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Reviewed, UniProtKB/Swiss-Prot P63568 (ARGD_MYCTU)

Last modified June 16, 2009. Version 35. 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

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Names and origin

Protein namesRecommended name:
    Acetylornithine aminotransferase
      Short name=ACOAT
    EC=2.6.1.11
Gene names
Name: argD
Ordered Locus Names: Rv1655, MT1693
ORF Names: MTCY06H11.20
OrganismMycobacterium tuberculosis [Complete proteome] [HAMAP]
Taxonomic identifier1773 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

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Protein attributes

Sequence length400 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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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.

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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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 400400Acetylornithine aminotransferase HAMAP MF_01107
PRO_0000112756

Regions

Region224 – 2274Pyridoxal phosphate binding By similarity

Sites

Binding site1391Pyridoxal phosphate; via carbonyl oxygen By similarity
Binding site1421N(2)-acetyl-L-ornithine By similarity
Binding site2811N(2)-acetyl-L-ornithine By similarity
Binding site2821Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2531N6-(pyridoxal phosphate)lysine By similarity

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Sequences

Sequence LengthMass (Da)Tools
P63568-1 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 833846D529795019

FASTA40040,910
        10         20         30         40         50         60 
MTGASTTTAT MRQRWQAVMM NNYGTPPIAL ASGDGAVVTD VDGRTYIDLL GGIAVNVLGH 

        70         80         90        100        110        120 
RHPAVIEAVT RQMSTLGHTS NLYATEPGIA LAEELVALLG ADQRTRVFFC NSGAEANEAA 

       130        140        150        160        170        180 
FKLSRLTGRT KLVAAHDAFH GRTMGSLALT GQPAKQTPFA PLPGDVTHVG YGDVDALAAA 

       190        200        210        220        230        240 
VDDHTAAVFL EPIMGESGVV VPPAGYLAAA RDITARRGAL LVLDEVQTGM GRTGAFFAHQ 

       250        260        270        280        290        300 
HDGITPDVVT LAKGLGGGLP IGACLAVGPA AELLTPGLHG STFGGNPVCA AAALAVLRVL 

       310        320        330        340        350        360 
ASDGLVRRAE VLGKSLRHGI EALGHPLIDH VRGRGLLLGI ALTAPHAKDA EATARDAGYL 

       370        380        390        400 
VNAAAPDVIR LAPPLIIAEA QLDGFVAALP AILDRAVGAP

« Hide

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Cross-references

Sequence databases

BX842577 Genomic DNA. Translation: CAB06649.1.
AE000516 Genomic DNA. Translation: AAK45962.1.
PIRB70621.
RefSeqNP_216171.1.
NP_336148.1.

3D structure databases

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

Genome annotation databases

GeneID885187.
925079.
GenomeReviewsGene locus MT1693 in contig AE000516_GR.
Gene locus Rv1655 in contig AL123456_GR.
KEGGmtc:MT1693.
mtu:Rv1655.
TIGRMT1693.

Organism-specific databases

TubercuListRv1655.

Phylogenomic databases

HOGENOMP63568.
OMAP63568. PIQGENG.

Enzyme and pathway databases

BRENDA2.6.1.11. 809.

Family and domain databases

HAMAPMF_01107.
[Tree]
InterProIPR005814. Aminotrans_3.
IPR004636. ArgD_aminotrans.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[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]
TIGRFAMsTIGR00707. argD. 1 hit.
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameARGD_MYCTU
AccessionPrimary (citable) accession number: P63568
Secondary accession number(s): P94990
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: June 16, 2009
This is version 35 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)

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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