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Protein

NH(3)-dependent NAD(+) synthetase

Gene

nadE

Organism
Bacillus anthracis
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.UniRule annotation1 Publication

Catalytic activityi

ATP + deamido-NAD+ + NH3 = AMP + diphosphate + NAD+.UniRule annotation1 Publication

Kineticsi

  1. KM=289 µM for ATP1 Publication
  2. KM=152 µM for deamido-NAD+1 Publication

    pH dependencei

    Optimum pH is 8.1 Publication

    Pathwayi: NAD(+) biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes NAD(+) from deamido-NAD(+) (ammonia route).UniRule annotation
    Proteins known to be involved in this subpathway in this organism are:
    1. NH(3)-dependent NAD(+) synthetase (nadE), NH(3)-dependent NAD(+) synthetase (nadE), NH(3)-dependent NAD(+) synthetase (nadE)
    This subpathway is part of the pathway NAD(+) biosynthesis, which is itself part of Cofactor biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes NAD(+) from deamido-NAD(+) (ammonia route), the pathway NAD(+) biosynthesis and in Cofactor biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Metal bindingi51MagnesiumUniRule annotation1 Publication1
    Binding sitei138Deamido-NADUniRule annotation1
    Binding sitei158ATPUniRule annotation1 Publication1
    Metal bindingi163MagnesiumUniRule annotation1 Publication1
    Binding sitei171Deamido-NADUniRule annotation1 Publication1
    Binding sitei178Deamido-NADUniRule annotation1
    Binding sitei187ATPUniRule annotation1 Publication1
    Binding sitei209ATP; via amide nitrogen and carbonyl oxygenUniRule annotation1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi45 – 52ATPUniRule annotation1 Publication8
    Nucleotide bindingi258 – 259Deamido-NADUniRule annotation2

    GO - Molecular functioni

    • ATP binding Source: UniProtKB-KW
    • NAD+ synthase (glutamine-hydrolyzing) activity Source: TIGR
    • NAD+ synthase activity Source: UniProtKB-EC

    GO - Biological processi

    • asexual sporulation Source: TIGR
    • NAD biosynthetic process Source: UniProtKB-UniPathway
    • NADH metabolic process Source: TIGR

    Keywordsi

    Molecular functionLigase
    LigandATP-binding, Magnesium, Metal-binding, NAD, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi6.3.1.5. 634.
    UniPathwayiUPA00253; UER00333.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NH(3)-dependent NAD(+) synthetaseUniRule annotation (EC:6.3.1.5UniRule annotation)
    Gene namesi
    Name:nadEUniRule annotation
    Ordered Locus Names:BA_1998, GBAA_1998, BAS1855
    OrganismiBacillus anthracis
    Taxonomic identifieri1392 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
    Proteomesi
    • UP000000594 Componenti: Chromosome

    Pathology & Biotechi

    Chemistry databases

    ChEMBLiCHEMBL5271.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001521561 – 272NH(3)-dependent NAD(+) synthetaseAdd BLAST272

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation1 Publication

    Protein-protein interaction databases

    STRINGi198094.BA_1998.

    Chemistry databases

    BindingDBiQ81RP3.

    Structurei

    Secondary structure

    1272
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi3 – 11Combined sources9
    Helixi19 – 37Combined sources19
    Beta strandi41 – 45Combined sources5
    Helixi50 – 68Combined sources19
    Beta strandi74 – 79Combined sources6
    Beta strandi82 – 84Combined sources3
    Helixi89 – 98Combined sources10
    Beta strandi101 – 105Combined sources5
    Helixi109 – 122Combined sources14
    Helixi129 – 151Combined sources23
    Beta strandi154 – 156Combined sources3
    Helixi162 – 166Combined sources5
    Turni171 – 175Combined sources5
    Beta strandi178 – 180Combined sources3
    Turni181 – 184Combined sources4
    Helixi187 – 196Combined sources10
    Helixi201 – 203Combined sources3
    Beta strandi214 – 216Combined sources3
    Helixi221 – 225Combined sources5
    Helixi229 – 236Combined sources8
    Helixi243 – 255Combined sources13
    Helixi256 – 260Combined sources5
    Helixi267 – 272Combined sources6

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2PZ8X-ray2.00A/B1-272[»]
    2PZAX-ray2.40A/B1-272[»]
    2PZBX-ray1.90A/B/C/D1-272[»]
    ProteinModelPortaliQ81RP3.
    SMRiQ81RP3.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ81RP3.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the NAD synthetase family.UniRule annotation

    Phylogenomic databases

    eggNOGiENOG4105C4K. Bacteria.
    COG0171. LUCA.
    HOGENOMiHOG000238070.
    KOiK01916.
    OMAiLVSMPES.

    Family and domain databases

    CDDicd00553. NAD_synthase. 1 hit.
    Gene3Di3.40.50.620. 1 hit.
    HAMAPiMF_00193. NadE_ammonia_dep. 1 hit.
    InterProiView protein in InterPro
    IPR022310. NAD/GMP_synthase.
    IPR003694. NAD_synthase.
    IPR022926. NH(3)-dep_NAD(+)_synth.
    IPR014729. Rossmann-like_a/b/a_fold.
    PANTHERiPTHR23090. PTHR23090. 1 hit.
    PfamiView protein in Pfam
    PF02540. NAD_synthase. 1 hit.
    TIGRFAMsiTIGR00552. nadE. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q81RP3-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTLQEQIMKA LHVQPVIDPK AEIRKRVDFL KDYVKKTGAK GFVLGISGGQ
    60 70 80 90 100
    DSTLAGRLAQ LAVEEIRNEG GNATFIAVRL PYKVQKDEDD AQLALQFIQA
    110 120 130 140 150
    DQSVAFDIAS TVDAFSNQYE NLLDESLTDF NKGNVKARIR MVTQYAIGGQ
    160 170 180 190 200
    KGLLVIGTDH AAEAVTGFFT KFGDGGADLL PLTGLTKRQG RALLQELGAD
    210 220 230 240 250
    ERLYLKMPTA DLLDEKPGQA DETELGITYD QLDDYLEGKT VPADVAEKIE
    260 270
    KRYTVSEHKR QVPASMFDDW WK
    Length:272
    Mass (Da):30,101
    Last modified:June 1, 2003 - v1
    Checksum:iB58A9792E8075B98
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE016879 Genomic DNA. Translation: AAP25889.1.
    AE017334 Genomic DNA. Translation: AAT31119.1.
    AE017225 Genomic DNA. Translation: AAT54170.1.
    RefSeqiNP_844403.1. NC_003997.3.
    WP_000174879.1. NZ_MVOA01000031.1.
    YP_028119.1. NC_005945.1.

    Genome annotation databases

    EnsemblBacteriaiAAP25889; AAP25889; BA_1998.
    AAT31119; AAT31119; GBAA_1998.
    AAT54170; AAT54170; BAS1855.
    GeneIDi1087061.
    2851218.
    KEGGiban:BA_1998.
    bar:GBAA_1998.
    bat:BAS1855.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE016879 Genomic DNA. Translation: AAP25889.1.
    AE017334 Genomic DNA. Translation: AAT31119.1.
    AE017225 Genomic DNA. Translation: AAT54170.1.
    RefSeqiNP_844403.1. NC_003997.3.
    WP_000174879.1. NZ_MVOA01000031.1.
    YP_028119.1. NC_005945.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2PZ8X-ray2.00A/B1-272[»]
    2PZAX-ray2.40A/B1-272[»]
    2PZBX-ray1.90A/B/C/D1-272[»]
    ProteinModelPortaliQ81RP3.
    SMRiQ81RP3.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi198094.BA_1998.

    Chemistry databases

    BindingDBiQ81RP3.
    ChEMBLiCHEMBL5271.

    Protocols and materials databases

    DNASUi1087061.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAP25889; AAP25889; BA_1998.
    AAT31119; AAT31119; GBAA_1998.
    AAT54170; AAT54170; BAS1855.
    GeneIDi1087061.
    2851218.
    KEGGiban:BA_1998.
    bar:GBAA_1998.
    bat:BAS1855.

    Phylogenomic databases

    eggNOGiENOG4105C4K. Bacteria.
    COG0171. LUCA.
    HOGENOMiHOG000238070.
    KOiK01916.
    OMAiLVSMPES.

    Enzyme and pathway databases

    UniPathwayiUPA00253; UER00333.
    BRENDAi6.3.1.5. 634.

    Miscellaneous databases

    EvolutionaryTraceiQ81RP3.

    Family and domain databases

    CDDicd00553. NAD_synthase. 1 hit.
    Gene3Di3.40.50.620. 1 hit.
    HAMAPiMF_00193. NadE_ammonia_dep. 1 hit.
    InterProiView protein in InterPro
    IPR022310. NAD/GMP_synthase.
    IPR003694. NAD_synthase.
    IPR022926. NH(3)-dep_NAD(+)_synth.
    IPR014729. Rossmann-like_a/b/a_fold.
    PANTHERiPTHR23090. PTHR23090. 1 hit.
    PfamiView protein in Pfam
    PF02540. NAD_synthase. 1 hit.
    TIGRFAMsiTIGR00552. nadE. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiNADE_BACAN
    AccessioniPrimary (citable) accession number: Q81RP3
    Secondary accession number(s): Q6HZW9, Q6KTU9
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 13, 2004
    Last sequence update: June 1, 2003
    Last modified: May 10, 2017
    This is version 101 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    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.