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Reviewed, UniProtKB/Swiss-Prot Q9JTX9 (ARGD_NEIMA)

Last modified June 16, 2009. Version 58. 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:
    Acetylornithine aminotransferase
      Short name=ACOAT
    EC=2.6.1.11
Gene names
Name: argD
Ordered Locus Names: NMA1584
OrganismNeisseria meningitidis serogroup A [Complete proteome] [HAMAP]
Taxonomic identifier65699 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

Protein attributes

Sequence length397 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + L-glutamate. HAMAP MF_01107

Cofactor

Binds 1 pyridoxal phosphate per subunit By similarity.

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 4/4. HAMAP MF_01107

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm Probable.

Miscellaneous

May also have succinyldiaminopimelate aminotransferase activity, thus carrying out the corresponding step in lysine biosynthesis. HAMAP MF_01107

Sequence similarities

Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Arginine biosynthesis
   Cellular componentCytoplasm
   LigandPyridoxal phosphate
   Molecular functionAminotransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processarginine biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionN2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity

Inferred from electronic annotation. Source: HAMAP

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 397397Acetylornithine aminotransferase HAMAP MF_01107
PRO_0000112759

Regions

Region214 – 2174Pyridoxal phosphate binding By similarity

Sites

Binding site1291Pyridoxal phosphate; via carbonyl oxygen By similarity
Binding site1321N(2)-acetyl-L-ornithine By similarity
Binding site2711N(2)-acetyl-L-ornithine By similarity
Binding site2721Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2431N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9JTX9-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: BE4DB264C16144D8

FASTA39742,547
        10         20         30         40         50         60 
MQNYLTPNFA FAPMIPERAS GSRVWDTEGR EYIDFSGGIA VNALGHCHPA LVDALNAQMH 

        70         80         90        100        110        120 
KLWHISNIYT TRPAQELAQK LVANSFADKV FFCNSGSEAN EAALKLARKY ARDRFGGGKS 

       130        140        150        160        170        180 
EIVACINSFH GRTLFTVSVG GQPKYSKDYA PLPQGITHVP FNDIAALEAA VGEQTCAVII 

       190        200        210        220        230        240 
EPIQGESGIL PATAEYLQTA RRLCDRHNAL LILDEVQTGM GHTGRLFAYE HYGVVPDILS 

       250        260        270        280        290        300 
SAKALGCGFP IGAMLATETI AAAFQPGTHG STFGGNPMAC AVGSRAFDII NAPETLHNVR 

       310        320        330        340        350        360 
SQGQKLQTAL LDLGRKTGLF SQVRGMGLLL GCVLDAPYRG RASEITAAAL KHGVMILVAG 

       370        380        390 
ADVLRFAPSL LLNDEDTAEG LRRLEHVLTE FAAANRP 

« Hide

Cross-references

Sequence databases

AL157959 Genomic DNA. Translation: CAM08728.1.
PIRC81851.
RefSeqYP_002342900.1.

3D structure databases

HSSPHSSP built from PDB template 1QJ3 based on UniProtKB P12995.
ModBaseSearch...

Genome annotation databases

GeneID907972.
GenomeReviewsGene locus NMA1584 in contig AL157959_GR.
KEGGnma:NMA1584.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ9JTX9.
OMAQ9JTX9. NAISARY.

Enzyme and pathway databases

BioCycNMEN122587:NMA1584-MON.
BRENDA2.6.1.11. 292829.

Family and domain databases

HAMAPMF_01107.
[Tree]
InterProIPR005814. Aminotrans_3.
IPR004636. ArgD_aminotrans.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR017652. SuccinylOrn_transaminase.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
PANTHERPTHR11986. Aminotrans_3. 1 hit.
PTHR11986:SF19. ArgD_aminotrans. 1 hit.
PfamPF00202. Aminotran_3. 1 hit.
[Graphical view]
TIGRFAMsTIGR03246. arg_catab_astC. 1 hit.
TIGR00707. argD. 1 hit.
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameARGD_NEIMA
AccessionPrimary (citable) accession number: Q9JTX9
Secondary accession number(s): A1ISH2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 12, 2003
Last sequence update: October 1, 2000
Last modified: June 16, 2009
This is version 58 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