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Protein

UDP-sulfoquinovose synthase, chloroplastic

Gene

SQD1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the biosynthesis of sulfolipids found in thylakoid membranes. Converts UDP-glucose and sulfite to the sulfolipid head group precursor UDP-sulfoquinovose.1 Publication

Catalytic activityi

UDP-alpha-D-sulfoquinovose + H2O = UDP-alpha-D-glucose + sulfite.

Cofactori

Enzyme regulationi

Concentrations above 100 µM sulfite inhibit the reaction.

Kineticsi

  1. KM=150 µM for UDP-glucose
  2. KM=10 µM for sulfite

    pH dependencei

    Optimum pH is 7.5-9.5.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei184 – 1841NADCombined sources2 Publications
    Binding sitei184 – 1841SubstrateCombined sources2 Publications
    Binding sitei202 – 2021NADCombined sources2 Publications
    Active sitei228 – 2281Combined sources1 Publication
    Binding sitei228 – 2281SubstrateCombined sources1 Publication
    Active sitei265 – 2651Proton acceptorCombined sources1 Publication
    Binding sitei265 – 2651NADCombined sources2 Publications
    Binding sitei265 – 2651SubstrateCombined sources2 Publications
    Active sitei269 – 2691Combined sources1 Publication
    Binding sitei269 – 2691NADCombined sources2 Publications
    Binding sitei292 – 2921SubstrateCombined sources1 Publication
    Binding sitei295 – 2951NAD; via amide nitrogenCombined sources2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi95 – 962NADCombined sources2 Publications
    Nucleotide bindingi115 – 1195NADCombined sources2 Publications
    Nucleotide bindingi158 – 1592NADCombined sources2 Publications

    GO - Molecular functioni

    • coenzyme binding Source: InterPro
    • sulfotransferase activity Source: TAIR
    • UDPsulfoquinovose synthase activity Source: UniProtKB-EC
    • zinc ion binding Source: TAIR

    GO - Biological processi

    • cellular response to phosphate starvation Source: TAIR
    • glycolipid biosynthetic process Source: TAIR
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-1201.
    RETL1328306-WGS:GSTH-3531-MONOMER.
    BRENDAi3.13.1.1. 399.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    UDP-sulfoquinovose synthase, chloroplastic (EC:3.13.1.1)
    Alternative name(s):
    Sulfite:UDP-glucose sulfotransferase
    Sulfolipid biosynthesis protein
    Gene namesi
    Name:SQD1
    Ordered Locus Names:At4g33030
    ORF Names:F26P21.150
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    Proteomesi
    • UP000006548 Componenti: Chromosome 4

    Organism-specific databases

    TAIRiAT4G33030.

    Subcellular locationi

    GO - Cellular componenti

    • chloroplast Source: TAIR
    Complete GO annotation...

    Keywords - Cellular componenti

    Chloroplast, Plastid

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi228 – 2281T → A: Loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 8686ChloroplastCuratedAdd
    BLAST
    Chaini87 – 477391UDP-sulfoquinovose synthase, chloroplasticPRO_0000010469Add
    BLAST

    Proteomic databases

    PaxDbiO48917.
    PRIDEiO48917.

    Expressioni

    Inductioni

    Induced in response to altered availability of inorganic phosphate.2 Publications

    Gene expression databases

    GenevisibleiO48917. AT.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi14725. 1 interaction.
    IntActiO48917. 1 interaction.
    STRINGi3702.AT4G33030.1.

    Structurei

    Secondary structure

    1
    477
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi86 – 905Combined sources
    Turni91 – 933Combined sources
    Helixi95 – 10612Combined sources
    Beta strandi110 – 1156Combined sources
    Helixi118 – 1269Combined sources
    Helixi137 – 14812Combined sources
    Beta strandi153 – 1575Combined sources
    Helixi162 – 17211Combined sources
    Beta strandi175 – 1795Combined sources
    Helixi186 – 1894Combined sources
    Helixi193 – 21725Combined sources
    Beta strandi222 – 2265Combined sources
    Helixi229 – 2324Combined sources
    Beta strandi241 – 2488Combined sources
    Beta strandi251 – 2566Combined sources
    Helixi264 – 28320Combined sources
    Beta strandi286 – 2927Combined sources
    Beta strandi294 – 2963Combined sources
    Helixi303 – 3053Combined sources
    Helixi307 – 3093Combined sources
    Turni317 – 3193Combined sources
    Helixi322 – 33211Combined sources
    Beta strandi336 – 3394Combined sources
    Beta strandi345 – 3506Combined sources
    Helixi351 – 36313Combined sources
    Beta strandi371 – 3766Combined sources
    Beta strandi378 – 3825Combined sources
    Helixi383 – 39513Combined sources
    Turni396 – 3983Combined sources
    Beta strandi403 – 4064Combined sources
    Helixi424 – 4274Combined sources
    Helixi437 – 44913Combined sources
    Helixi451 – 4533Combined sources
    Helixi456 – 4583Combined sources
    Turni465 – 4673Combined sources
    Beta strandi469 – 4713Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1I24X-ray1.20A86-477[»]
    1I2BX-ray1.75A86-477[»]
    1I2CX-ray1.60A86-477[»]
    1QRRX-ray1.60A84-477[»]
    ProteinModelPortaliO48917.
    SMRiO48917. Positions 86-475.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO48917.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni322 – 3254Substrate bindingCombined sources2 Publications
    Regioni337 – 3393Substrate bindingCombined sources2 Publications
    Regioni410 – 4123Substrate bindingCombined sources2 Publications

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiKOG1371. Eukaryota.
    COG1087. LUCA.
    HOGENOMiHOG000014371.
    InParanoidiO48917.
    KOiK06118.
    OMAiEEHYYNP.
    PhylomeDBiO48917.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR001509. Epimerase_deHydtase_N.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF01370. Epimerase. 1 hit.
    [Graphical view]
    SUPFAMiSSF51735. SSF51735. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O48917-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAHLLSASCP SVISLSSSSS KNSVKPFVSG QTFFNAQLLS RSSLKGLLFQ
    60 70 80 90 100
    EKKPRKSCVF RATAVPITQQ APPETSTNNS SSKPKRVMVI GGDGYCGWAT
    110 120 130 140 150
    ALHLSKKNYE VCIVDNLVRR LFDHQLGLES LTPIASIHDR ISRWKALTGK
    160 170 180 190 200
    SIELYVGDIC DFEFLAESFK SFEPDSVVHF GEQRSAPYSM IDRSRAVYTQ
    210 220 230 240 250
    HNNVIGTLNV LFAIKEFGEE CHLVKLGTMG EYGTPNIDIE EGYITITHNG
    260 270 280 290 300
    RTDTLPYPKQ ASSFYHLSKV HDSHNIAFTC KAWGIRATDL NQGVVYGVKT
    310 320 330 340 350
    DETEMHEELR NRLDYDAVFG TALNRFCVQA AVGHPLTVYG KGGQTRGYLD
    360 370 380 390 400
    IRDTVQCVEI AIANPAKAGE FRVFNQFTEQ FSVNELASLV TKAGSKLGLD
    410 420 430 440 450
    VKKMTVPNPR VEAEEHYYNA KHTKLMELGL EPHYLSDSLL DSLLNFAVQF
    460 470
    KDRVDTKQIM PSVSWKKIGV KTKSMTT
    Length:477
    Mass (Da):53,114
    Last modified:June 1, 1998 - v1
    Checksum:i25F7304C10B025A9
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF022082 mRNA. Translation: AAB94073.1.
    AL031804 Genomic DNA. Translation: CAA21212.1.
    AL161582 Genomic DNA. Translation: CAB80020.1.
    CP002687 Genomic DNA. Translation: AEE86162.1.
    AF380641 mRNA. Translation: AAK55722.1.
    AY113071 mRNA. Translation: AAM47379.1.
    PIRiT05311.
    RefSeqiNP_195029.1. NM_119457.3.
    UniGeneiAt.2479.

    Genome annotation databases

    EnsemblPlantsiAT4G33030.1; AT4G33030.1; AT4G33030.
    GeneIDi829440.
    GrameneiAT4G33030.1; AT4G33030.1; AT4G33030.
    KEGGiath:AT4G33030.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF022082 mRNA. Translation: AAB94073.1.
    AL031804 Genomic DNA. Translation: CAA21212.1.
    AL161582 Genomic DNA. Translation: CAB80020.1.
    CP002687 Genomic DNA. Translation: AEE86162.1.
    AF380641 mRNA. Translation: AAK55722.1.
    AY113071 mRNA. Translation: AAM47379.1.
    PIRiT05311.
    RefSeqiNP_195029.1. NM_119457.3.
    UniGeneiAt.2479.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1I24X-ray1.20A86-477[»]
    1I2BX-ray1.75A86-477[»]
    1I2CX-ray1.60A86-477[»]
    1QRRX-ray1.60A84-477[»]
    ProteinModelPortaliO48917.
    SMRiO48917. Positions 86-475.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi14725. 1 interaction.
    IntActiO48917. 1 interaction.
    STRINGi3702.AT4G33030.1.

    Proteomic databases

    PaxDbiO48917.
    PRIDEiO48917.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiAT4G33030.1; AT4G33030.1; AT4G33030.
    GeneIDi829440.
    GrameneiAT4G33030.1; AT4G33030.1; AT4G33030.
    KEGGiath:AT4G33030.

    Organism-specific databases

    TAIRiAT4G33030.

    Phylogenomic databases

    eggNOGiKOG1371. Eukaryota.
    COG1087. LUCA.
    HOGENOMiHOG000014371.
    InParanoidiO48917.
    KOiK06118.
    OMAiEEHYYNP.
    PhylomeDBiO48917.

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-1201.
    RETL1328306-WGS:GSTH-3531-MONOMER.
    BRENDAi3.13.1.1. 399.

    Miscellaneous databases

    EvolutionaryTraceiO48917.
    PROiO48917.

    Gene expression databases

    GenevisibleiO48917. AT.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR001509. Epimerase_deHydtase_N.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF01370. Epimerase. 1 hit.
    [Graphical view]
    SUPFAMiSSF51735. SSF51735. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Phosphate availability affects the thylakoid lipid composition and the expression of SQD1, a gene required for sulfolipid biosynthesis in Arabidopsis thaliana."
      Essigmann B., Gueler S., Narang R.A., Linke D., Benning C.
      Proc. Natl. Acad. Sci. U.S.A. 95:1950-1955(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, INDUCTION.
      Strain: cv. Col-2.
    2. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
      Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
      , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
      Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    3. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    5. "Recombinant Arabidopsis SQD1 converts UDP-glucose and sulfite to the sulfolipid head group precursor UDP-sulfoquinovose in vitro."
      Sanda S., Leustek T., Theisen M.J., Garavito R.M., Benning C.
      J. Biol. Chem. 276:3941-3946(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF THR-228.
    6. "Changes in gene expression in Arabidopsis shoots during phosphate starvation and the potential for developing smart plants."
      Hammond J.P., Bennett M.J., Bowen H.C., Broadley M.R., Eastwood D.C., May S.T., Rahn C., Swarup R., Woolaway K.E., White P.J.
      Plant Physiol. 132:578-596(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    7. "Crystal structure of SQD1, an enzyme involved in the biosynthesis of the plant sulfolipid headgroup donor UDP-sulfoquinovose."
      Mulichak A.M., Theisen M.J., Essigmann B., Benning C., Garavito R.M.
      Proc. Natl. Acad. Sci. U.S.A. 96:13097-13102(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH NAD(+) AND UDP-GLUCOSE, ACTIVE SITE.
    8. "Characterization of the active site of UDP-sulfoquinovose synthase: formation of the sulfonic acid product in the crystalline state."
      Theisen M.J., Sanda S.L., Ginell S.L., Benning C., Garavito R.M.
      Submitted (FEB-2001) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) OF 86-477 IN COMPLEX WITH NAD; UDP-GLUCOSE AND UDP-SULFOQUINOVOSE.

    Entry informationi

    Entry nameiSQD1_ARATH
    AccessioniPrimary (citable) accession number: O48917
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 31, 2003
    Last sequence update: June 1, 1998
    Last modified: April 13, 2016
    This is version 123 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.