Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9ZNW0

- MOCS3_ARATH

UniProt

Q9ZNW0 - MOCS3_ARATH

Protein

Adenylyltransferase and sulfurtransferase MOCS3

Gene

MOCS3

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Plays a central role in 2-thiolation of mcm5S2U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers URM1 and MOCS2A. Its N-terminus first activates URM1 and MOCS2A as acyl-adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to URM1 and MOCS2A to form thiocarboxylation (-COSH) of their C-terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as nucleophile towards URM1 and MOCS2A. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor; NFS1 probably acting as a sulfur donor for thiocarboxylation reactions.UniRule annotation

    Catalytic activityi

    ATP + [molybdopterin-synthase sulfur-carrier protein]-Gly-Gly = diphosphate + [molybdopterin-synthase sulfur-carrier protein]-Gly-Gly-AMP.UniRule annotation
    [Molybdopterin-synthase sulfur-carrier protein]-Gly-Gly-AMP + [cysteine desulfurase]-S-sulfanyl-L-cysteine = AMP + [molybdopterin-synthase sulfur-carrier protein]-Gly-NH-CH(2)-C(O)SH + cysteine desulfurase.UniRule annotation

    Cofactori

    Binds 1 zinc ion per subunit.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei101 – 1011ATP; via amide nitrogenUniRule annotation
    Binding sitei122 – 1221ATPUniRule annotation
    Binding sitei146 – 1461ATPUniRule annotation
    Metal bindingi231 – 2311ZincUniRule annotation
    Metal bindingi234 – 2341ZincUniRule annotation
    Active sitei248 – 2481Glycyl thioester intermediate; for adenylyltransferase activityUniRule annotation
    Metal bindingi306 – 3061ZincUniRule annotation
    Metal bindingi309 – 3091ZincUniRule annotation
    Active sitei422 – 4221Cysteine persulfide intermediate; for sulfurtransferase activityUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi129 – 1335ATPUniRule annotation
    Nucleotide bindingi190 – 1912ATPUniRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. molybdopterin-synthase adenylyltransferase activity Source: UniProtKB-EC
    4. molybdopterin-synthase sulfurtransferase activity Source: UniProtKB-EC
    5. Mo-molybdopterin cofactor sulfurase activity Source: TAIR
    6. thiosulfate sulfurtransferase activity Source: InterPro

    GO - Biological processi

    1. enzyme active site formation via L-cysteine persulfide Source: UniProtKB-HAMAP
    2. Mo-molybdopterin cofactor biosynthetic process Source: UniProtKB-HAMAP
    3. tRNA wobble position uridine thiolation Source: InterPro

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Molybdenum cofactor biosynthesis, tRNA processing

    Keywords - Ligandi

    ATP-binding, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    BioCyciARA:GQT-2702-MONOMER.
    ARA:GQT-2704-MONOMER.
    ReactomeiREACT_187830. Molybdenum cofactor biosynthesis.
    UniPathwayiUPA00344.
    UPA00988.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Adenylyltransferase and sulfurtransferase MOCS3UniRule annotation
    Alternative name(s):
    Molybdenum cofactor synthesis protein 3UniRule annotation
    Including the following 2 domains:
    Molybdopterin-synthase adenylyltransferaseUniRule annotation (EC:2.7.7.80UniRule annotation)
    Alternative name(s):
    Adenylyltransferase MOCS3UniRule annotation
    Sulfur carrier protein MOCS2A adenylyltransferaseUniRule annotation
    Molybdopterin-synthase sulfurtransferaseUniRule annotation (EC:2.8.1.11UniRule annotation)
    Alternative name(s):
    Sulfur carrier protein MOCS2A sulfurtransferaseUniRule annotation
    Sulfurtransferase 13UniRule annotation
    Short name:
    AtStr13
    Sulfurtransferase MOCS3UniRule annotation
    Gene namesi
    Name:MOCS3UniRule annotation
    Synonyms:CNX5UniRule annotation, STR13, UBA4UniRule annotation
    Ordered Locus Names:At5g55130
    ORF Names:MCO15.8
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 5

    Organism-specific databases

    TAIRiAT5G55130.

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytosol Source: InterPro

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 464464Adenylyltransferase and sulfurtransferase MOCS3PRO_0000120584Add
    BLAST

    Proteomic databases

    PaxDbiQ9ZNW0.
    PRIDEiQ9ZNW0.

    Expressioni

    Gene expression databases

    GenevestigatoriQ9ZNW0.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9ZNW0.
    SMRiQ9ZNW0. Positions 28-310, 345-464.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini358 – 462105RhodaneseUniRule annotationAdd
    BLAST

    Sequence similaritiesi

    In the N-terminal section; belongs to the HesA/MoeB/ThiF family. UBA4 subfamily.UniRule annotation
    Contains 1 rhodanese domain.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0476.
    HOGENOMiHOG000281219.
    InParanoidiQ9ZNW0.
    KOiK11996.
    OMAiVRKDPEC.
    PhylomeDBiQ9ZNW0.

    Family and domain databases

    Gene3Di3.40.250.10. 1 hit.
    3.40.50.720. 1 hit.
    HAMAPiMF_03049. MOCS3_Uba4.
    InterProiIPR028885. MOCS3/Uba4.
    IPR007901. MoeZ_MoeB.
    IPR009036. Molybdenum_cofac_synth_MoeB.
    IPR016040. NAD(P)-bd_dom.
    IPR001763. Rhodanese-like_dom.
    IPR000594. ThiF_NAD_FAD-bd.
    [Graphical view]
    PfamiPF05237. MoeZ_MoeB. 1 hit.
    PF00581. Rhodanese. 1 hit.
    PF00899. ThiF. 1 hit.
    [Graphical view]
    SMARTiSM00450. RHOD. 1 hit.
    [Graphical view]
    SUPFAMiSSF69572. SSF69572. 1 hit.
    PROSITEiPS50206. RHODANESE_3. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9ZNW0-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MMSNGGDSSE IVRELEELKL KKAEIEHRIS TLEAKLQDTA AVELYDAVSN    50
    GDSYLTAPEL EHGLSPDQIY RYSRQLLLPS FAVEGQSNLL KSSVLVIGAG 100
    GLGSPALLYL AACGVGQLGI IDHDVVELNN MHRQIIHTEA FIGHPKVKSA 150
    AAACRSINST IKVDEYVEAL RTSNALEILS QYDIIVDATD NPPSRYMISD 200
    CCVLLGKPLV SGAALGMEGQ LTVYNHNGGP CYRCLFPTPP PTSACQRCSD 250
    SGVLGVVPGV IGCLQALETI KLASLVGEPL SERMLLFDAL SARMRIVKIR 300
    GRSSQCTVCG DNSSFNKQTF KDFDYEDFTQ FPLFAGPLNL LPAESRISSK 350
    EFKEILQKKE QHVLLDVRPS HHYKIVSLPD SLNIPLANLE TRLNELTSAL 400
    KEKGNGHANT ESCTNPSVFV VCRRGNDSQR AVQYLRESGF DSAKDIIGGL 450
    EAWAANVNPN FPTY 464
    Length:464
    Mass (Da):50,574
    Last modified:May 1, 1999 - v1
    Checksum:i844C7C35C7737940
    GO
    Isoform 2 (identifier: Q9ZNW0-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         85-111: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:437
    Mass (Da):47,993
    Checksum:iD25E7E843FE21E11
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei85 – 11127Missing in isoform 2. 1 PublicationVSP_042632Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF124160 Genomic DNA. Translation: AAD18051.1.
    AF124159 mRNA. Translation: AAD18050.1.
    AB010071 Genomic DNA. Translation: BAB08582.1.
    CP002688 Genomic DNA. Translation: AED96586.1.
    CP002688 Genomic DNA. Translation: AED96587.1.
    BT029156 mRNA. Translation: ABJ17091.1.
    AK317295 mRNA. Translation: BAH19971.1.
    RefSeqiNP_001032076.1. NM_001036999.1. [Q9ZNW0-2]
    NP_200324.1. NM_124895.2. [Q9ZNW0-1]
    UniGeneiAt.24643.
    At.48080.

    Genome annotation databases

    EnsemblPlantsiAT5G55130.1; AT5G55130.1; AT5G55130. [Q9ZNW0-1]
    GeneIDi835604.
    KEGGiath:AT5G55130.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF124160 Genomic DNA. Translation: AAD18051.1 .
    AF124159 mRNA. Translation: AAD18050.1 .
    AB010071 Genomic DNA. Translation: BAB08582.1 .
    CP002688 Genomic DNA. Translation: AED96586.1 .
    CP002688 Genomic DNA. Translation: AED96587.1 .
    BT029156 mRNA. Translation: ABJ17091.1 .
    AK317295 mRNA. Translation: BAH19971.1 .
    RefSeqi NP_001032076.1. NM_001036999.1. [Q9ZNW0-2 ]
    NP_200324.1. NM_124895.2. [Q9ZNW0-1 ]
    UniGenei At.24643.
    At.48080.

    3D structure databases

    ProteinModelPortali Q9ZNW0.
    SMRi Q9ZNW0. Positions 28-310, 345-464.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PaxDbi Q9ZNW0.
    PRIDEi Q9ZNW0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT5G55130.1 ; AT5G55130.1 ; AT5G55130 . [Q9ZNW0-1 ]
    GeneIDi 835604.
    KEGGi ath:AT5G55130.

    Organism-specific databases

    TAIRi AT5G55130.

    Phylogenomic databases

    eggNOGi COG0476.
    HOGENOMi HOG000281219.
    InParanoidi Q9ZNW0.
    KOi K11996.
    OMAi VRKDPEC.
    PhylomeDBi Q9ZNW0.

    Enzyme and pathway databases

    UniPathwayi UPA00344 .
    UPA00988 .
    BioCyci ARA:GQT-2702-MONOMER.
    ARA:GQT-2704-MONOMER.
    Reactomei REACT_187830. Molybdenum cofactor biosynthesis.

    Miscellaneous databases

    PROi Q9ZNW0.

    Gene expression databases

    Genevestigatori Q9ZNW0.

    Family and domain databases

    Gene3Di 3.40.250.10. 1 hit.
    3.40.50.720. 1 hit.
    HAMAPi MF_03049. MOCS3_Uba4.
    InterProi IPR028885. MOCS3/Uba4.
    IPR007901. MoeZ_MoeB.
    IPR009036. Molybdenum_cofac_synth_MoeB.
    IPR016040. NAD(P)-bd_dom.
    IPR001763. Rhodanese-like_dom.
    IPR000594. ThiF_NAD_FAD-bd.
    [Graphical view ]
    Pfami PF05237. MoeZ_MoeB. 1 hit.
    PF00581. Rhodanese. 1 hit.
    PF00899. ThiF. 1 hit.
    [Graphical view ]
    SMARTi SM00450. RHOD. 1 hit.
    [Graphical view ]
    SUPFAMi SSF69572. SSF69572. 1 hit.
    PROSITEi PS50206. RHODANESE_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and sequencing of a genomic region coding for the MPT-synthase-sulphurylase (Cnx5) in A.thaliana."
      Nieder J., Gutzke G., Mendel R.R.
      Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: cv. Columbia.
    2. "Molybdenum cofactor biosynthesis: identification of A.thaliana cDNAs homologous to the E.coli sulfotransferase MoeB."
      Nieder J., Stallmeyer B., Brinkmann H., Mendel R.R.
      (In) Cram W.J., de Kok L.J., Stulen I., Brunold C., Rennenberg H. (eds.); Sulphur Metabolism in Higher Plants, pp.275-277, Backhuys Publishers, Leiden (1997)
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Strain: cv. Columbia.
    3. "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence features of the regions of 1,456,315 bp covered by nineteen physically assigned P1 and TAC clones."
      Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N., Tabata S.
      DNA Res. 5:41-54(1998) [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. "Whole genome sequence comparisons and 'full-length' cDNA sequences: a combined approach to evaluate and improve Arabidopsis genome annotation."
      Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M., Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M., Weissenbach J., Salanoubat M.
      Genome Res. 14:406-413(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Strain: cv. Columbia.
    6. "Analysis of multiple occurrences of alternative splicing events in Arabidopsis thaliana using novel sequenced full-length cDNAs."
      Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M., Shinozaki K.
      DNA Res. 16:155-164(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Strain: cv. Columbia.
      Tissue: Rosette leaf.
    7. "Differential expression of Arabidopsis sulfurtransferases under various growth conditions."
      Bartels A., Mock H.P., Papenbrock J.
      Plant Physiol. Biochem. 45:178-187(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENE FAMILY.

    Entry informationi

    Entry nameiMOCS3_ARATH
    AccessioniPrimary (citable) accession number: Q9ZNW0
    Secondary accession number(s): B9DGV4, Q058R2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 26, 2002
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 104 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, Multifunctional enzyme, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3