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G2SS12 (G2SS12_LACRR) Unreviewed, UniProtKB/TrEMBL

Last modified April 16, 2014. Version 17. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

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:LRC_17180 EMBL AEN78960.1
OrganismLactobacillus ruminis (strain ATCC 27782 / RF3) [Complete proteome] [HAMAP] EMBL AEN78960.1
Taxonomic identifier1069534 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length425 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

Region241 – 2444Pyridoxal phosphate binding By similarity HAMAP-Rule MF_01107

Sites

Binding site1351Pyridoxal phosphate; via carbonyl oxygen By similarity HAMAP-Rule MF_01107
Binding site1381N2-acetyl-L-ornithine By similarity HAMAP-Rule MF_01107
Binding site2991Pyridoxal phosphate By similarity HAMAP-Rule MF_01107

Amino acid modifications

Modified residue2701N6-(pyridoxal phosphate)lysine By similarity HAMAP-Rule MF_01107

Sequences

Sequence LengthMass (Da)Tools
G2SS12 [UniParc].

Last modified November 16, 2011. Version 1.
Checksum: A801693CFBC42698

FASTA42546,524
        10         20         30         40         50         60 
MESLYERSLK VFPPVAGRAT KIGAVSGQGS WLIDESGKKY LDFASGVAVV NCGHNHPKVV 

        70         80         90        100        110        120 
EAVEKQLHEL VHGGHNVVYY PKYVELAEKL VARVGKPGEY KVYFSNSGAE ANEGAVKLAL 

       130        140        150        160        170        180 
KATGRPGIIA FNGSFHGRTL LCASMTASSA LYRENYEPEL PQVYHADFPD VWNTDLTEQE 

       190        200        210        220        230        240 
EIERCLNSVH KIFTNLILPE RVACMVIEPV QGEGGYLPAP KRFIAELRKI CDEHGILLIF 

       250        260        270        280        290        300 
DEVQSGYGRT GYLFAKDYYG VQPDIFTSAK AIANGIPLSA VIGKTEYMDK WLAGSHGGTF 

       310        320        330        340        350        360 
GGNPLACAAG CAVLDVIDED FLEDVRKKGA FIRERLEDLK VTHSNVISSI RGIGMMNGVE 

       370        380        390        400        410        420 
FRKDGKPLPK IVSKVQEIAL SKGLILLNCG TFHNVIRLIP PLTATKEEIE QAIGIIDECL 


KEIEG 

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References

[1]"Genome sequences and comparative genomics of two Lactobacillus ruminis strains from the bovine and human intestinal tracts."
Forde B.M., Neville B.A., O'Donnell M.M., Riboulet-Bisson E., Claesson M.J., Coghlan A., Ross R.P., O'Toole P.W.
Microb. Cell Fact. 10:S13-S13(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27782 / RF3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP003032 Genomic DNA. Translation: AEN78960.1.
RefSeqYP_004832896.1. NC_015975.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEN78960; AEN78960; LRC_17180.
GeneID11140621.
KEGGlrm:LRC_17180.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK00823.

Enzyme and pathway databases

BioCycLRUM1069534:GJVX-1792-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.
PfamPF00202. Aminotran_3. 1 hit.
[Graphical view]
PIRSFPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
SUPFAMSSF53383. SSF53383. 1 hit.
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameG2SS12_LACRR
AccessionPrimary (citable) accession number: G2SS12
Entry history
Integrated into UniProtKB/TrEMBL: November 16, 2011
Last sequence update: November 16, 2011
Last modified: April 16, 2014
This is version 17 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)