FT                   /note="Probable fructokinase-6, chloroplastic"
FT                   /id="PRO_0000430866"
FT   REGION          34..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        304
FT                   /note="S -> R (in Ref. 3; BX816698)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   384 AA;  41471 MW;  8873EC5152F65928 CRC64;
     MALQATTTTF CFSGPTFRST PHSLTSKRPI SIKATTSSPS RLSNSRSNLK GRALSSDGST
     QESPYVVCFG EMLIDFVPTT SGLSLADAPA FKKAPGGAPA NVAVGIARLG GSSAFIGKVG
     EDEFGYMLAN ILKDNNVNND GMRFDPGART ALAFVTLTNE GEREFMFYRN PSADMLLEES
     ELDFDLIKKA KIFHYGSISL ITEPCKSAHI SAAKAAKEAG VILSYDPNLR LPLWPSADNA
     REEILSIWET ADIIKISEEE IVFLTKGEDP YDDNVVRKLF HPKLKLLLVT EGPEGCRYYT
     KDFSGRVHGL KVDVVDTTGA GDAFVAGILS QLANDLSLLQ DEERLREALM FANACGALTV
     KVRGAIPALP TKEAVHEALL KAVV
 
 
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