UniProtKB - P11458 (NADA_ECOLI)
Protein
Quinolinate synthase A
Gene
nadA
Organism
Escherichia coli (strain K12)
Status
Functioni
Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate.3 Publications
Catalytic activityi
- EC:2.5.1.72
Cofactori
[4Fe-4S] cluster2 PublicationsNote: Binds 1 [4Fe-4S] cluster per subunit.2 Publications
Activity regulationi
Activity is greater under oxic conditions and is regulated by a redox-active disulfide bond.
: NAD(+) biosynthesis Pathwayi
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:
- Quinolinate synthase A (nadA), Quinolinate synthase A (nadA)
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 47 | IminoaspartateBy similarity | 1 | |
Binding sitei | 68 | Iminoaspartate; via amide nitrogenBy similarity | 1 | |
Binding sitei | 139 | IminoaspartateBy similarity | 1 | |
Binding sitei | 156 | IminoaspartateBy similarity | 1 | |
Binding sitei | 226 | IminoaspartateBy similarity | 1 | |
Binding sitei | 243 | IminoaspartateBy similarity | 1 |
GO - Molecular functioni
- 4 iron, 4 sulfur cluster binding Source: EcoCyc
- metal ion binding Source: UniProtKB-KW
- quinolinate synthetase A activity Source: EcoCyc
GO - Biological processi
- 'de novo' NAD biosynthetic process from aspartate Source: EcoCyc
Keywordsi
Molecular function | Transferase |
Biological process | Pyridine nucleotide biosynthesis |
Ligand | 4Fe-4S, Iron, Iron-sulfur, Metal-binding |
Enzyme and pathway databases
BioCyci | EcoCyc:QUINOLINATE-SYNTHA-MONOMER MetaCyc:QUINOLINATE-SYNTHA-MONOMER |
UniPathwayi | UPA00253;UER00327 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:nadA Synonyms:nicA Ordered Locus Names:b0750, JW0733 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
Cytoplasm and Cytosol
Cytosol
- cytosol Source: EcoCyc
Keywords - Cellular componenti
CytoplasmPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 291 | C → S: Activity is 3.3-fold lower under oxic conditions than under anoxic conditions. 1 Publication | 1 | |
Mutagenesisi | 294 | C → S: Activity is 13-fold lower under oxic conditions than under anoxic conditions. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000155760 | 1 – 347 | Quinolinate synthase AAdd BLAST | 347 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 291 ↔ 294 | Redox-active |
Keywords - PTMi
Disulfide bondProteomic databases
jPOSTi | P11458 |
PaxDbi | P11458 |
PRIDEi | P11458 |
Interactioni
Subunit structurei
Homodimer.
1 PublicationProtein-protein interaction databases
BioGRIDi | 4263028, 14 interactors 849727, 2 interactors |
DIPi | DIP-1027N |
IntActi | P11458, 6 interactors |
STRINGi | 511145.b0750 |
Family & Domainsi
Sequence similaritiesi
Keywords - Domaini
Redox-active centerPhylogenomic databases
eggNOGi | COG0379, Bacteria |
HOGENOMi | CLU_047382_1_0_6 |
InParanoidi | P11458 |
PhylomeDBi | P11458 |
Family and domain databases
Gene3Di | 3.40.50.10800, 3 hits |
HAMAPi | MF_00567, NadA_type1, 1 hit |
InterProi | View protein in InterPro IPR003473, NadA IPR036094, NadA_sf IPR023513, Quinolinate_synth_A_type1 |
PANTHERi | PTHR30573, PTHR30573, 1 hit |
Pfami | View protein in Pfam PF02445, NadA, 1 hit |
SUPFAMi | SSF142754, SSF142754, 1 hit |
TIGRFAMsi | TIGR00550, nadA, 1 hit |
i Sequence
Sequence statusi: Complete.
P11458-1 [UniParc]FASTAAdd to basket
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
Sequence cautioni
The sequence CAA31216 differs from that shown. Reason: Frameshift.Curated
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 35 – 36 | RL → LR in CAA31216 (PubMed:2841129).Curated | 2 | |
Sequence conflicti | 153 | V → G in CAA31216 (PubMed:2841129).Curated | 1 | |
Sequence conflicti | 170 | G → C in CAA31216 (PubMed:2841129).Curated | 1 | |
Sequence conflicti | 329 | E → R in CAA31216 (PubMed:2841129).Curated | 1 |
Mass spectrometryi
Molecular mass is 38246 Da. 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 |
PIRi | F64810, SYECQA |
RefSeqi | NP_415271.1, NC_000913.3 WP_000115290.1, NZ_SSZK01000002.1 |
Genome annotation databases
EnsemblBacteriai | AAC73837; AAC73837; b0750 BAA35409; BAA35409; BAA35409 |
GeneIDi | 57728455 945351 |
KEGGi | ecj:JW0733 eco:b0750 |
PATRICi | fig|1411691.4.peg.1529 |
Similar proteinsi
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 |
PIRi | F64810, SYECQA |
RefSeqi | NP_415271.1, NC_000913.3 WP_000115290.1, NZ_SSZK01000002.1 |
3D structure databases
SMRi | P11458 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 4263028, 14 interactors 849727, 2 interactors |
DIPi | DIP-1027N |
IntActi | P11458, 6 interactors |
STRINGi | 511145.b0750 |
Proteomic databases
jPOSTi | P11458 |
PaxDbi | P11458 |
PRIDEi | P11458 |
Genome annotation databases
EnsemblBacteriai | AAC73837; AAC73837; b0750 BAA35409; BAA35409; BAA35409 |
GeneIDi | 57728455 945351 |
KEGGi | ecj:JW0733 eco:b0750 |
PATRICi | fig|1411691.4.peg.1529 |
Organism-specific databases
EchoBASEi | EB0624 |
Phylogenomic databases
eggNOGi | COG0379, Bacteria |
HOGENOMi | CLU_047382_1_0_6 |
InParanoidi | P11458 |
PhylomeDBi | P11458 |
Enzyme and pathway databases
UniPathwayi | UPA00253;UER00327 |
BioCyci | EcoCyc:QUINOLINATE-SYNTHA-MONOMER MetaCyc:QUINOLINATE-SYNTHA-MONOMER |
Miscellaneous databases
PROi | PR:P11458 |
Family and domain databases
Gene3Di | 3.40.50.10800, 3 hits |
HAMAPi | MF_00567, NadA_type1, 1 hit |
InterProi | View protein in InterPro IPR003473, NadA IPR036094, NadA_sf IPR023513, Quinolinate_synth_A_type1 |
PANTHERi | PTHR30573, PTHR30573, 1 hit |
Pfami | View protein in Pfam PF02445, NadA, 1 hit |
SUPFAMi | SSF142754, SSF142754, 1 hit |
TIGRFAMsi | TIGR00550, nadA, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | NADA_ECOLI | |
Accessioni | P11458Primary (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: | February 10, 2021 | |
This is version 164 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Direct protein sequencing, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families