SUR1_ARATH
ID SUR1_ARATH Reviewed; 462 AA.
AC Q9SIV0; F4IVH1; Q940P9;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=S-alkyl-thiohydroximate lyase SUR1;
DE EC=4.4.1.-;
DE AltName: Full=Protein ABERRANT LATERAL ROOT FORMATION 1;
DE AltName: Full=Protein HOOKLESS 3;
DE AltName: Full=Protein ROOTY;
DE AltName: Full=Protein ROOTY 1;
DE AltName: Full=Protein SUPERROOT 1;
GN Name=SUR1; Synonyms=ALF1, HLS3, RTY, RTY1; OrderedLocusNames=At2g20610;
GN ORFNames=F23N11.7;
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] (ISOFORM 1).
RA Gopalraj M., Olszewski N.E.;
RT "The ROOTY/SUPERROOT1 gene of Arabidopsis encodes a putative tyrosine
RT aminotransferase.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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] (ISOFORM 1).
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 [LARGE SCALE MRNA] (ISOFORM 2).
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 [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=7657165; DOI=10.1101/gad.9.17.2131;
RA Celenza J.L. Jr., Grisafi P.L., Fink G.R.;
RT "A pathway for lateral root formation in Arabidopsis thaliana.";
RL Genes Dev. 9:2131-2142(1995).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=8589625; DOI=10.2307/3870131;
RA Boerjan W., Cervera M.T., Delarue M., Beeckman T., Dewitte W., Bellini C.,
RA Caboche M., Van Onckelen H., Van Montagu M., Inze D.;
RT "Superroot, a recessive mutation in Arabidopsis, confers auxin
RT overproduction.";
RL Plant Cell 7:1405-1419(1995).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=12242367; DOI=10.2307/3870148;
RA King J.J., Stimart D.P., Fisher R.H., Bleecker A.B.;
RT "A mutation altering auxin homeostasis and plant morphology in
RT Arabidopsis.";
RL Plant Cell 7:2023-2037(1995).
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=8612271; DOI=10.1016/s0092-8674(00)81095-8;
RA Lehman A., Black R., Ecker J.R.;
RT "HOOKLESS1, an ethylene response gene, is required for differential cell
RT elongation in the Arabidopsis hypocotyl.";
RL Cell 85:183-194(1996).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=14871316; DOI=10.1111/j.1365-313x.2004.02002.x;
RA Mikkelsen M.D., Naur P., Halkier B.A.;
RT "Arabidopsis mutants in the C-S lyase of glucosinolate biosynthesis
RT establish a critical role for indole-3-acetaldoxime in auxin homeostasis.";
RL Plant J. 37:770-777(2004).
CC -!- FUNCTION: C-S lyase involved in glucosinolate biosynthesis. Converts S-
CC (alkylacetohydroximoyl)-L-cysteine to thiohydroximate. Functions in
CC auxin homeostasis. Probably required for glucosinolate activation in
CC response to pathogens. {ECO:0000269|PubMed:14871316}.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:14871316};
CC -!- INTERACTION:
CC Q9SIV0; F4K773: At5g37478; NbExp=3; IntAct=EBI-25518528, EBI-25518517;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9SIV0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SIV0-2; Sequence=VSP_041760, VSP_041761;
CC -!- DISRUPTION PHENOTYPE: Hyperproliferation of lateral roots. Small and
CC epinastic cotyledons and true leaves. Rare floral organs and sterile
CC flowers. High levels of endogenous free and conjugated auxin.
CC {ECO:0000269|PubMed:12242367, ECO:0000269|PubMed:7657165,
CC ECO:0000269|PubMed:8589625, ECO:0000269|PubMed:8612271}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AF301898; AAG37061.1; -; mRNA.
DR EMBL; AC007048; AAD21706.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07041.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07042.1; -; Genomic_DNA.
DR EMBL; AY050987; AAK93664.1; -; mRNA.
DR EMBL; AY054204; AAL06865.1; -; mRNA.
DR EMBL; AY091293; AAM14232.1; -; mRNA.
DR EMBL; BX820228; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; C84591; C84591.
DR RefSeq; NP_179650.1; NM_127622.4. [Q9SIV0-1]
DR RefSeq; NP_973489.1; NM_201760.2. [Q9SIV0-2]
DR AlphaFoldDB; Q9SIV0; -.
DR SMR; Q9SIV0; -.
DR BioGRID; 1938; 1.
DR IntAct; Q9SIV0; 1.
DR STRING; 3702.AT2G20610.1; -.
DR PaxDb; Q9SIV0; -.
DR PRIDE; Q9SIV0; -.
DR ProteomicsDB; 226767; -. [Q9SIV0-1]
DR EnsemblPlants; AT2G20610.1; AT2G20610.1; AT2G20610. [Q9SIV0-1]
DR EnsemblPlants; AT2G20610.2; AT2G20610.2; AT2G20610. [Q9SIV0-2]
DR GeneID; 816585; -.
DR Gramene; AT2G20610.1; AT2G20610.1; AT2G20610. [Q9SIV0-1]
DR Gramene; AT2G20610.2; AT2G20610.2; AT2G20610. [Q9SIV0-2]
DR KEGG; ath:AT2G20610; -.
DR Araport; AT2G20610; -.
DR TAIR; locus:2046056; AT2G20610.
DR eggNOG; KOG0259; Eukaryota.
DR HOGENOM; CLU_017584_4_2_1; -.
DR InParanoid; Q9SIV0; -.
DR OMA; AKENDNW; -.
DR OrthoDB; 734452at2759; -.
DR PhylomeDB; Q9SIV0; -.
DR BioCyc; ARA:AT2G20610-MON; -.
DR BioCyc; MetaCyc:AT2G20610-MON; -.
DR PRO; PR:Q9SIV0; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SIV0; baseline and differential.
DR Genevisible; Q9SIV0; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0016846; F:carbon-sulfur lyase activity; IDA:TAIR.
DR GO; GO:0004838; F:L-tyrosine:2-oxoglutarate aminotransferase activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0080108; F:S-alkylthiohydroximate lyase activity; IMP:TAIR.
DR GO; GO:0048830; P:adventitious root development; TAS:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IDA:TAIR.
DR GO; GO:0019761; P:glucosinolate biosynthetic process; IMP:TAIR.
DR GO; GO:0009684; P:indoleacetic acid biosynthetic process; IMP:TAIR.
DR GO; GO:0001560; P:regulation of cell growth by extracellular stimulus; IMP:TAIR.
DR GO; GO:0006572; P:tyrosine catabolic process; IBA:GO_Central.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR005958; TyrNic_aminoTrfase.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR PIRSF; PIRSF000517; Tyr_transaminase; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01265; tyr_nico_aTase; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Growth regulation; Lyase; Pyridoxal phosphate;
KW Reference proteome.
FT CHAIN 1..462
FT /note="S-alkyl-thiohydroximate lyase SUR1"
FT /id="PRO_0000412723"
FT VAR_SEQ 406..436
FT /note="DALGLKNWMRITIGVEAHMLEDALERLKGFC -> KIMKLSSMSLDLSFDTK
FT MGFVGNVLQGMLWV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_041760"
FT VAR_SEQ 437..462
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_041761"
FT CONFLICT 66
FT /note="K -> E (in Ref. 5; BX820228)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="K -> R (in Ref. 5; BX820228)"
FT /evidence="ECO:0000305"
FT CONFLICT 414
FT /note="M -> V (in Ref. 4; AAL06865)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 462 AA; 51088 MW; 72D110A444E892EB CRC64;
MSEEQPHANL AVPAFKTEKE PITQTRNGQS SVWRFGGSDK AAKASTVTLR GVIYMLFDNC
GKDVNKTILP LGHGDPSVYP CFRTCIEAED AVVDVLRSGK GNSYGPGAGI LPARRAVADY
MNRDLPHKLT PEDIFLTAGC NQGIEIVFES LARPNANILL PRPGFPHYDA RAAYSGLEVR
KFDLLPEKEW EIDLEGIEAI ADENTVAMVV INPNNPCGNV YSHDHLKKVA ETARKLGIMV
ISDEVYDRTI FGDNPFVSMG KFASIVPVLT LAGISKGWVV PGWKIGWIAL NDPEGVFETT
KVLQSIKQNL DVTPDPATII QAALPAILEK ADKNFFAKKN KILKHNVDLV CDRLKDIPCV
VCPKKPESCT YLLTKLELSL MDNIKDDIDF CVKLAREENL VFLPGDALGL KNWMRITIGV
EAHMLEDALE RLKGFCTRHA KKTETETESL QALKLSDNNL EM
