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 24-JAN-2024, entry version 149.
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.O23461; -.
DR iPTMnet; O23461; -.
DR PaxDb; 3702-AT4G16130-1; -.
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; AT4G16130; ARA1.
DR eggNOG; KOG0631; Eukaryota.
DR HOGENOM; CLU_012602_0_0_1; -.
DR InParanoid; O23461; -.
DR OMA; FFDWEEE; -.
DR OrthoDB; 5491727at2759; -.
DR PhylomeDB; O23461; -.
DR BioCyc; ARA:AT4G16130-MONOMER; -.
DR BioCyc; MetaCyc:AT4G16130-MONOMER; -.
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:0016020; C:membrane; IEA:UniProtKB-SubCell.
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 Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.890; GHMP kinase, C-terminal domain; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1.
DR InterPro; IPR012369; Galk_glycosyltransferase.
DR InterPro; IPR019539; GalKase_N.
DR InterPro; IPR036554; GHMP_kinase_C_sf.
DR InterPro; IPR006204; GHMP_kinase_N_dom.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR PANTHER; PTHR38134:SF2; GALACTOKINASE; 1.
DR PANTHER; PTHR38134; SLR1395 PROTEIN; 1.
DR Pfam; PF10509; GalKase_gal_bdg; 1.
DR Pfam; PF00288; GHMP_kinases_N; 1.
DR PIRSF; PIRSF036399; Gal_kin_glcsltr; 1.
DR PRINTS; PR00959; MEVGALKINASE.
DR SUPFAM; SSF55060; GHMP Kinase, C-terminal domain; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 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
//
