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A7HDU1 (A7HDU1_ANADF) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Acetylornithine aminotransferase HAMAP-Rule MF_01107
Short name=ACOAT HAMAP-Rule MF_01107
EC=2.6.1.11 HAMAP-Rule MF_01107
Gene names
Name:argD HAMAP-Rule MF_01107
Ordered Locus Names:Anae109_2686
OrganismAnaeromyxobacter sp. (strain Fw109-5) [Complete proteome] [HAMAP] EMBL ABS26887.1
Taxonomic identifier404589 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Deltaproteobacteria › Myxococcales › Cystobacterineae › Myxococcaceae › Anaeromyxobacter

Protein attributes

Sequence length402 AA.
Sequence statusComplete.
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-Rule MF_01107

Cofactor

Binds 1 pyridoxal phosphate per subunit By similarity. HAMAP-Rule MF_01107

Pathway

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

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01107

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01107.

Miscellaneous

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

Sequence similarities

Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily. HAMAP-Rule MF_01107

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region226 – 2294Pyridoxal phosphate binding By similarity HAMAP-Rule MF_01107

Sites

Binding site1411Pyridoxal phosphate; via carbonyl oxygen By similarity HAMAP-Rule MF_01107
Binding site1441N2-acetyl-L-ornithine By similarity HAMAP-Rule MF_01107
Binding site2831N2-acetyl-L-ornithine By similarity HAMAP-Rule MF_01107
Binding site2841Pyridoxal phosphate By similarity HAMAP-Rule MF_01107

Amino acid modifications

Modified residue2551N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01107

Sequences

Sequence LengthMass (Da)Tools
A7HDU1 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: C609C40EE64B0098

FASTA40242,289
        10         20         30         40         50         60 
MTGNNESIAR RAQQVLTPNY RQQPVALVRG EGVRVWDADG NEYLDFLGGV AVNVLGHCHP 

        70         80         90        100        110        120 
ALVKALEEQA RTVWHVSNHY FIPRQVELAE ALLAVTPWAA RAFFCNSGAE ANEAMLKLAR 

       130        140        150        160        170        180 
KHHHDLGHPE RNVIVACDDS FHGRSLFTVT VGGQPKYREG FAPLVPGVRH VPYGDLAALE 

       190        200        210        220        230        240 
AALDDTAAAF IVEPIMGESG VIPAPEGYLK SARELTRRKG ALLCLDEVQT GVGRTGKLWA 

       250        260        270        280        290        300 
HEWAGVTPDL MSSAKSLGGG FPIGALLASE EVGQHLSAGS HGSTYGGNPL GCAVALAVLA 

       310        320        330        340        350        360 
ELKGGVLERS REVGARLRAG LERLAAGGRV ASVRGRGMLL AVVVKGVSAA EVMKAARARG 

       370        380        390        400 
LIVNAIGEDV LRLAPPLTLT AAEADLAVER LAAAIAAAPA KP

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References

[1]"Complete sequence of Anaeromyxobacter sp. Fw109-5."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Lykidis A., Fields M., Richardson P.
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Fw109-5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000769 Genomic DNA. Translation: ABS26887.1.
RefSeqYP_001379871.1. NC_009675.1.

3D structure databases

ProteinModelPortalA7HDU1.
ModBaseSearch...

Protein-protein interaction databases

STRING404589.Anae109_2686.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABS26887; ABS26887; Anae109_2686.
GeneID5374181.
KEGGafw:Anae109_2686.
PATRIC20930693. VBIAnaSp113478_2803.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG4992.
HOGENOMHOG000020206.
KOK00821.
OMAFIVEPIM.
ProtClustDBCLSK946351.

Enzyme and pathway databases

BioCycASP404589:GHMT-2742-MONOMER.
UniPathwayUPA00068; UER00109.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
HAMAPMF_01107. ArgD_aminotrans_3.
InterProIPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
IPR004636. Trfase_AcOrn/SuccOrn_fam.
[Graphical view]
PANTHERPTHR11986. PTHR11986. 1 hit.
PTHR11986:SF19. PTHR11986:SF19. 1 hit.
PfamPF00202. Aminotran_3. 1 hit.
[Graphical view]
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMsTIGR00707. argD. 1 hit.
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameA7HDU1_ANADF
AccessionPrimary (citable) accession number: A7HDU1
Entry history
Integrated into UniProtKB/TrEMBL: September 11, 2007
Last sequence update: September 11, 2007
Last modified: May 1, 2013
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info