B2UAP5 (NADA_RALPJ) 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:	Rpic_2717

Organism

Ralstonia pickettii (strain 12J) [Complete proteome] [HAMAP]

Taxonomic identifier

402626 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Ralstonia › Burkholderia pickettii

Protein attributes

Sequence length	382 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_00567
Catalytic activity	Glycerone phosphate + iminosuccinate = pyridine-2,3-dicarboxylate + 2 H2O + phosphate. HAMAP-Rule MF_00567
Cofactor	Binds 1 4Fe-4S cluster per subunit By similarity.
Pathway	Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from iminoaspartate: step 1/1. HAMAP-Rule MF_00567
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the quinolinate synthase A family. Type 1 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
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 – 382	382	Quinolinate synthase A HAMAP-Rule MF_00567		PRO_1000129421
Sites
	Binding site	63	1	Iminoaspartate By similarity
	Binding site	84	1	Iminoaspartate; via amide nitrogen By similarity
	Binding site	155	1	Iminoaspartate By similarity
	Binding site	172	1	Iminoaspartate By similarity
	Binding site	242	1	Iminoaspartate By similarity
	Binding site	259	1	Iminoaspartate By similarity

Sequences

	Sequence		Length	Mass (Da)
	B2UAP5 [UniParc]. Last modified July 1, 2008. Version 1. Checksum: F30923B3576E56A5	FASTA	382	41,479
	10 20 30 40 50 60 METHIKTVEF ERPDMLSEAQ SGASCVAHAW AKVPPVLSRE ERDELKARIK RLLKEREAVL 70 80 90 100 110 120 VAHYYVDADL QDLAEETGGC VSDSLEMARF GRDHSAKTLI VAGVRFMGET AKILSPEKTV 130 140 150 160 170 180 LMPDLDATCS LDLGCPPDEF AAFCDAHPDR TVVVYANTSA AVKARADWMV TSSIGLKIVQ 190 200 210 220 230 240 HLHAQGKKIL WAPDRHLGSY IQKQTGADML MWQGSCLVHD EFKGVELDLL RAEHPNAKIL 250 260 270 280 290 300 VHPESPESVV AQADVVGSTS QLIAAAQSLS AQEFIVATDN GILHKMRMAA PGKRFIEAPT 310 320 330 340 350 360 AGNAATCKSC AHCPWMAMNA LTNLAEVLET GRNEIHVDPA IGRQAVVCID RMLDFAAREK 370 380 ATVRPQGDLA ANAQLFQGIG PA

References

[1]

"Complete sequence of chromosome 1 of Ralstonia pickettii 12J." Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. , Kyrpides N., Mikhailova N., Marsh T., Richardson P. Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 12J.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001068 Genomic DNA. Translation: ACD27842.1.
RefSeq	YP_001900274.1. NC_010682.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	402626.Rpic_2717.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ACD27842; ACD27842; Rpic_2717.
GeneID	6289101.
KEGG	rpi:Rpic_2717.
PATRIC	20256240. VBIRalPic63053_3853.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0379.
HOGENOM	HOG000222769.
KO	K03517.
OMA	GCPADEF.
ProtClustDB	PRK09375.
Enzyme and pathway databases
BioCyc	RPIC402626:GH94-2846-MONOMER.
UniPathway	UPA00253; UER00327.
Family and domain databases
HAMAP	MF_00567. NadA_type1.
InterPro	IPR003473. NadA. IPR023513. Quinolinate_synth_A_type1. [Graphical view]
Pfam	PF02445. NadA. 1 hit. [Graphical view]
TIGRFAMs	TIGR00550. nadA. 1 hit.
ProtoNet	Search...

Entry information

Entry name

NADA_RALPJ

Accession

Primary (citable) accession number: B2UAP5

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	July 1, 2008
Last modified:	May 1, 2013
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program