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P10902

- NADB_ECOLI

UniProt

P10902 - NADB_ECOLI

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Protein
L-aspartate oxidase
Gene
nadB, nicB, b2574, JW2558
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 – 2441 By similarity
Active sitei263 – 2631 By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi12 – 2615FAD Reviewed prediction
Add
BLAST

GO - Molecular functioni

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

GO - Biological processi

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

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
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 540540L-aspartate oxidase
PRO_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

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.

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti160 – 1601S → T1 Publication
Sequence conflicti160 – 1601S → T1 Publication
Sequence conflicti160 – 1601S → T1 Publication
Sequence conflicti485 – 4851N → D in CAA31217. 1 Publication

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

« Hide 'large scale' publications
  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: May 14, 2014
This is version 141 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

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