Reviewed, UniProtKB/Swiss-Prot Q49617 (NADB_MYCLE)

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:	ML1226
ORF Names:	B1170_C1_167

Organism

Mycobacterium leprae [Complete proteome] [HAMAP]

Taxonomic identifier

1769 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium

Protein attributes

Sequence length	526 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.
Sequence caution	The sequence AAA17059.1 differs from that shown. Reason: Frameshift at position 399.

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	NAD biosynthetic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	L-aspartate oxidase activity Inferred from electronic annotation. Source: InterPro electron carrier activity 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 – 526	526	L-aspartate oxidase		PRO_0000184388
Regions
	Nucleotide binding	13 – 27	15	FAD Potential
Sites
	Active site	234	1	By similarity
	Active site	257	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q49617-1 [UniParc]. Last modified April 27, 2001. Version 2. Checksum: A90A6EC4332C248D	FASTA	526	54,182
	10 20 30 40 50 60 MAVPDWKHAA DVVVIGTGVA GLAAALAAHR AGRNVVVLTK ADQRRGETAT HYAQGGIAVV 70 80 90 100 110 120 LPGSDDSVDA HASDTLAAGA GMCNLDTVYS IVAEGYHAVT ELVGYGARFD ESIPGRWAVT 130 140 150 160 170 180 CEGGHSRRRI VHAGGDATGA EVQRALDHAA DVLDIRTSHL ALRVLHDGTV VNGVSVLNPN 190 200 210 220 230 240 GWGIVSAPSV ILASGGLGHL YGATTNPEGS TGDGIALALW AGVAVSDLEF IQFHPTMLFA 250 260 270 280 290 300 AGTGTGGRRP LVTEAIRGEG AILLDSKGNS VTSGVHPLGD LAPRDVVAAA IDARLKATGD 310 320 330 340 350 360 SCVYLDARGI DGFASRFPTV TAACRTVGID PAREPIPVVP GAHYSCGGIV TDAYGQTELA 370 380 390 400 410 420 GLFAAGEVAR TGMHGANRLA SNSLLEGLVV GGRAGRAAAA HAAAAGRAYV SKLEPVTHHA 430 440 450 460 470 480 LKRRELQRVM SRDAAVMRNA AGLQRLSDTL AEAPIRHVTG RRDFEDVALT LTARAVAAAA 490 500 510 520 LARNESRGCH HCTEYPDTAP EHARSTVIRL ADDQNLVRAE ALATVG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Smith D.R., Robison K. Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Massive gene decay in the leprosy bacillus." Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R., Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E., Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K., Duthoy S. , Feltwell T., Fraser A., Hamlin N., Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S., Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R., Barrell B.G. Nature 409:1007-1011(2001) [PubMed: 11234002] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: TN.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U00010 Genomic DNA. Translation: AAA17059.1. Frameshift. AL583921 Genomic DNA. Translation: CAC31607.1. Different initiation.
PIR	D87062. S72695.
RefSeq	NP_301888.1.
3D structure databases
HSSP	HSSP built from PDB template 1CHU based on UniProtKB P10902.
ModBase	Search...
Genome annotation databases
GeneID	910334.
GenomeReviews	Gene locus ML1226 in contig AL450380_GR.
KEGG	mle:ML1226.
NMPDR	fig|272631.1.peg.760.
Organism-specific databases
Leproma	ML1226.
CMR	Search...
Phylogenomic databases
HOGENOM	Q49617.
Enzyme and pathway databases
BioCyc	MLEP272631:ML1226-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.
ProtoNet	Search...

Entry information

Entry name

NADB_MYCLE

Accession

Primary (citable) accession number: Q49617
Secondary accession number(s): Q9CC64

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	April 27, 2001
Last modified:	November 25, 2008
This is version 59 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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