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Protein

Molybdenum cofactor sulfurase

Gene

ABA3

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

Functioni

Sulfurates the molybdenum cofactor. Sulfation of molybdenum is essential for xanthine dehydrogenase (XDH) and aldehyde oxidase (ADO) enzymes in which molybdenum cofactor is liganded by 1 oxygen and 1 sulfur atom in active form. Modulates cold stress- and osmotic stress-responsive gene expression by acting as key regulator of abscisic acid (ABA) biosynthesis.UniRule annotation5 Publications

Catalytic activityi

Molybdenum cofactor + L-cysteine + reduced acceptor + 2 H+ = thio-molybdenum cofactor + L-alanine + H2O + oxidized acceptor.UniRule annotation2 Publications

Cofactori

pyridoxal 5'-phosphateUniRule annotation1 Publication

Kineticsi

  1. KM=50 µM for L-cystein1 Publication
  2. KM=200 µM for L-selenocystein1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei430 – 4301

    GO - Molecular functioni

    • molybdenum ion binding Source: UniProtKB-HAMAP
    • Mo-molybdopterin cofactor sulfurase activity Source: TAIR
    • pyridoxal phosphate binding Source: UniProtKB-HAMAP
    • selenocysteine lyase activity Source: TAIR
    • transferase activity Source: UniProtKB-KW

    GO - Biological processi

    • abscisic acid biosynthetic process Source: TAIR
    • auxin-activated signaling pathway Source: TAIR
    • defense response to bacterium Source: TAIR
    • molybdenum incorporation into molybdenum-molybdopterin complex Source: TAIR
    • Mo-molybdopterin cofactor biosynthetic process Source: UniProtKB-HAMAP
    • protein import into chloroplast stroma Source: TAIR
    • response to cold Source: TAIR
    • response to heat Source: TAIR
    • response to osmotic stress Source: TAIR
    • response to salt stress Source: TAIR
    • stomatal movement Source: TAIR
    • sugar mediated signaling pathway Source: TAIR
    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Molybdenum cofactor biosynthesis

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BRENDAi2.8.1.9. 399.
    ReactomeiR-ATH-947581. Molybdenum cofactor biosynthesis.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Molybdenum cofactor sulfuraseUniRule annotation (EC:2.8.1.9UniRule annotation2 Publications)
    Short name:
    MCSUniRule annotation
    Short name:
    MOSUniRule annotation
    Short name:
    MoCo sulfuraseUniRule annotation
    Alternative name(s):
    Abscisic acid protein 3
    Low expression of osmotically expressive genes protein 5
    Molybdenum cofactor sulfurtransferaseUniRule annotation
    Gene namesi
    Name:ABA3
    Synonyms:LOS5
    Ordered Locus Names:At1g16540
    ORF Names:F19K19.13
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    Proteomesi
    • UP000006548 Componenti: Chromosome 1

    Organism-specific databases

    TAIRiAT1G16540.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi106 – 1061G → E in los5-1; induces a deficience in stress-induced ABA accumulation. 1 Publication
    Mutagenesisi271 – 2711K → S: Loss of function. 1 Publication
    Mutagenesisi430 – 4301C → A: Induces a strong reduction in enzyme activity. 1 Publication
    Mutagenesisi469 – 4691G → E in aba3-1; induces a reduced ABA biosynthesis. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 819819Molybdenum cofactor sulfurasePRO_0000249958Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei271 – 2711N6-(pyridoxal phosphate)lysine

    Proteomic databases

    PaxDbiQ9C5X8.
    PRIDEiQ9C5X8.

    PTM databases

    iPTMnetiQ9C5X8.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed.1 Publication

    Inductioni

    Up-regulated in response to drought, salt or ABA treatment.1 Publication

    Gene expression databases

    GenevisibleiQ9C5X8. AT.

    Interactioni

    Protein-protein interaction databases

    STRINGi3702.AT1G16540.1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9C5X8.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini650 – 817168MOSCUniRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. MOCOS subfamily.UniRule annotation
    Contains 1 MOSC domain.UniRule annotation

    Phylogenomic databases

    eggNOGiKOG2142. Eukaryota.
    COG0520. LUCA.
    COG3217. LUCA.
    HOGENOMiHOG000029698.
    InParanoidiQ9C5X8.
    KOiK15631.
    OMAiCQSKVCG.
    PhylomeDBiQ9C5X8.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    HAMAPiMF_03050. MOCOS.
    InterProiIPR000192. Aminotrans_V_dom.
    IPR005302. MoCF_Sase_C.
    IPR028886. MoCo_sulfurase.
    IPR005303. MOSC_N.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    IPR011037. Pyrv_Knase-like_insert_dom.
    [Graphical view]
    PfamiPF00266. Aminotran_5. 2 hits.
    PF03473. MOSC. 1 hit.
    PF03476. MOSC_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF50800. SSF50800. 1 hit.
    SSF53383. SSF53383. 2 hits.
    PROSITEiPS51340. MOSC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9C5X8-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MEAFLKEFGD YYGYPDGPKN IQEIRDTEFK RLDKGVVYLD HAGSTLYSEL
    60 70 80 90 100
    QMEYIFKDFT SNVFGNPHSQ SDISSATSDL IADARHQVLE YFNASPEDYS
    110 120 130 140 150
    CLFTSGATAA LKLVGETFPW TQDSNFLYTM ENHNSVLGIR EYALAQGASA
    160 170 180 190 200
    CAVDIEEAAN QPGQLTNSGP SIKVKHRAVQ MRNTSKLQKE ESRGNAYNLF
    210 220 230 240 250
    AFPSECNFSG LRFNLDLVKL MKENTETVLQ GSPFSKSKRW MVLIDAAKGC
    260 270 280 290 300
    ATLPPDLSEY PADFVVLSFY KLFGYPTGLG ALLVRNDAAK LLKKTYFSGG
    310 320 330 340 350
    TVAASIADID FVKRRERVEE FFEDGSASFL SIAAIRHGFK LLKSLTPSAI
    360 370 380 390 400
    WMHTTSLSIY VKKKLQALRH GNGAAVCVLY GSENLELSSH KSGPTVTFNL
    410 420 430 440 450
    KRPDGSWFGY LEVEKLASLS GIQLRTGCFC NPGACAKYLE LSHSELRSNV
    460 470 480 490 500
    EAGHICWDDN DVINGKPTGA VRVSFGYMST FEDAKKFIDF IISSFASPPK
    510 520 530 540 550
    KTGNGTVVSG RFPQLPSEDL ESKESFPSHY LKSITVYPIK SCAGFSVIRW
    560 570 580 590 600
    PLCRTGLLHD REWMVQGLTG EILTQKKVPE MSLIKTFIDL EEGLLSVESS
    610 620 630 640 650
    RCEDKLHIRI KSDSYNPRND EFDSHANILE NRNEETRINR WFTNAIGRQC
    660 670 680 690 700
    KLLRYSSSTS KDCLNRNKSP GLCRDLESNI NFANEAQFLL ISEESVADLN
    710 720 730 740 750
    RRLEAKDEDY KRAHEKLNPH RFRPNLVISG GEPYGEDKWK TVKIGDNHFT
    760 770 780 790 800
    SLGGCNRCQM INISNEAGLV KKSNEPLTTL ASYRRVKGKI LFGTLLRYEI
    810
    DEKRQCWIGV GEEVNPDIE
    Length:819
    Mass (Da):91,803
    Last modified:June 1, 2001 - v1
    Checksum:i81FE806B186B4007
    GO

    Sequence cautioni

    The sequence AAG10824.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF325457 mRNA. Translation: AAK12939.1.
    AY034895 mRNA. Translation: AAK58888.1.
    AC011808 Genomic DNA. Translation: AAG10824.1. Sequence problems.
    CP002684 Genomic DNA. Translation: AEE29467.1.
    PIRiG86300.
    RefSeqiNP_564001.1. NM_101519.2.
    UniGeneiAt.18927.

    Genome annotation databases

    EnsemblPlantsiAT1G16540.1; AT1G16540.1; AT1G16540.
    GeneIDi838224.
    GrameneiAT1G16540.1; AT1G16540.1; AT1G16540.
    KEGGiath:AT1G16540.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF325457 mRNA. Translation: AAK12939.1.
    AY034895 mRNA. Translation: AAK58888.1.
    AC011808 Genomic DNA. Translation: AAG10824.1. Sequence problems.
    CP002684 Genomic DNA. Translation: AEE29467.1.
    PIRiG86300.
    RefSeqiNP_564001.1. NM_101519.2.
    UniGeneiAt.18927.

    3D structure databases

    ProteinModelPortaliQ9C5X8.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi3702.AT1G16540.1.

    PTM databases

    iPTMnetiQ9C5X8.

    Proteomic databases

    PaxDbiQ9C5X8.
    PRIDEiQ9C5X8.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiAT1G16540.1; AT1G16540.1; AT1G16540.
    GeneIDi838224.
    GrameneiAT1G16540.1; AT1G16540.1; AT1G16540.
    KEGGiath:AT1G16540.

    Organism-specific databases

    TAIRiAT1G16540.

    Phylogenomic databases

    eggNOGiKOG2142. Eukaryota.
    COG0520. LUCA.
    COG3217. LUCA.
    HOGENOMiHOG000029698.
    InParanoidiQ9C5X8.
    KOiK15631.
    OMAiCQSKVCG.
    PhylomeDBiQ9C5X8.

    Enzyme and pathway databases

    BRENDAi2.8.1.9. 399.
    ReactomeiR-ATH-947581. Molybdenum cofactor biosynthesis.

    Miscellaneous databases

    PROiQ9C5X8.

    Gene expression databases

    GenevisibleiQ9C5X8. AT.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    HAMAPiMF_03050. MOCOS.
    InterProiIPR000192. Aminotrans_V_dom.
    IPR005302. MoCF_Sase_C.
    IPR028886. MoCo_sulfurase.
    IPR005303. MOSC_N.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    IPR011037. Pyrv_Knase-like_insert_dom.
    [Graphical view]
    PfamiPF00266. Aminotran_5. 2 hits.
    PF03473. MOSC. 1 hit.
    PF03476. MOSC_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF50800. SSF50800. 1 hit.
    SSF53383. SSF53383. 2 hits.
    PROSITEiPS51340. MOSC. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "ABA3 is a molybdenum cofactor sulfurase required for activation of aldehyde oxidase and xanthine dehydrogenase in Arabidopsis thaliana."
      Bittner F., Oreb M., Mendel R.R.
      J. Biol. Chem. 276:40381-40384(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLY-469.
    2. "The arabidopsis los5/aba3 locus encodes a molybdenum cofactor sulfurase and modulates cold stress- and osmotic stress-responsive gene expression."
      Xiong L., Ishitani M., Lee H., Zhu J.-K.
      Plant Cell 13:2063-2083(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION, MUTAGENESIS OF GLY-106 AND GLY-469.
    3. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
      Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
      , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
      Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    4. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    5. "Tandem orientation of duplicated xanthine dehydrogenase genes from Arabidopsis thaliana: differential gene expression and enzyme activities."
      Hesberg C., Haensch R., Mendel R.R., Bittner F.
      J. Biol. Chem. 279:13547-13554(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "Characterization of the NifS-like domain of ABA3 from Arabidopsis thaliana provides insight into the mechanism of molybdenum cofactor sulfuration."
      Heidenreich T., Wollers S., Mendel R.R., Bittner F.
      J. Biol. Chem. 280:4213-4218(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: COFACTOR, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PYRIDOXAL PHOSPHATE AT LYS-271, MUTAGENESIS OF LYS-271 AND CYS-430.
    7. "Binding of sulfurated molybdenum cofactor to the C-terminal domain of ABA3 from Arabidopsis thaliana provides insight into the mechanism of molybdenum cofactor sulfuration."
      Wollers S., Heidenreich T., Zarepour M., Zachmann D., Kraft C., Zhao Y., Mendel R.R., Bittner F.
      J. Biol. Chem. 283:9642-9650(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF C-TERMINAL DOMAIN.

    Entry informationi

    Entry nameiMOCOS_ARATH
    AccessioniPrimary (citable) accession number: Q9C5X8
    Secondary accession number(s): Q9FX72
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 19, 2006
    Last sequence update: June 1, 2001
    Last modified: July 6, 2016
    This is version 90 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

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. 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.