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Reviewed, UniProtKB/Swiss-Prot P24087 (ARGD_LEPIN)

Last modified June 16, 2009. Version 69. 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: LA_2153
OrganismLeptospira interrogans [Complete proteome] [HAMAP]
Taxonomic identifier173 [NCBI]
Taxonomic lineageBacteria › Spirochaetes › Spirochaetales › Leptospiraceae › Leptospira

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Protein attributes

Sequence length406 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 – 406406Acetylornithine aminotransferase HAMAP MF_01107
PRO_0000112751

Regions

Region113 – 1142Pyridoxal phosphate binding By similarity
Region233 – 2364Pyridoxal phosphate binding By similarity

Sites

Binding site1451Pyridoxal phosphate; via carbonyl oxygen By similarity
Binding site1481N(2)-acetyl-L-ornithine By similarity
Binding site2901N(2)-acetyl-L-ornithine By similarity
Binding site2911Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2621N6-(pyridoxal phosphate)lysine By similarity

Experimental info

Sequence conflict3581K → R in AAA72087. Ref.2
Sequence conflict367 – 40640AGLVV…VLKQN → QGS in AAA72087. Ref.2

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Sequences

Sequence LengthMass (Da)Tools
P24087-1 [UniParc].

Last modified December 6, 2002. Version 2.
Checksum: 5AB51966B5062614

FASTA40644,866
        10         20         30         40         50         60 
MNDADIHKEL FQHTKELADH YLLNTYARYD VAFRYGVNEL LFDFDNKQYI DFHCGVAVTN 

        70         80         90        100        110        120 
LGHADPDIIE VVRSQADKLF HTSNLFYSEE ASKLAELLIL NSFPGKVFLT NSGTEAIEGA 

       130        140        150        160        170        180 
FKLARKYAYS KSIVDPIILS LEKSFHGRSV SGMSLTGQDK IRKGYGELLK GIEFIEPNND 

       190        200        210        220        230        240 
EALVAAFERY QGRIVALIEE PILGESGIIP LSRNFLTLSR ELTEENEALL IFDEIQTGMG 

       250        260        270        280        290        300 
RTGTLFAFET MGFSPDAMTL AKGLGSGFPI GALIVGEKYQ DLFTQGSHGS TFGGNHLAAA 

       310        320        330        340        350        360 
VAYETIRIIQ TREILNNVNI CSDIAFTRLR EMQEKYPVIS EVRGKGLHIG LELKVPSKPI 

       370        380        390        400 
AEACLSAGLV VNATADNVVR IMPPLTISTD FLNQGLDILE SVLKQN

« Hide

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References

« Hide 'large scale' references
[1]"Unique physiological and pathogenic features of Leptospira interrogans revealed by whole-genome sequencing."
Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X., Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X., Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H. expand/collapse author list , Yin H.-F., Zhang Y., Zhu G.-F., Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y., Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I., Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.
Nature 422:888-893(2003) [PubMed: 12712204] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 56601 / Serogroup Icterohaemorrhagiae / Serovar lai.
[2]"Cloning and analysis of the leuB gene of Leptospira interrogans serovar pomona."
Ding M., Yelton D.B.
J. Gen. Microbiol. 139:1093-1103(1993) [PubMed: 8336106] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 239-406.
Strain: Kenniwicki / Serogroup Pomona / Serovar pomona.

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Cross-references

Sequence databases

AE010300 Genomic DNA. Translation: AAN49352.1.
M59431 Unassigned DNA. Translation: AAA72087.1.
RefSeqNP_712334.1.

3D structure databases

HSSPHSSP built from PDB template 2DKB based on UniProtKB P16932.
ModBaseSearch...

Genome annotation databases

GeneID1151496.
GenomeReviewsGene locus LA_2153 in contig AE010300_GR.
KEGGlil:LA2153.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP24087.
OMAP24087. EHIDEMS.

Enzyme and pathway databases

BioCycLINT-130-01:LINT-130-01-001719-MON.
LINT189518:LA2153-MON.
BRENDA2.6.1.11. 258108.

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]
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameARGD_LEPIN
AccessionPrimary (citable) accession number: P24087
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: December 6, 2002
Last modified: June 16, 2009
This is version 69 of the entry and version 2 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