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ARAK_ARATH
ID   ARAK_ARATH              Reviewed;        1039 AA.
AC   O23461; B9DI14; O23723; Q0WLW4;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=L-arabinokinase;
DE            Short=AtISA1;
DE            EC=2.7.1.46;
GN   Name=ARA1; Synonyms=ISA1; OrderedLocusNames=At4g16130;
GN   ORFNames=dl4105w, FCAALL.288;
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=9461215; DOI=10.1038/35140;
RA   Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA   Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA   Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA   Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA   De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA   Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA   Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA   Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA   Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA   Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA   Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA   Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT   "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT   thaliana.";
RL   Nature 391:485-488(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
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=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   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 9-1039.
RX   PubMed=9524266; DOI=10.1016/s0378-1119(98)00049-3;
RA   Gy I., Aubourg S., Sherson S., Cobbett C.S., Cheron A., Kreis M.,
RA   Lecharny A.;
RT   "Analysis of a 14-kb fragment containing a putative cell wall gene and a
RT   candidate for the ARA1, arabinose kinase, gene from chromosome IV of
RT   Arabidopsis thaliana.";
RL   Gene 209:201-210(1998).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 155-1039.
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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 453-1039.
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   FUNCTION, AND MUTAGENESIS OF GLU-705.
RX   PubMed=10344205; DOI=10.1023/a:1006181908753;
RA   Sherson S., Gy I., Medd J., Schmidt R., Dean C., Kreis M., Lecharny A.,
RA   Cobbett C.;
RT   "The arabinose kinase, ARA1, gene of Arabidopsis is a novel member of the
RT   galactose kinase gene family.";
RL   Plant Mol. Biol. 39:1003-1012(1999).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA   Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT   "Multidimensional protein identification technology (MudPIT) analysis of
RT   ubiquitinated proteins in plants.";
RL   Mol. Cell. Proteomics 6:601-610(2007).
CC   -!- FUNCTION: Arabinose kinase. Involved in the salvage pathway which
CC       converts free L-arabinose to UDP-L-arabinose. May play a role in
CC       arabinose transport. {ECO:0000269|PubMed:10344205}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-arabinose = ADP + beta-L-arabinose 1-phosphate + H(+);
CC         Xref=Rhea:RHEA:20153, ChEBI:CHEBI:15378, ChEBI:CHEBI:17535,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:57521, ChEBI:CHEBI:456216;
CC         EC=2.7.1.46;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- MISCELLANEOUS: Sup1, a suppressor of the ara1-1 arabinose-sensitive
CC       phenotype, contains a second point mutation resulting in a premature
CC       stop codon and a complete loss of kinase activity. Therefore, the
CC       putative arabinose transport function is independent from the kinase
CC       activity.
CC   -!- SIMILARITY: Belongs to the GHMP kinase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BT003908; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAA74753.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; Z97340; CAB10392.1; -; Genomic_DNA.
DR   EMBL; AL161543; CAB78655.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE83696.1; -; Genomic_DNA.
DR   EMBL; BT003908; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; Y14404; CAA74753.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AK317724; BAH20381.1; -; mRNA.
DR   EMBL; AK230073; BAF01893.1; -; mRNA.
DR   PIR; F71427; F71427.
DR   RefSeq; NP_193348.1; NM_117706.3.
DR   AlphaFoldDB; O23461; -.
DR   SMR; O23461; -.
DR   BioGRID; 12593; 4.
DR   IntAct; O23461; 3.
DR   STRING; 3702.AT4G16130.1; -.
DR   iPTMnet; O23461; -.
DR   PaxDb; O23461; -.
DR   PRIDE; O23461; -.
DR   ProteomicsDB; 240888; -.
DR   EnsemblPlants; AT4G16130.1; AT4G16130.1; AT4G16130.
DR   GeneID; 827299; -.
DR   Gramene; AT4G16130.1; AT4G16130.1; AT4G16130.
DR   KEGG; ath:AT4G16130; -.
DR   Araport; AT4G16130; -.
DR   TAIR; locus:2130105; AT4G16130.
DR   eggNOG; KOG0631; Eukaryota.
DR   HOGENOM; CLU_012602_0_0_1; -.
DR   InParanoid; O23461; -.
DR   OMA; FFDWEEE; -.
DR   OrthoDB; 106752at2759; -.
DR   PhylomeDB; O23461; -.
DR   BioCyc; ARA:AT4G16130-MON; -.
DR   BioCyc; MetaCyc:AT4G16130-MON; -.
DR   BRENDA; 2.7.1.46; 399.
DR   PRO; PR:O23461; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; O23461; baseline and differential.
DR   Genevisible; O23461; AT.
DR   GO; GO:0005829; C:cytosol; IDA:TAIR.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0009702; F:L-arabinokinase activity; IDA:TAIR.
DR   GO; GO:0019566; P:arabinose metabolic process; IDA:TAIR.
DR   GO; GO:0006012; P:galactose metabolic process; IBA:GO_Central.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.70.890; -; 1.
DR   InterPro; IPR012369; Galk_glycosyltransferase.
DR   InterPro; IPR019539; GalKase_N.
DR   InterPro; IPR013750; GHMP_kinase_C_dom.
DR   InterPro; IPR036554; GHMP_kinase_C_sf.
DR   InterPro; IPR006204; GHMP_kinase_N_dom.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   Pfam; PF10509; GalKase_gal_bdg; 1.
DR   Pfam; PF08544; GHMP_kinases_C; 1.
DR   Pfam; PF00288; GHMP_kinases_N; 1.
DR   PIRSF; PIRSF036399; Gal_kin_glcsltr; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55060; SSF55060; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Carbohydrate metabolism; Kinase; Membrane; Nucleotide-binding;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..1039
FT                   /note="L-arabinokinase"
FT                   /id="PRO_0000407404"
FT   TRANSMEM        662..678
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        745
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         693..703
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   SITE            557
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         705
FT                   /note="E->K: In ara1-1; arabinose sensitivity and loss of
FT                   kinase activity."
FT                   /evidence="ECO:0000269|PubMed:10344205"
FT   CONFLICT        144
FT                   /note="K -> E (in Ref. 4; BT003908)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        585
FT                   /note="V -> A (in Ref. 5; CAA74753)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        681
FT                   /note="E -> G (in Ref. 6; BAH20381)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        890
FT                   /note="Q -> E (in Ref. 5; CAA74753)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        961
FT                   /note="Q -> R (in Ref. 4; BT003908)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1039 AA;  114261 MW;  82843127FCCB66B5 CRC64;
     MSERAKLQKK KKVTEDLLDS LLLLPPWRNF AISQSHQSII ESSSQRLPEK MRIDENEGVS
     ASSKHLVFAY YVTGHGFGHA TRVVEVVRHL IAAGHDVHVV TGAPDFVFTS EIQSPRLKIR
     KVLLDCGAVQ ADALTVDRLA SLEKYVETAV VPRAEILETE VEWLHSIKAD FVVSDVVPVA
     CRAAADAGIR SVCVTNFSWD FIYAEYVMAA GYHHRSIVWQ IAEDYSHCEF LIRLPGYCPM
     PAFRDVIDVP LVVRRLHKSR KEVRKELGIA EDVNVVILNF GGQPSGWNLK ETSLPTGWLC
     LVCGASETLE LPPNFIKLAK DAYTPDIIAA SDCMLGKIGY GTVSEALSYK VPFVFVRRDY
     FNEEPFLRNM LEFYQCGVEM IRRDLLMGQW TPYLERAVSL KPCYEGGING GEIAAHILQE
     TAIGRHCASD KLSGARRLRD AIILGYQLQR VPGRDIAIPE WYSRAENELG QSAGSSPTVQ
     ANENNSLVES CIDDFDILQG DVQGLSDTCT FLKSLAMLDA IHDSEKSTEK KTVRERKAAG
     GLFNWEEEIF VARAPGRLDV MGGIADYSGS LVLQMPIREA CHVAVQRNLP GKHRLWKHAQ
     ARQQAKGQVP TPVLQIVSYG SEISNRAPTF DMDLSDFMDG DEPISYEKAR KFFAQDPAQK
     WAAYVAGTIL VLMIELGVRF EDSISLLVSS AVPEGKGVSS SAAVEVASMS AIAAAHGLSI
     DPRDLAILCQ KVENHIVGAP CGVMDQMTSS CGEANKLLAM ICQPAEVVGL VEIPNHVRFW
     GIDSGIRHSV GGADYRSVRV GAYMGRKMIK SMASSILSPS ASSANGGNPE ELEDEGIDLL
     EAEASLDYLC NLSPHRYEAR YADKLPDIML GQTFIEEYAD HDDPVTVIDQ KRSYSVKAPA
     RHPIYENFRV KTFKALLTSA TSDEQLTALG GLLYQCHYSY SACGLGSDGT NRLVQLVQGM
     QHNKSNSEDG TLYGAKITGG GSGGTVCVVG RNSLRSSQQI LEIQQRYKAA TGYLPLIFEG
     SSPGAGKFGY LRIRRRISL
 
 
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