nadB:Gene Product(s): Difference between revisions

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GO:0008734
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L-aspartate oxidase activity
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[[PMID:2841129]]<ref name=PMID:2841129/>
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IMP: Inferred from Mutant Phenotype
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F
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Table 2
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complete
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Revision as of 01:20, 4 March 2008

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Quickview   Gene   Gene Product(s)   Expression   Evolution   On One Page    
Nomenclature Function Interactions Localization Sequence Structure Resources Accessions Links References Suggestions

Nomenclature

Standard name

NadB product

Synonyms

quinolinate synthase, L-aspartate oxidase (B protein) subunit product[1], B2574 product[2][1], Nic product[2][1], NicB product[2][1], NadB product[2][1]

Product description

L-ASPARTATE-OXID-MONOMER[2][3];

Component of ; quinolinate synthase complex[2][3]

EC number (for enzymes)
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Notes

Function

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Gene Ontology

Qualifier GO ID GO term name Reference(s) Evidence Code with/from Aspect Notes Status
GO:0005737

cytoplasm

C

Seeded from Riley et al 2006 [1].

required fields missing

GO:0009435

NAD biosynthetic process

P

Seeded from EcoCyc 11.1[3].

required fields missing

GO:0008734

L-aspartate oxidase activity

PMID:2841129[4]

IMP: Inferred from Mutant Phenotype

F

Table 2

complete

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Interactions

Partner Type Partner Notes

Protein

Subunits of quinolinate synthase complex

could be indirect

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Notes

Localization

Compartment Description Evidence Notes
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Notes

Structure and Physical Properties

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Physical Properties

Sequence

at EcoCyc

MNTLPEHSCD VLIIGSGAAG LSLALRLADQ HQVIVLSKGP VTEGSTFYAQ GGIAAVFDET
DSIDSHVEDT LIAGAGICDR HAVEFVASNA RSCVQWLIDQ GVLFDTHIQP NGEESYHLTR
EGGHSHRRIL HAADATGREV ETTLVSKALN HPNIRVLERS NAVDLIVSDK IGLPGTRRVV
GAWVWNRNKE TVETCHAKAV VLATGGASKV YQYTTNPDIS SGDGIAMAWR AGCRVANLEF
NQFHPTALYH PQARNFLLTE ALRGEGAYLK RPDGTRFMPD FDERGELAPR DIVARAIDHE
MKRLGADCMF LDISHKPADF IRQHFPMIYE KLLGLGIDLT QEPVPIVPAA HYTCGGVMVD
DHGRTDVEGL YAIGEVSYTG LHGANRMASN SLLECLVYGW SAAEDITRRM PYAHDISTLP
PWDESRVENP DERVVIQHNW HELRLFMWDY VGIVRTTKRL ERALRRITML QQEIDEYYAH
FRVSNNLLEL RNLVQVAELI VRCAMMRKES RGLHFTLDYP ELLTHSGPSI LSPGNHYINR
Mol. Wt

60.34 kDa (calc) [2]

pI

5.6[2]

Extinction coefficient

69330 - 70455 (calc based on 17 Y, 8 W, and 9 C residues)

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Domains/Motifs/Modification Sites

Type Residues Description Notes
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Structure

Structure Type Organism Accession Residues covered Notes

2.2

Escherichia coli

1CHU STRUCTURE OF L-ASPARTATE OXIDASE: IMPLICATIONS FOR THE SUCCINATE DEHYDROGENASE/

X-RAY DIFFRACTION

Escherichia coli

1KNR L-aspartate oxidase: R386L mutant

X-RAY DIFFRACTION

Escherichia coli

1KNP E. coli L-aspartate oxidase: mutant R386L in complex with succinate

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Notes

Gene Product Resources

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Resource type Source Notes/Reference
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Notes

Accessions in Other Databases

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Database Accession Notes

EcoCyc (EcoliWiki Page)

EcoCyc:L-ASPARTATE-OXID-MONOMER

UniProt (EcoliWiki Page)

UniProt:P10902

PFAM (EcoliWiki Page)

PFAM:PF00890

RefSeq (EcoliWiki Page)

RefSeq:NP_417069

ModBase (EcoliWiki Page)

ModBase:P10902

PDB (EcoliWiki Page)

PDB:1KNP

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Notes

Links

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Name URL Comments
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References

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See Help:References for how to manage references in EcoliWiki.

  1. ↑ 1.0 1.1 1.2 1.3 1.4 1.5 1.6 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. ↑ 2.0 2.1 2.2 2.3 2.4 2.5 2.6 2.7 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. ↑ 3.0 3.1 3.2 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  4. ↑ Flachmann, R et al. (1988) Molecular biology of pyridine nucleotide biosynthesis in Escherichia coli. Cloning and characterization of quinolinate synthesis genes nadA and nadB. Eur. J. Biochem. 175 221-8 PubMed


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