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Reviewed, UniProtKB/Swiss-Prot O57765 (NADB_PYRHO)

Last modified November 3, 2009. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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: PH0015
OrganismPyrococcus horikoshii [Complete proteome] [HAMAP]
Taxonomic identifier53953 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length464 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Catalyzes the oxidation of L-aspartate to iminoaspartate.

Catalytic activity

L-aspartate + O2 = iminosuccinate + H2O2.

Cofactor

FAD.

Pathway

Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (oxidase route): step 1/1.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the FAD-dependent oxidoreductase 2 family. NadB subfamily.

Ontologies

Keywords
   Biological processPyridine nucleotide biosynthesis
   Cellular componentCytoplasm
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processNAD biosynthetic process

Inferred from electronic annotation. Source: InterPro

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionL-aspartate oxidase activity

Inferred from electronic annotation. Source: EC

electron carrier activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 464464L-aspartate oxidase
PRO_0000184410

Regions

Nucleotide binding7 – 2115FAD Potential

Sites

Active site2131 By similarity
Active site2301 By similarity

Sequences

Sequence LengthMass (Da)Tools
O57765-1 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 6D5504A7EFAD738D

FASTA46451,296
        10         20         30         40         50         60 
MMEMRVGIVG GGLAGLTAAI ALAEKGFDVS IIGPRSTDSN SYLAQAGIAL PLLEGDSIRI 

        70         80         90        100        110        120 
HVLDTIKAGK YINDEEIVWN VISKSSEAHD FLTSHGVTFT GNELEGGHSY PRIFTIKSET 

       130        140        150        160        170        180 
GKHIIPILEK HARELDVNFI RGFVEEIGIN NGKLAGVFLQ GELLKFDAVV IAAGGFSGLY 

       190        200        210        220        230        240 
RFTAGVKNNI GLLIGDVALK GVPLRDMEFV QFHPTGFIGK RTYLITEAVR GAGAKLVTGD 

       250        260        270        280        290        300 
GERFVNELET RDIVARAIYM KMLEGKGVFL DARGIENFKD RFPYIYSVLR GEGINPEKDL 

       310        320        330        340        350        360 
IPITPVAHYT IGGISVDAFY RTRIKGLYAI GESACNGFHG ANRLASNSLL ECVVSGLEVA 

       370        380        390        400        410        420 
RTISREKPKR EVNDAPYSFN ELGDVDSIRE VLWNHAGIVR DEWSLREGLR KLKEIEVDER 

       430        440        450        460 
LKLVAKAVII SALKREESRG AHYRKDYPFM RKEFEHSSFF YPNV 

« Hide

References

[1]"Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3."
Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S., Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K., Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T. expand/collapse author list , Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T., Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.
DNA Res. 5:55-76(1998) [PubMed: 9679194] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: OT3.

Cross-references

Sequence databases

BA000001 Genomic DNA. Translation: BAA29083.1.
PIRD71219.
RefSeqNP_142038.1.

3D structure databases

HSSPHSSP built from PDB template 1CHU based on UniProtKB P10902.
ModBaseSearch...

Genome annotation databases

GeneID1443917.
GenomeReviewsGene locus PH0015 in contig BA000001_GR.
KEGGpho:PH0015.
NMPDRfig|70601.1.peg.17.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMO57765.
OMANENCETS.

Enzyme and pathway databases

BRENDA1.4.3.16. 74679.

Family and domain databases

InterProIPR003953. FAD_bind2_N.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR004112. Fum_Rdtase/Succ_DH_flav_C.
IPR005288. NadB.
[Graphical view]
PfamPF00890. FAD_binding_2. 1 hit.
PF02910. Succ_DH_flav_C. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
TIGRFAMsTIGR00551. nadB. 1 hit.
ProtoNetSearch...

Entry information

Entry nameNADB_PYRHO
AccessionPrimary (citable) accession number: O57765
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: August 1, 1998
Last modified: November 3, 2009
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents