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Reviewed, UniProtKB/Swiss-Prot Q81M98 (ARGD_BACAN)

Last modified February 9, 2010. 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

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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: BA_4352, GBAA_4352, BAS4037
OrganismBacillus anthracis [Complete proteome] [HAMAP]
Taxonomic identifier1392 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

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Protein attributes

Sequence length386 AA.
Sequence statusComplete.
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. HAMAP MF_01107

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. HAMAP MF_01107

Subcellular location

Cytoplasm Probable HAMAP MF_01107.

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 – 386386Acetylornithine aminotransferase HAMAP MF_01107
PRO_0000112716

Regions

Region208 – 2114Pyridoxal phosphate binding By similarity

Sites

Binding site1231Pyridoxal phosphate; via carbonyl oxygen By similarity
Binding site1261N(2)-acetyl-L-ornithine By similarity
Binding site2651N(2)-acetyl-L-ornithine By similarity
Binding site2661Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue2371N6-(pyridoxal phosphate)lysine By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q81M98-1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 24C581C59564DE0C

FASTA38642,179
        10         20         30         40         50         60 
MISHLFQTYG RRTVEFVKGN GTKVIDNNGK QYLDFTSGIG VCNLGHCHPT VMKAVQEQLN 

        70         80         90        100        110        120 
DIWHISNLFT NSLQEEVASL LTENIALDYV FFCNSGAEAN EAALKLARKH TGKSLVVTCE 

       130        140        150        160        170        180 
QSFHGRTFGT MSATGQNKVK EGFGPLLPSF LHTPFNDIKA LKEVMNEEVA AVMVEVVQGE 

       190        200        210        220        230        240 
GGVIPADLSF LKEIETLCKK FGSLFIIDEV QTGIGRTGTL FAYEQMGIDP HIVTTAKALG 

       250        260        270        280        290        300 
NGIPVGAMIG RKELGTSFTA GSHGSTFGGN YVAMAAAKEV LQVSKRLSFL KEVQEKGEYV 

       310        320        330        340        350        360 
LQKLQEELQH VECIQNIRGK GLMVGIECTH EVASFIEQLE KEGLLVLQAG PNVIRLLPPL 

       370        380 
IVTNEELEQA VYMIKKVVCT KNVSII

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References

[1]"The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria."
Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. expand/collapse author list , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.
Nature 423:81-86(2003) [PubMed: 12721629] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames / isolate Porton.
[2]"Bacillus anthracis comparative genomics."
Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames ancestor.
[3]"Complete genome sequence of Bacillus anthracis Sterne."
Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sterne.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE016879 Genomic DNA. Translation: AAP28070.1.
AE017334 Genomic DNA. Translation: AAT35422.1.
AE017225 Genomic DNA. Translation: AAT56338.1. Different initiation.
RefSeqNP_846584.1.
YP_022688.1.
YP_030287.2.

3D structure databases

SMRQ81M98. Positions 4-378.
ModBaseSearch...

Genome annotation databases

GeneID1087573.
2816449.
2850294.
GenomeReviewsGene locus BA_4352 in contig AE016879_GR.
Gene locus BAS4037 in contig AE017225_GR.
Gene locus GBAA_4352 in contig AE017334_GR.
KEGGban:BA4352.
bar:GBAA4352.
bat:BAS4037.
TIGRBA_4352.
GBAA_4352.

Phylogenomic databases

HOGENOMHBG725944.
OMAHIVTTAK.

Enzyme and pathway databases

BioCycBANT260799:BAS4037-MONOMER.
BANT261594:GBAA4352-MONOMER.
BRENDA2.6.1.11. 267517.

Family and domain databases

HAMAPMF_01107. ArgD_aminotrans_3.
[Tree]
InterProIPR004636. AcOrn/succinylOrn_aminoTrfase.
IPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase_major_dom.
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_BACAN
AccessionPrimary (citable) accession number: Q81M98
Secondary accession number(s): Q6HTQ1, Q6KIZ6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: June 1, 2003
Last modified: February 9, 2010
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)

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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