Skip Header

Contribute Send feedback
Read comments (?) or add your own

A9L1C6 (A9L1C6_SHEB9) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Quinolinate synthase A HAMAP-Rule MF_00567
EC=2.5.1.72 HAMAP-Rule MF_00567
Gene names
Name:nadA HAMAP-Rule MF_00567
Ordered Locus Names:Sbal195_2202 EMBL ABX49371.1
OrganismShewanella baltica (strain OS195) [Complete proteome] [HAMAP] EMBL ABX49371.1
Taxonomic identifier399599 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Shewanellaceae › Shewanella ›

Protein attributes

Sequence length360 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate By similarity. HAMAP-Rule MF_00567 SAAS SAAS003473

Catalytic activity

Glycerone phosphate + iminosuccinate = pyridine-2,3-dicarboxylate + 2 H2O + phosphate. HAMAP-Rule MF_00567 SAAS SAAS003473

Cofactor

Binds 1 4Fe-4S cluster per subunit By similarity. HAMAP-Rule MF_00567 SAAS SAAS003473

Pathway

Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from iminoaspartate: step 1/1. HAMAP-Rule MF_00567 SAAS SAAS003473

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00567 SAAS SAAS003473

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00567.

Sequence similarities

Belongs to the quinolinate synthase A family. Type 1 subfamily. HAMAP-Rule MF_00567

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Binding site531Iminoaspartate By similarity HAMAP-Rule MF_00567
Binding site741Iminoaspartate; via amide nitrogen By similarity HAMAP-Rule MF_00567
Binding site1451Iminoaspartate By similarity HAMAP-Rule MF_00567
Binding site1621Iminoaspartate By similarity HAMAP-Rule MF_00567
Binding site2321Iminoaspartate By similarity HAMAP-Rule MF_00567
Binding site2491Iminoaspartate By similarity HAMAP-Rule MF_00567

Sequences

Sequence LengthMass (Da)Tools
A9L1C6 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: C8C9FCD4263299BF

FASTA36039,167
        10         20         30         40         50         60 
MSQFAPSPFA PTIETIDYPF PPKPVPLSDA QKADYKTRIK QLLIEKDAVL VAHYYTDPEI 

        70         80         90        100        110        120 
QALAEETGGC VSDSLEMARF GRDHPAKTLI VAGVKFMGET AKILSPEKTI LMPTLEATCS 

       130        140        150        160        170        180 
LDLGCPIDKF SAFCDAHPDH TVVVYANTSA AVKARADWVV TSSIALEIVE HLDSESKKII 

       190        200        210        220        230        240 
WGPDRHLGSY IAKQTGAEML MWQGDCIVHD EFKSNALRDM KSVYPDAAIL VHPESPANVV 

       250        260        270        280        290        300 
AMADAVGSTS QLIKAAQTMP NERFIVATDR GIFYKMQQAA PGKILIEAPT GGNGATCKSC 

       310        320        330        340        350        360 
AHCPWMAMNG LQAIEASLAD SDKTTHEIFV DEDLRVKALI PLTRMLDFAQ TLNMKVKGNA

« Hide

References

[1]"Complete sequence of chromosome of Shewanella baltica OS195."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E. expand/collapse author list , Brettar I., Rodrigues J., Konstantinidis K., Klappenbach J., Hofle M., Tiedje J., Richardson P.
Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: OS195 EMBL ABX49371.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000891 Genomic DNA. Translation: ABX49371.1.
RefSeqYP_001554631.1. NC_009997.1.

3D structure databases

ProteinModelPortalA9L1C6.
ModBaseSearch...

Protein-protein interaction databases

STRING399599.Sbal195_2202.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABX49371; ABX49371; Sbal195_2202.
GeneID5753955.
KEGGsbn:Sbal195_2202.
PATRIC23470565. VBISheBal33754_2279.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0379.
HOGENOMHOG000222769.
KOK03517.
OMAGCPADEF.
ProtClustDBPRK09375.

Enzyme and pathway databases

BioCycSBAL399599:GH6B-2537-MONOMER.
UniPathwayUPA00253; UER00327.

Family and domain databases

HAMAPMF_00567. NadA_type1.
InterProIPR003473. NadA.
IPR023513. Quinolinate_synth_A_type1.
[Graphical view]
PfamPF02445. NadA. 1 hit.
[Graphical view]
TIGRFAMsTIGR00550. nadA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameA9L1C6_SHEB9
AccessionPrimary (citable) accession number: A9L1C6
Entry history
Integrated into UniProtKB/TrEMBL: February 5, 2008
Last sequence update: February 5, 2008
Last modified: May 1, 2013
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info