Reviewed, UniProtKB/Swiss-Prot Q9X8N8 (NADB_STRCO)

Names and origin

Protein names

Recommended name:
    L-aspartate oxidase
      Short name=LASPO
    EC=1.4.3.16
Alternative name(s):
    Quinolinate synthetase B

Gene names

Name:	nadB
Ordered Locus Names:	SCO3382
ORF Names:	SCE94.33c

Organism

Streptomyces coelicolor [Complete proteome] [HAMAP]

Taxonomic identifier

1902 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length	580 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes the oxidation of L-aspartate to iminoaspartate.
Catalytic activity	L-aspartate + H(2)O + O(2) = oxaloacetate + NH(3) + H(2)O(2).
Cofactor	FAD.
Pathway	Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (oxidase route): step 1/1.
Subcellular location	CytoplasmBy similarity.
Sequence similarities	Belongs to the FAD-dependent oxidoreductase 2 family. NadB subfamily.

Ontologies

Keywords
Biological process	Pyridine nucleotide biosynthesis
Cellular component	Cytoplasm
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 580	580	L-aspartate oxidase		PRO_0000184401
Regions
	Nucleotide binding	22 – 36	15	FAD Potential
Sites
	Active site	248	1	By similarity
	Active site	270	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9X8N8-1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: CA8E4026CC1AF7D4	FASTA	580	61,274
	10 20 30 40 50 60 MTSTGIRLHA PAPGWAIAAD VVVVGSGVAG LTAALRCESA GLRTVVVTKA RLDDGSTRWA 70 80 90 100 110 120 QGGVAAALGE GDTPEQHLDD TLVAGAGLCD QDAVRILVTE GPDAVRRLIA TGAHFDESTE 130 140 150 160 170 180 GGLALTREGG HHRRRIAHAG GDATGAEISR ALVEAVRARG LRTVENALVL DLLTDAEGRT 190 200 210 220 230 240 AGVTLHVMGE GQHDGVGAVH APAVVLATGG MGQVFSATTN PSVSTGDGVA LALRAGAEVS 250 260 270 280 290 300 DLEFVQFHPT VLFLGSDAEG QQPLVSEAVR GEGAHLVDAD GVRFMQGRHE LAELAPRDIV 310 320 330 340 350 360 AKAITRRMQE HGADHMYLDA RHFGRTMWEH RFPTILAACR AHGIDPVTEP VPVAPAAHYA 370 380 390 400 410 420 SGGVRTDAHG RTTVPGLYAC GEVACTGVHG ANRLASNSLL EGLVYAERIA ADIAAAHTAG 430 440 450 460 470 480 TLHARVPAPL PHPDHSQHPR HPLLPPEARL TIQRIMTEGA GVLRSADSLA RAADRLHGLH 490 500 510 520 530 540 AEAREALHEH GKTSEPGVDT WEATNLLCVA RVLVAAAARR EETRGCHWRE DHADRDDTTW 550 560 570 580 RRHVVVRLNP DRTLAVHTTD TPEFPPTVHG AQPTHRPQEQ

References

[1]

"Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2)." Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L., Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A., Fraser A., Goble A. , Hidalgo J., Hornsby T., Howarth S., Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A. Nature 417:141-147(2002) [PubMed: 12000953] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-471 / A3(2) / M145.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL939116 Genomic DNA. Translation: CAB40882.1.
PIR	T36393.
RefSeq	NP_627590.1.
3D structure databases
HSSP	HSSP built from PDB template 1CHU based on UniProtKB P10902.
ModBase	Search...
Genome annotation databases
GeneID	1098819.
GenomeReviews	Gene locus SCO3382 in contig AL645882_GR.
KEGG	sco:SCO3382.
NMPDR	fig|100226.1.peg.3342.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q9X8N8.
Enzyme and pathway databases
BioCyc	SCOE100226:SCO3382-MON.
Family and domain databases
InterPro	IPR003953. FAD_bind2_N. IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR004112. Fum_Rdtase/Succ_DHase_flav_C. IPR005288. NadB. IPR001100. Pyr_nuc-diS_OxRdtase. [Graphical view]
Pfam	PF00890. FAD_binding_2. 1 hit. PF02910. Succ_DH_flav_C. 1 hit. [Graphical view]
PRINTS	PR00368. FADPNR. PR00411. PNDRDTASEI.
TIGRFAMs	TIGR00551. nadB. 1 hit.
BLOCKS	Search...
ProtoNet	Search...

Entry information

Entry name

NADB_STRCO

Accession

Primary (citable) accession number: Q9X8N8

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2002
Last sequence update:	November 1, 1999
Last modified:	November 4, 2008
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)