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Q2YNT7

- MOAA_BRUA2

UniProt

Q2YNT7 - MOAA_BRUA2

Protein

Cyclic pyranopterin monophosphate synthase

Gene

moaA

Organism
Brucella abortus (strain 2308)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 64 (01 Oct 2014)
      Sequence version 1 (07 Feb 2006)
      Previous versions | rss
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    Functioni

    Catalyzes, together with MoaC, the conversion of 5'-GTP to cyclic pyranopterin monophosphate (cPMP or molybdopterin precursor Z).UniRule annotation

    Catalytic activityi

    GTP = cyclic pyranopterin phosphate + diphosphate.UniRule annotation

    Cofactori

    Binds 2 4Fe-4S clusters. Binds 1 4Fe-4S cluster coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine and 1 4Fe-4S cluster coordinated with 3 cysteines and the GTP-derived substrate.UniRule annotation
    Binds 1 S-adenosyl-L-methionine per subunit.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei28 – 281GTPUniRule annotation
    Metal bindingi35 – 351Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi39 – 391Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
    Binding sitei41 – 411S-adenosyl-L-methionineUniRule annotation
    Metal bindingi42 – 421Iron-sulfur 1 (4Fe-4S-S-AdoMet)UniRule annotation
    Binding sitei77 – 771GTPUniRule annotation
    Binding sitei81 – 811S-adenosyl-L-methionine; via carbonyl oxygenUniRule annotation
    Binding sitei111 – 1111GTPUniRule annotation
    Binding sitei135 – 1351S-adenosyl-L-methionineUniRule annotation
    Binding sitei171 – 1711GTPUniRule annotation
    Binding sitei205 – 2051S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygenUniRule annotation
    Metal bindingi268 – 2681Iron-sulfur 2 (4Fe-4S-substrate)UniRule annotation
    Metal bindingi271 – 2711Iron-sulfur 2 (4Fe-4S-substrate)UniRule annotation
    Metal bindingi285 – 2851Iron-sulfur 2 (4Fe-4S-substrate)UniRule annotation

    GO - Molecular functioni

    1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
    2. cyclic pyranopterin monophosphate synthase activity Source: UniProtKB-EC
    3. GTP binding Source: UniProtKB-KW
    4. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. Mo-molybdopterin cofactor biosynthetic process Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Molybdenum cofactor biosynthesis

    Keywords - Ligandi

    4Fe-4S, GTP-binding, Iron, Iron-sulfur, Metal-binding, Nucleotide-binding, S-adenosyl-L-methionine

    Enzyme and pathway databases

    BioCyciBABO359391:GKDV-989-MONOMER.
    BMEL359391:GJOQ-989-MONOMER.
    UniPathwayiUPA00344.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cyclic pyranopterin monophosphate synthaseUniRule annotation (EC:4.1.99.18UniRule annotation)
    Alternative name(s):
    Molybdenum cofactor biosynthesis protein AUniRule annotation
    Gene namesi
    Name:moaAUniRule annotation
    Ordered Locus Names:BAB1_0973
    OrganismiBrucella abortus (strain 2308)
    Taxonomic identifieri359391 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella
    ProteomesiUP000002719: Chromosome I

    Subcellular locationi

    GO - Cellular componenti

    1. molybdopterin synthase complex Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 344344Cyclic pyranopterin monophosphate synthasePRO_1000054175Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer and homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi359391.BAB1_0973.

    Structurei

    3D structure databases

    ProteinModelPortaliQ2YNT7.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni273 – 2753GTP bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the radical SAM superfamily. MoaA family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG2896.
    HOGENOMiHOG000228680.
    KOiK03639.
    OMAiMFHQITG.
    OrthoDBiEOG64XXNN.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_01225_B. MoaA_B.
    InterProiIPR013785. Aldolase_TIM.
    IPR006638. Elp3/MiaB/NifB.
    IPR013483. MoaA.
    IPR000385. MoaA_NifB_PqqE_Fe-S-bd_CS.
    IPR010505. Mob_synth_C.
    IPR007197. rSAM.
    [Graphical view]
    PfamiPF06463. Mob_synth_C. 1 hit.
    PF04055. Radical_SAM. 1 hit.
    [Graphical view]
    SMARTiSM00729. Elp3. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR02666. moaA. 1 hit.
    PROSITEiPS01305. MOAA_NIFB_PQQE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q2YNT7-1 [UniParc]FASTAAdd to Basket

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    MRNVQDQPLV SPTEPMIDPF GRAVTYLRVS VTDRCDFRCT YCMAEHMTFL    50
    PKKDLLTLEE LDRLCSVFIE KGVRKLRLTG GEPLVRKNIM HLIGNLSRHL 100
    KSGALDELTL TTNGSQLARF AGELADCGVR RINVSLDTLN PEKFRTITRW 150
    GDLSRVLEGI DAAQKAAIHV KINAVALKDF NDAEIPELIR WAHGRGMDVT 200
    LIETMPMGEI EFDRTDQYLP LSQVRADLAS QFTLADIPYR TGGPARYVTI 250
    SETGGRLGFI TPMTYNFCES CNRVRLTCTG MLYMCLGQND DADLRKALRE 300
    SESDEHLSQA IDEAISRKPK GHDFIIDREH NRPSVARHMS LTGG 344
    Length:344
    Mass (Da):38,687
    Last modified:February 7, 2006 - v1
    Checksum:i50B8258570E51148
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM040264 Genomic DNA. Translation: CAJ10929.1.
    RefSeqiYP_414393.1. NC_007618.1.

    Genome annotation databases

    EnsemblBacteriaiCAJ10929; CAJ10929; BAB1_0973.
    GeneIDi3787635.
    KEGGibmf:BAB1_0973.
    PATRICi17844877. VBIBruMel86222_1015.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM040264 Genomic DNA. Translation: CAJ10929.1 .
    RefSeqi YP_414393.1. NC_007618.1.

    3D structure databases

    ProteinModelPortali Q2YNT7.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 359391.BAB1_0973.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAJ10929 ; CAJ10929 ; BAB1_0973 .
    GeneIDi 3787635.
    KEGGi bmf:BAB1_0973.
    PATRICi 17844877. VBIBruMel86222_1015.

    Phylogenomic databases

    eggNOGi COG2896.
    HOGENOMi HOG000228680.
    KOi K03639.
    OMAi MFHQITG.
    OrthoDBi EOG64XXNN.

    Enzyme and pathway databases

    UniPathwayi UPA00344 .
    BioCyci BABO359391:GKDV-989-MONOMER.
    BMEL359391:GJOQ-989-MONOMER.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    HAMAPi MF_01225_B. MoaA_B.
    InterProi IPR013785. Aldolase_TIM.
    IPR006638. Elp3/MiaB/NifB.
    IPR013483. MoaA.
    IPR000385. MoaA_NifB_PqqE_Fe-S-bd_CS.
    IPR010505. Mob_synth_C.
    IPR007197. rSAM.
    [Graphical view ]
    Pfami PF06463. Mob_synth_C. 1 hit.
    PF04055. Radical_SAM. 1 hit.
    [Graphical view ]
    SMARTi SM00729. Elp3. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR02666. moaA. 1 hit.
    PROSITEi PS01305. MOAA_NIFB_PQQE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 2308.

    Entry informationi

    Entry nameiMOAA_BRUA2
    AccessioniPrimary (citable) accession number: Q2YNT7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: February 7, 2006
    Last modified: October 1, 2014
    This is version 64 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Brucella abortus strain 2308
      Brucella abortus (strain 2308): 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