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P10902

- NADB_ECOLI

UniProt

P10902 - NADB_ECOLI

Protein

L-aspartate oxidase

Gene

nadB

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 4 (29 Aug 2003)
      Previous versions | rss
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    Functioni

    Catalyzes the oxidation of L-aspartate to iminoaspartate.

    Catalytic activityi

    L-aspartate + O2 = iminosuccinate + H2O2.

    Cofactori

    FAD.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei244 – 2441By similarity
    Active sitei263 – 2631By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi12 – 2615FADSequence AnalysisAdd
    BLAST

    GO - Molecular functioni

    1. flavin adenine dinucleotide binding Source: EcoCyc
    2. L-aspartate:fumarate oxidoreductase activity Source: EcoCyc
    3. L-aspartate oxidase activity Source: EcoCyc

    GO - Biological processi

    1. 'de novo' NAD biosynthetic process from aspartate Source: EcoCyc

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Pyridine nucleotide biosynthesis

    Keywords - Ligandi

    FAD, Flavoprotein

    Enzyme and pathway databases

    BioCyciEcoCyc:L-ASPARTATE-OXID-MONOMER.
    ECOL316407:JW2558-MONOMER.
    MetaCyc:L-ASPARTATE-OXID-MONOMER.
    UniPathwayiUPA00253; UER00326.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    L-aspartate oxidase (EC:1.4.3.16)
    Short name:
    LASPO
    Alternative name(s):
    Quinolinate synthase B
    Gene namesi
    Name:nadB
    Synonyms:nicB
    Ordered Locus Names:b2574, JW2558
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10631. nadB.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 540540L-aspartate oxidasePRO_0000184384Add
    BLAST

    Post-translational modificationi

    Contains two disulfide bonds.

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PaxDbiP10902.
    PRIDEiP10902.

    Expressioni

    Gene expression databases

    GenevestigatoriP10902.

    Interactioni

    Subunit structurei

    Monomer.

    Protein-protein interaction databases

    DIPiDIP-556N.
    IntActiP10902. 7 interactions.
    STRINGi511145.b2574.

    Structurei

    Secondary structure

    1
    540
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 83
    Beta strandi10 – 145
    Helixi18 – 2710
    Turni28 – 303
    Beta strandi33 – 364
    Beta strandi38 – 403
    Helixi45 – 484
    Helixi60 – 7314
    Turni74 – 763
    Helixi80 – 9920
    Beta strandi110 – 1134
    Helixi145 – 1506
    Beta strandi154 – 1574
    Beta strandi159 – 1679
    Helixi168 – 1703
    Beta strandi178 – 1869
    Turni187 – 1904
    Beta strandi191 – 1966
    Beta strandi198 – 2025
    Helixi208 – 2103
    Beta strandi211 – 2155
    Helixi217 – 2193
    Helixi223 – 2308
    Beta strandi241 – 2488
    Helixi260 – 2645
    Beta strandi268 – 2703
    Helixi278 – 2803
    Helixi285 – 2873
    Helixi290 – 30415
    Beta strandi309 – 3124
    Helixi319 – 3246
    Helixi326 – 3338
    Turni334 – 3363
    Turni339 – 3413
    Beta strandi344 – 35411
    Beta strandi356 – 3583
    Beta strandi366 – 3683
    Beta strandi370 – 3723
    Helixi374 – 3763
    Beta strandi380 – 3823
    Helixi390 – 40920
    Helixi410 – 4123
    Helixi430 – 45021
    Beta strandi451 – 4555
    Helixi457 – 47822
    Helixi485 – 50622

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CHUX-ray2.20A1-540[»]
    1KNPX-ray2.60A1-540[»]
    1KNRX-ray2.50A1-540[»]
    ProteinModelPortaliP10902.
    SMRiP10902. Positions 5-533.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP10902.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0029.
    HOGENOMiHOG000160476.
    KOiK00278.
    OMAiAWDASQV.
    OrthoDBiEOG696BWH.
    PhylomeDBiP10902.

    Family and domain databases

    Gene3Di1.20.58.100. 1 hit.
    3.90.700.10. 1 hit.
    InterProiIPR003953. FAD_bind_dom.
    IPR013027. FAD_pyr_nucl-diS_OxRdtase.
    IPR015939. Fum_Rdtase/Succ_DH_flav-like_C.
    IPR005288. NadB.
    IPR027477. Succ_DH/fumarate_Rdtase_cat.
    [Graphical view]
    PfamiPF00890. FAD_binding_2. 1 hit.
    PF02910. Succ_DH_flav_C. 1 hit.
    [Graphical view]
    PRINTSiPR00368. FADPNR.
    SUPFAMiSSF46977. SSF46977. 1 hit.
    SSF56425. SSF56425. 1 hit.
    TIGRFAMsiTIGR00551. nadB. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P10902-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNTLPEHSCD VLIIGSGAAG LSLALRLADQ HQVIVLSKGP VTEGSTFYAQ    50
    GGIAAVFDET DSIDSHVEDT LIAGAGICDR HAVEFVASNA RSCVQWLIDQ 100
    GVLFDTHIQP NGEESYHLTR EGGHSHRRIL HAADATGREV ETTLVSKALN 150
    HPNIRVLERS NAVDLIVSDK IGLPGTRRVV GAWVWNRNKE TVETCHAKAV 200
    VLATGGASKV YQYTTNPDIS SGDGIAMAWR AGCRVANLEF NQFHPTALYH 250
    PQARNFLLTE ALRGEGAYLK RPDGTRFMPD FDERGELAPR DIVARAIDHE 300
    MKRLGADCMF LDISHKPADF IRQHFPMIYE KLLGLGIDLT QEPVPIVPAA 350
    HYTCGGVMVD DHGRTDVEGL YAIGEVSYTG LHGANRMASN SLLECLVYGW 400
    SAAEDITRRM PYAHDISTLP PWDESRVENP DERVVIQHNW HELRLFMWDY 450
    VGIVRTTKRL ERALRRITML QQEIDEYYAH FRVSNNLLEL RNLVQVAELI 500
    VRCAMMRKES RGLHFTLDYP ELLTHSGPSI LSPGNHYINR 540
    Length:540
    Mass (Da):60,337
    Last modified:August 29, 2003 - v4
    Checksum:i7B6CFF633BD4AFEC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti160 – 1601S → T(PubMed:2841129)Curated
    Sequence conflicti160 – 1601S → T1 PublicationCurated
    Sequence conflicti160 – 1601S → T1 PublicationCurated
    Sequence conflicti485 – 4851N → D in CAA31217. (PubMed:2841129)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X12714 Genomic DNA. Translation: CAA31217.1.
    D13169 Genomic DNA. Translation: BAA02446.1.
    D64044 Genomic DNA. Translation: BAA10921.1.
    U00096 Genomic DNA. Translation: AAC75627.1.
    AP009048 Genomic DNA. Translation: BAE76750.1.
    PIRiE65035. OXECLD.
    RefSeqiNP_417069.1. NC_000913.3.
    YP_490802.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75627; AAC75627; b2574.
    BAE76750; BAE76750; BAE76750.
    GeneIDi12934288.
    947049.
    KEGGiecj:Y75_p2527.
    eco:b2574.
    PATRICi32120547. VBIEscCol129921_2676.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X12714 Genomic DNA. Translation: CAA31217.1 .
    D13169 Genomic DNA. Translation: BAA02446.1 .
    D64044 Genomic DNA. Translation: BAA10921.1 .
    U00096 Genomic DNA. Translation: AAC75627.1 .
    AP009048 Genomic DNA. Translation: BAE76750.1 .
    PIRi E65035. OXECLD.
    RefSeqi NP_417069.1. NC_000913.3.
    YP_490802.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CHU X-ray 2.20 A 1-540 [» ]
    1KNP X-ray 2.60 A 1-540 [» ]
    1KNR X-ray 2.50 A 1-540 [» ]
    ProteinModelPortali P10902.
    SMRi P10902. Positions 5-533.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-556N.
    IntActi P10902. 7 interactions.
    STRINGi 511145.b2574.

    Proteomic databases

    PaxDbi P10902.
    PRIDEi P10902.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC75627 ; AAC75627 ; b2574 .
    BAE76750 ; BAE76750 ; BAE76750 .
    GeneIDi 12934288.
    947049.
    KEGGi ecj:Y75_p2527.
    eco:b2574.
    PATRICi 32120547. VBIEscCol129921_2676.

    Organism-specific databases

    EchoBASEi EB0625.
    EcoGenei EG10631. nadB.

    Phylogenomic databases

    eggNOGi COG0029.
    HOGENOMi HOG000160476.
    KOi K00278.
    OMAi AWDASQV.
    OrthoDBi EOG696BWH.
    PhylomeDBi P10902.

    Enzyme and pathway databases

    UniPathwayi UPA00253 ; UER00326 .
    BioCyci EcoCyc:L-ASPARTATE-OXID-MONOMER.
    ECOL316407:JW2558-MONOMER.
    MetaCyc:L-ASPARTATE-OXID-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P10902.
    PROi P10902.

    Gene expression databases

    Genevestigatori P10902.

    Family and domain databases

    Gene3Di 1.20.58.100. 1 hit.
    3.90.700.10. 1 hit.
    InterProi IPR003953. FAD_bind_dom.
    IPR013027. FAD_pyr_nucl-diS_OxRdtase.
    IPR015939. Fum_Rdtase/Succ_DH_flav-like_C.
    IPR005288. NadB.
    IPR027477. Succ_DH/fumarate_Rdtase_cat.
    [Graphical view ]
    Pfami PF00890. FAD_binding_2. 1 hit.
    PF02910. Succ_DH_flav_C. 1 hit.
    [Graphical view ]
    PRINTSi PR00368. FADPNR.
    SUPFAMi SSF46977. SSF46977. 1 hit.
    SSF56425. SSF56425. 1 hit.
    TIGRFAMsi TIGR00551. nadB. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Molecular biology of pyridine nucleotide biosynthesis in Escherichia coli. Cloning and characterization of quinolinate synthesis genes nadA and nadB."
      Flachmann R., Kunz N., Seifert J., Guetlich M., Wientjes F.-J., Laeufer A., Gassen H.G.
      Eur. J. Biochem. 175:221-228(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-19.
    2. Kunz N.
      Submitted (APR-1989) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. "Non-ribosomal proteins affecting the assembly of ribosomes in Escherichia coli."
      Nashimoto H.
      (In) Nierhaus K.H. (eds.); The translational apparatus, pp.185-195, Plenum Press, New York (1993)
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    4. Nashimoto H., Saito N.
      Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    6. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    7. "Expression of the E. coli nadB gene and characterization of the gene product L-aspartate oxidase."
      Seifert J., Kunz N., Flachmann R., Laeufer A., Jany K.-D., Gassen H.G.
      Biol. Chem. Hoppe-Seyler 371:239-248(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, PARTIAL PROTEIN SEQUENCE.
    8. "Structure of L-aspartate oxidase: implications for the succinate dehydrogenase/fumarate reductase oxidoreductase family."
      Mattevi A., Tedeschi G., Bacchella L., Coda A., Negri A., Ronchi S.
      Structure 7:745-756(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).

    Entry informationi

    Entry nameiNADB_ECOLI
    AccessioniPrimary (citable) accession number: P10902
    Secondary accession number(s): P78099, Q2MAF6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: August 29, 2003
    Last modified: October 1, 2014
    This is version 142 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3