O25910 (NADA_HELPY) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Quinolinate synthase A
EC=2.5.1.72

Gene names

Name:	nadA
Ordered Locus Names:	HP_1356

Organism

Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori) [Reference proteome] [HAMAP]

Taxonomic identifier

85962 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › delta/epsilon subdivisions › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter › Helicobacter pylori

Protein attributes

Sequence length	336 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate By similarity. HAMAP-Rule MF_00569
Catalytic activity	Glycerone phosphate + iminosuccinate = pyridine-2,3-dicarboxylate + 2 H2O + phosphate. HAMAP-Rule MF_00569
Cofactor	Binds 1 4Fe-4S cluster per subunit By similarity.
Pathway	Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from iminoaspartate: step 1/1. HAMAP-Rule MF_00569
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the quinolinate synthase A family. Type 3 subfamily.

Ontologies

Keywords
Biological process	Pyridine nucleotide biosynthesis
Cellular component	Cytoplasm
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding
Molecular function	Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	NAD biosynthetic process Inferred from electronic annotation. Source: HAMAP quinolinate biosynthetic process Inferred from electronic annotation. Source: GOC
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW quinolinate synthetase A activity Inferred from electronic annotation. Source: HAMAP transferase activity, transferring alkyl or aryl (other than methyl) groups Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 336	336	Quinolinate synthase A HAMAP-Rule MF_00569		PRO_0000155818
Sites
	Binding site	25	1	Iminoaspartate By similarity
	Binding site	42	1	Iminoaspartate; via amide nitrogen By similarity
	Binding site	117	1	Iminoaspartate By similarity
	Binding site	138	1	Iminoaspartate By similarity
	Binding site	224	1	Iminoaspartate By similarity
	Binding site	241	1	Iminoaspartate By similarity

Sequences

	Sequence		Length	Mass (Da)
	O25910 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 963569A848239C4F	FASTA	336	37,813
	10 20 30 40 50 60 MPTDNDLKAA ILELLRDLDV LLVAHFYQKD EIVELAHYTG DSLELAKIAS QSDKNLIVFC 70 80 90 100 110 120 GVHFMGESVK ALAFDKQVIM PKLSCCSMAR MIDSHYYDRS VHLLKECGVK EFYPITYINS 130 140 150 160 170 180 NAEVKAKVAK DDGVVCTSRN ASKIFNHALK QNKKIFFLPD KCLGENLALE NGLKSAILGA 190 200 210 220 230 240 NSQEEIKNAD VVCYNGFCSV HQLFKLEDIE FYRQKYPDIL IAVHPECEPS VVSNADFSGS 250 260 270 280 290 300 TSQIIEFVEK LSPNQKVAIG TESHLVNRLK AKRHHQNTFI LSSTLALCPT MNETTLKDLF 310 320 330 EVLKAYKNHR AYNTIELKDE VARLAKLALT KMMELS

References

[1]

"The complete genome sequence of the gastric pathogen Helicobacter pylori." Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A., Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N., Loftus B.J., Richardson D.L., Dodson R.J. , Khalak H.G., Glodek A., McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E., Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D., Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S., Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C. Nature 388:539-547(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700392 / 26695.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000511 Genomic DNA. Translation: AAD08398.1.
PIR	D64689.
RefSeq	NP_208148.1. NC_000915.1. YP_006935278.1. NC_018939.1.
3D structure databases
ProteinModelPortal	O25910.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-3397N.
MINT	MINT-168022.
STRING	85962.HP1356.
Protocols and materials databases
DNASU	900347.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAD08398; AAD08398; HP_1356.
GeneID	13870565. 900347.
KEGG	heo:C694_07000. hpy:HP1356.
PATRIC	20594099. VBIHelPyl33062_1420.
Phylogenomic databases
eggNOG	COG0379.
KO	K03517.
OMA	DKCLGEN.
ProtClustDB	PRK09375.
Enzyme and pathway databases
UniPathway	UPA00253; UER00327.
Family and domain databases
HAMAP	MF_00569. NadA_type3.
InterPro	IPR003473. NadA. IPR023515. Quinolinate_synth_A_type3. [Graphical view]
Pfam	PF02445. NadA. 1 hit. [Graphical view]
TIGRFAMs	TIGR00550. nadA. 1 hit.
ProtoNet	Search...

Entry information

Entry name

NADA_HELPY

Accession

Primary (citable) accession number: O25910

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 25, 2002
Last sequence update:	January 1, 1998
Last modified:	May 1, 2013
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program