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GLPK_ARATH
ID   GLPK_ARATH              Reviewed;         522 AA.
AC   Q9M8L4; A0JPS9;
DT   01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Glycerol kinase;
DE            Short=Glycerokinase;
DE            EC=2.7.1.30;
DE   AltName: Full=ATP:glycerol 3-phosphotransferase;
DE   AltName: Full=Protein GLYCEROL INSENSITIVE 1;
DE   AltName: Full=Protein NONHOST RESISTANCE TO P. S. PHASEOLICOLA 1;
GN   Name=GLPK; Synonyms=GLI1, NHO1; OrderedLocusNames=At1g80460;
GN   ORFNames=T21F11.21;
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 [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=14756771; DOI=10.1111/j.1365-313x.2003.01989.x;
RA   Eastmond P.J.;
RT   "Glycerol-insensitive Arabidopsis mutants: gli1 seedlings lack glycerol
RT   kinase, accumulate glycerol and are more resistant to abiotic stress.";
RL   Plant J. 37:617-625(2004).
RN   [2]
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA   Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA   Shinozaki K.;
RT   "Analysis of multiple occurrences of alternative splicing events in
RT   Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL   DNA Res. 16:155-164(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT   "Arabidopsis ORF Clones.";
RL   Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   FUNCTION.
RX   PubMed=11226196; DOI=10.2307/3871287;
RA   Lu M., Tang X., Zhou J.M.;
RT   "Arabidopsis NHO1 is required for general resistance against Pseudomonas
RT   bacteria.";
RL   Plant Cell 13:437-447(2001).
RN   [7]
RP   FUNCTION, AND INDUCTION BY PATHOGEN.
RX   PubMed=12626746; DOI=10.1073/pnas.0637377100;
RA   Kang L., Li J., Zhao T., Xiao F., Tang X., Thilmony R., He S., Zhou J.M.;
RT   "Interplay of the Arabidopsis nonhost resistance gene NHO1 with bacterial
RT   virulence.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:3519-3524(2003).
RN   [8]
RP   INDUCTION BY FLAGELLIN.
RX   PubMed=16123135; DOI=10.1073/pnas.0502425102;
RA   Li X., Lin H., Zhang W., Zou Y., Zhang J., Tang X., Zhou J.M.;
RT   "Flagellin induces innate immunity in nonhost interactions that is
RT   suppressed by Pseudomonas syringae effectors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:12990-12995(2005).
RN   [9]
RP   INDUCTION BY PATHOGEN.
RX   PubMed=22286136; DOI=10.1105/tpc.111.093245;
RA   Rojas C.M., Senthil-Kumar M., Wang K., Ryu C.M., Kaundal A., Mysore K.S.;
RT   "Glycolate oxidase modulates reactive oxygen species-mediated signal
RT   transduction during nonhost resistance in Nicotiana benthamiana and
RT   Arabidopsis.";
RL   Plant Cell 24:336-352(2012).
CC   -!- FUNCTION: Key enzyme in the regulation of glycerol uptake and
CC       metabolism. Required for resistance to nonhost Pseudomonas bacteria and
CC       to the pathogenic fungus B.cinerea. {ECO:0000269|PubMed:11226196,
CC       ECO:0000269|PubMed:12626746, ECO:0000269|PubMed:14756771}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + glycerol = ADP + H(+) + sn-glycerol 3-phosphate;
CC         Xref=Rhea:RHEA:21644, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:57597, ChEBI:CHEBI:456216;
CC         EC=2.7.1.30; Evidence={ECO:0000269|PubMed:14756771};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=58 uM for glycerol {ECO:0000269|PubMed:14756771};
CC         KM=268 uM for ATP {ECO:0000269|PubMed:14756771};
CC   -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase
CC       pathway; sn-glycerol 3-phosphate from glycerol: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q9M8L4-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Highly expressed in germinating seeds and senescent
CC       leaves, and at lower levels in roots, leaves, flowers and siliques.
CC       {ECO:0000269|PubMed:14756771}.
CC   -!- INDUCTION: By the bacterial pathogens P.syringae pv. phaseolicola, pv.
CC       syringae, pv. tomato and pv. tabaci, and flagellin.
CC       {ECO:0000269|PubMed:12626746, ECO:0000269|PubMed:16123135,
CC       ECO:0000269|PubMed:22286136}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC       conditons, but mutant plants accumulate high levels of glycerol, can
CC       grow on synthetic medium containing glycerol and have increased
CC       resistance to salt, cold, osmotic and drought stresses.
CC       {ECO:0000269|PubMed:14756771}.
CC   -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000305}.
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DR   EMBL; AY234854; AAO61418.1; -; mRNA.
DR   EMBL; AC018849; AAF27123.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE36407.1; -; Genomic_DNA.
DR   EMBL; AK316784; BAH19502.1; -; mRNA.
DR   EMBL; BT029299; ABK32113.1; -; mRNA.
DR   PIR; D96836; D96836.
DR   RefSeq; NP_178161.1; NM_106694.4. [Q9M8L4-1]
DR   AlphaFoldDB; Q9M8L4; -.
DR   SMR; Q9M8L4; -.
DR   BioGRID; 29603; 1.
DR   STRING; 3702.AT1G80460.1; -.
DR   PaxDb; Q9M8L4; -.
DR   PRIDE; Q9M8L4; -.
DR   ProteomicsDB; 248588; -. [Q9M8L4-1]
DR   EnsemblPlants; AT1G80460.1; AT1G80460.1; AT1G80460. [Q9M8L4-1]
DR   GeneID; 844385; -.
DR   Gramene; AT1G80460.1; AT1G80460.1; AT1G80460. [Q9M8L4-1]
DR   KEGG; ath:AT1G80460; -.
DR   Araport; AT1G80460; -.
DR   TAIR; locus:2198928; AT1G80460.
DR   eggNOG; KOG2517; Eukaryota.
DR   HOGENOM; CLU_009281_2_3_1; -.
DR   InParanoid; Q9M8L4; -.
DR   OMA; MLPTIHS; -.
DR   PhylomeDB; Q9M8L4; -.
DR   BioCyc; ARA:AT1G80460-MON; -.
DR   SABIO-RK; Q9M8L4; -.
DR   UniPathway; UPA00618; UER00672.
DR   PRO; PR:Q9M8L4; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9M8L4; baseline and differential.
DR   Genevisible; Q9M8L4; AT.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004370; F:glycerol kinase activity; IDA:TAIR.
DR   GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IBA:GO_Central.
DR   GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR   GO; GO:0019563; P:glycerol catabolic process; IMP:TAIR.
DR   GO; GO:0006071; P:glycerol metabolic process; IBA:GO_Central.
DR   GO; GO:0046167; P:glycerol-3-phosphate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IBA:GO_Central.
DR   GO; GO:0009617; P:response to bacterium; IEP:TAIR.
DR   GO; GO:0010188; P:response to microbial phytotoxin; IEP:TAIR.
DR   GO; GO:0002237; P:response to molecule of bacterial origin; IEP:TAIR.
DR   GO; GO:0006641; P:triglyceride metabolic process; IBA:GO_Central.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR000577; Carb_kinase_FGGY.
DR   InterPro; IPR018485; Carb_kinase_FGGY_C.
DR   InterPro; IPR018483; Carb_kinase_FGGY_CS.
DR   InterPro; IPR018484; Carb_kinase_FGGY_N.
DR   InterPro; IPR005999; Glycerol_kin.
DR   Pfam; PF02782; FGGY_C; 1.
DR   Pfam; PF00370; FGGY_N; 1.
DR   PIRSF; PIRSF000538; GlpK; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   TIGRFAMs; TIGR01311; glycerol_kin; 1.
DR   PROSITE; PS00933; FGGY_KINASES_1; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cytoplasm; Glycerol metabolism; Kinase;
KW   Nucleotide-binding; Plant defense; Reference proteome; Transferase.
FT   CHAIN           1..522
FT                   /note="Glycerol kinase"
FT                   /id="PRO_0000422109"
FT   BINDING         15
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         19
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         89..90
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         143
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         255..256
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         276
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         321
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         430..434
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        467
FT                   /note="G -> R (in Ref. 5; ABK32113)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   522 AA;  56437 MW;  7470EE0F3F9EE4B1 CRC64;
     MAKENGFIGS IDQGTTSTRF IIYDHDARPV ASHQVEFTQF YPEAGWVEHD PMEILESVKV
     CIAKALDKAT ADGHNVDGGL KAIGLTDQRE TTVVWSKSTG LPLHKAIVWM DARTSSICRR
     LEKELSGGRS HFVESCGLPI STYFSAMKLL WLMENVDDVK DAIKKGDAIF GTIDTWLIWN
     MTGGINGGLH VTDVTNASRT MLMNLKTLSW DQDTLKTLGI PAEILPKIVS NSEVIGEICK
     GWPIPGIKIA GCLGDQHAAM LGQACRKGEA KSTYGTGAFI LLNTGEVPIK SGHGLLTTLA
     YKLGPQAQTN YALEGSIAIA GAAVQWLRDS LGIIKSASEI EDLAAMVDST GGVYFVPAFN
     GLFAPWWRED ARGVCIGITR FTNKSHIARA VLESMCFQVK DVLDSMNKDA GEKGSLNNGK
     GEFLLRVDGG ATANNLLMQI QADLMGSPVV RPVDIETTAL GAAYAAGLAV GFWKEADIFE
     SGEKAKNSKV FRPAMEEGIR KKKVASWCKA VERTFDLADL SI
 
 
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