SETH3_ARATH
ID SETH3_ARATH Reviewed; 350 AA.
AC Q9M1T1;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Probable arabinose 5-phosphate isomerase;
DE Short=API;
DE EC=5.3.1.13;
DE AltName: Full=CBS domain-containing protein CBSSIS1;
GN Name=SETH3; Synonyms=CBSSIS1; OrderedLocusNames=At3g54690;
GN ORFNames=T5N23_50;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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;
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 [4]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19400948; DOI=10.1186/1471-2164-10-200;
RA Kushwaha H.R., Singh A.K., Sopory S.K., Singla-Pareek S.L., Pareek A.;
RT "Genome wide expression analysis of CBS domain containing proteins in
RT Arabidopsis thaliana (L.) Heynh and Oryza sativa L. reveals their
RT developmental and stress regulation.";
RL BMC Genomics 10:200-200(2009).
CC -!- FUNCTION: Catalyzes the reversible aldol-ketol isomerization between D-
CC ribulose 5-phosphate (Ru5P) and D-arabinose 5-phosphate (A5P).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-arabinose 5-phosphate = D-ribulose 5-phosphate;
CC Xref=Rhea:RHEA:23104, ChEBI:CHEBI:57693, ChEBI:CHEBI:58121;
CC EC=5.3.1.13;
CC -!- SIMILARITY: Belongs to the SIS family. GutQ/KpsF subfamily.
CC {ECO:0000305}.
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DR EMBL; AL138650; CAB77589.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79267.1; -; Genomic_DNA.
DR EMBL; AK227009; BAE99073.1; -; mRNA.
DR PIR; T47628; T47628.
DR RefSeq; NP_191029.1; NM_115326.5.
DR AlphaFoldDB; Q9M1T1; -.
DR SMR; Q9M1T1; -.
DR STRING; 3702.AT3G54690.1; -.
DR PaxDb; Q9M1T1; -.
DR PRIDE; Q9M1T1; -.
DR ProteomicsDB; 232831; -.
DR EnsemblPlants; AT3G54690.1; AT3G54690.1; AT3G54690.
DR GeneID; 824634; -.
DR Gramene; AT3G54690.1; AT3G54690.1; AT3G54690.
DR KEGG; ath:AT3G54690; -.
DR Araport; AT3G54690; -.
DR TAIR; locus:2102440; AT3G54690.
DR eggNOG; ENOG502RDRP; Eukaryota.
DR HOGENOM; CLU_040681_13_2_1; -.
DR InParanoid; Q9M1T1; -.
DR OMA; LMACLMR; -.
DR OrthoDB; 1167854at2759; -.
DR PhylomeDB; Q9M1T1; -.
DR BioCyc; ARA:AT3G54690-MON; -.
DR BioCyc; MetaCyc:AT3G54690-MON; -.
DR PRO; PR:Q9M1T1; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M1T1; baseline and differential.
DR Genevisible; Q9M1T1; AT.
DR GO; GO:0019146; F:arabinose-5-phosphate isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:1901135; P:carbohydrate derivative metabolic process; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd05014; SIS_Kpsf; 1.
DR Gene3D; 3.10.580.10; -; 1.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR004800; KdsD/KpsF-type.
DR InterPro; IPR001347; SIS_dom.
DR InterPro; IPR046348; SIS_dom_sf.
DR InterPro; IPR035474; SIS_Kpsf.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF01380; SIS; 1.
DR PIRSF; PIRSF004692; KdsD_KpsF; 1.
DR SMART; SM00116; CBS; 2.
DR SUPFAM; SSF53697; SSF53697; 1.
DR TIGRFAMs; TIGR00393; kpsF; 1.
DR PROSITE; PS51371; CBS; 2.
DR PROSITE; PS51464; SIS; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; CBS domain; Isomerase; Lipopolysaccharide biosynthesis;
KW Nucleotide-binding; Reference proteome; Repeat.
FT CHAIN 1..350
FT /note="Probable arabinose 5-phosphate isomerase"
FT /id="PRO_0000412226"
FT DOMAIN 60..203
FT /note="SIS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT DOMAIN 229..288
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 297..350
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT BINDING 75..80
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 94..95
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 133..142
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 167..169
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 295
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 78
FT /note="Catalytically relevant"
FT /evidence="ECO:0000250"
FT SITE 130
FT /note="Catalytically relevant"
FT /evidence="ECO:0000250"
FT SITE 171
FT /note="Catalytically relevant"
FT /evidence="ECO:0000250"
FT SITE 212
FT /note="Catalytically relevant"
FT /evidence="ECO:0000250"
SQ SEQUENCE 350 AA; 37749 MW; 6926AA514F33E2A3 CRC64;
MGSLPPPSLD FSSIDHNSLK NGGSSHQEIS HDNLLNLFKS QQDLLNHFFK HLDLSQTLDF
SRILLSTTGT VFFTGVGKSA FVANKVSQTL VSLSFRSSFL SPLDALHGDI GALSPRDVLV
FFSKSGATEE LLRLVPCARA KGAFLVSLTS VSGNPLAGVC DMNVHLPLQR ELCPFNLAPV
TSTAIQMVFG DTIAVALMAA RNLSKEEYAA NHPAGRIGKS LIFKVKDVMK KQEELPVCKE
GDLIMDQLVE LTSKGCGCLL VVDEHSRLIG TFTDGDLRRT LKASGEAIFK LSVGEMCNRK
PRTIGPETMA VEAMKKMESP PSPVQFLPVV NEDNTLIGIV TLHGLVSAGL
