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Protein

Quinolinate synthase A

Gene

nadA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate.3 Publications

Catalytic activityi

Glycerone phosphate + iminosuccinate = pyridine-2,3-dicarboxylate + 2 H2O + phosphate.

Cofactori

[4Fe-4S] cluster2 PublicationsNote: Binds 1 [4Fe-4S] cluster per subunit.2 Publications

Enzyme regulationi

Activity is greater under oxic conditions and is regulated by a redox-active disulfide bond.

Pathwayi: NAD(+) biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes quinolinate from iminoaspartate.
Proteins known to be involved in this subpathway in this organism are:
  1. Quinolinate synthase A (nadA)
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 quinolinate from iminoaspartate, the pathway NAD(+) biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei47 – 471IminoaspartateBy similarity
Binding sitei68 – 681Iminoaspartate; via amide nitrogenBy similarity
Binding sitei139 – 1391IminoaspartateBy similarity
Binding sitei156 – 1561IminoaspartateBy similarity
Binding sitei226 – 2261IminoaspartateBy similarity
Binding sitei243 – 2431IminoaspartateBy similarity

GO - Molecular functioni

GO - Biological processi

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

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Pyridine nucleotide biosynthesis

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:QUINOLINATE-SYNTHA-MONOMER.
ECOL316407:JW0733-MONOMER.
MetaCyc:QUINOLINATE-SYNTHA-MONOMER.
UniPathwayiUPA00253; UER00327.

Names & Taxonomyi

Protein namesi
Recommended name:
Quinolinate synthase A (EC:2.5.1.72)
Gene namesi
Name:nadA
Synonyms:nicA
Ordered Locus Names:b0750, JW0733
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10630. nadA.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi291 – 2911C → S: Activity is 3.3-fold lower under oxic conditions than under anoxic conditions. 1 Publication
Mutagenesisi294 – 2941C → S: Activity is 13-fold lower under oxic conditions than under anoxic conditions. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 347347Quinolinate synthase APRO_0000155760Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi291 ↔ 294Redox-active

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP11458.
PRIDEiP11458.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi4263028. 7 interactions.
DIPiDIP-1027N.
IntActiP11458. 6 interactions.
STRINGi511145.b0750.

Structurei

3D structure databases

ProteinModelPortaliP11458.
SMRiP11458. Positions 30-342.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiENOG4105D0I. Bacteria.
COG0379. LUCA.
HOGENOMiHOG000222769.
InParanoidiP11458.
KOiK03517.
OMAiIAHPECE.
PhylomeDBiP11458.

Family and domain databases

HAMAPiMF_00567. NadA_type1. 1 hit.
InterProiIPR003473. NadA.
IPR023513. Quinolinate_synth_A_type1.
[Graphical view]
PfamiPF02445. NadA. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00550. nadA. 1 hit.

Sequencei

Sequence statusi: Complete.

P11458-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVMFDPDTA IYPFPPKPTP LSIDEKAYYR EKIKRLLKER NAVMVAHYYT
60 70 80 90 100
DPEIQQLAEE TGGCISDSLE MARFGAKHPA STLLVAGVRF MGETAKILSP
110 120 130 140 150
EKTILMPTLQ AECSLDLGCP VEEFNAFCDA HPDRTVVVYA NTSAAVKARA
160 170 180 190 200
DWVVTSSIAV ELIDHLDSLG EKIIWAPDKH LGRYVQKQTG GDILCWQGAC
210 220 230 240 250
IVHDEFKTQA LTRLQEEYPD AAILVHPESP QAIVDMADAV GSTSQLIAAA
260 270 280 290 300
KTLPHQRLIV ATDRGIFYKM QQAVPDKELL EAPTAGEGAT CRSCAHCPWM
310 320 330 340
AMNGLQAIAE ALEQEGSNHE VHVDERLRER ALVPLNRMLD FAATLRG
Length:347
Mass (Da):38,241
Last modified:November 1, 1997 - v3
Checksum:i17014F7621E5EC6B
GO

Sequence cautioni

The sequence CAA31216 differs from that shown. Reason: Frameshift at positions 12 and 304. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti35 – 362RL → LR in CAA31216 (PubMed:2841129).Curated
Sequence conflicti153 – 1531V → G in CAA31216 (PubMed:2841129).Curated
Sequence conflicti170 – 1701G → C in CAA31216 (PubMed:2841129).Curated
Sequence conflicti329 – 3291E → R in CAA31216 (PubMed:2841129).Curated

Mass spectrometryi

Molecular mass is 38246 Da from positions 1 - 347. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12713 Genomic DNA. Translation: CAA31216.1. Frameshift.
U00096 Genomic DNA. Translation: AAC73837.1.
AP009048 Genomic DNA. Translation: BAA35409.1.
PIRiF64810. SYECQA.
RefSeqiNP_415271.1. NC_000913.3.
WP_000115290.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73837; AAC73837; b0750.
BAA35409; BAA35409; BAA35409.
GeneIDi945351.
KEGGiecj:JW0733.
eco:b0750.
PATRICi32116699. VBIEscCol129921_0775.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12713 Genomic DNA. Translation: CAA31216.1. Frameshift.
U00096 Genomic DNA. Translation: AAC73837.1.
AP009048 Genomic DNA. Translation: BAA35409.1.
PIRiF64810. SYECQA.
RefSeqiNP_415271.1. NC_000913.3.
WP_000115290.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP11458.
SMRiP11458. Positions 30-342.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263028. 7 interactions.
DIPiDIP-1027N.
IntActiP11458. 6 interactions.
STRINGi511145.b0750.

Proteomic databases

PaxDbiP11458.
PRIDEiP11458.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73837; AAC73837; b0750.
BAA35409; BAA35409; BAA35409.
GeneIDi945351.
KEGGiecj:JW0733.
eco:b0750.
PATRICi32116699. VBIEscCol129921_0775.

Organism-specific databases

EchoBASEiEB0624.
EcoGeneiEG10630. nadA.

Phylogenomic databases

eggNOGiENOG4105D0I. Bacteria.
COG0379. LUCA.
HOGENOMiHOG000222769.
InParanoidiP11458.
KOiK03517.
OMAiIAHPECE.
PhylomeDBiP11458.

Enzyme and pathway databases

UniPathwayiUPA00253; UER00327.
BioCyciEcoCyc:QUINOLINATE-SYNTHA-MONOMER.
ECOL316407:JW0733-MONOMER.
MetaCyc:QUINOLINATE-SYNTHA-MONOMER.

Miscellaneous databases

PROiP11458.

Family and domain databases

HAMAPiMF_00567. NadA_type1. 1 hit.
InterProiIPR003473. NadA.
IPR023513. Quinolinate_synth_A_type1.
[Graphical view]
PfamiPF02445. NadA. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00550. nadA. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiNADA_ECOLI
AccessioniPrimary (citable) accession number: P11458
Secondary accession number(s): P77373
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: November 1, 1997
Last modified: September 7, 2016
This is version 135 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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. 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.