Skip Header

Contribute Send feedback
Read comments (?) or add your own

B1Y3G6 (B1Y3G6_LEPCP) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 25. 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Amino-acid acetyltransferase HAMAP MF_01105
EC=2.3.1.1 HAMAP MF_01105
Alternative name(s):
N-acetylglutamate synthase HAMAP MF_01105
Gene names
Name:argA HAMAP MF_01105
Ordered Locus Names:Lcho_2228
OrganismLeptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix discophora (strain SP-6)) [Complete proteome] [HAMAP] EMBL ACB34494.1
Taxonomic identifier395495 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Leptothrix

Protein attributes

Sequence length446 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate. HAMAP MF_01105

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4. HAMAP MF_01105

Subcellular location

Cytoplasm By similarity HAMAP MF_01105.

Miscellaneous

In bacteria which possess the bifunctional enzyme ornithine acetyltransferase/N-acetylglutamate synthase (ArgJ), ArgA fulfills an anaplerotic role By similarity. HAMAP MF_01105

Sequence similarities

Belongs to the acetyltransferase family. ArgA subfamily. HAMAP MF_01105

Contains 1 N-acetyltransferase domain. HAMAP MF_01105

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Arginine biosynthesis HAMAP MF_01105
   Cellular componentCytoplasm HAMAP MF_01105
   Molecular functionAcyltransferase HAMAP MF_01105
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 functionacetyl-CoA:L-glutamate N-acetyltransferase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Domain299 – 435137N-acetyltransferase By similarity HAMAP MF_01105

Sequences

Sequence LengthMass (Da)Tools
B1Y3G6 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: 6EC84080FA65E5C3

FASTA44648,888
        10         20         30         40         50         60 
MNLVFPHTFV PWFRSVAPYI HAYHGKTFVV GMAGELIAAG KLSAFAQDLS ILHAMGIKLV 

        70         80         90        100        110        120 
VVHGFRPQVN EQLLAKGHPS RFSHGQRITD AVALDCAQEA AGQLRFEIEA AFSQGLPNTP 

       130        140        150        160        170        180 
MANATVRVVS GNFLTARPVG IVDGVDFIHS GVVRKVDSGT IRRAIDIGAL VLLSPFGFSP 

       190        200        210        220        230        240 
TGEAFNLAME DVATATAIAL QADKLLFITE VAGIHEQLDD PDSAIDTELA LADAKRLLAT 

       250        260        270        280        290        300 
LPSPTQPTDI AFYLQHCVKA CEGGVERSHI LPFGVDGALL MEVFTHDGIG TMVVDEKLES 

       310        320        330        340        350        360 
LREASSDDVG GVLQLIEPFE RDGTLVKRDR TEIERDIALY TVIEHDGIIF GCAALYPYPE 

       370        380        390        400        410        420 
ARTAEMAALT ISPQVQSQGD GERILKRIEQ RARALGLESI FVLTTRTMHW FIKRGFQNVD 

       430        440 
PEWLPDARKR KYNWDRRSQV LVKKLG

« Hide

References

[1]"Complete sequence of Leptothrix cholodnii SP-6."
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Lykidis A., Emerson D., Richardson P.
Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51168 / LMG 8142 / SP-6.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001013 Genomic DNA. Translation: ACB34494.1.
RefSeqYP_001791259.1. NC_010524.1.

3D structure databases

ProteinModelPortalB1Y3G6.
ModBaseSearch...

Protein-protein interaction databases

STRINGB1Y3G6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6160638.
GenomeReviewsGene locus Lcho_2228 in contig CP001013_GR.
KEGGlch:Lcho_2228.
PATRIC22394835. VBILepCho83238_2252.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG545264.
OMAAFNLAME.
ProtClustDBPRK05279.

Family and domain databases

HAMAPMF_01105. N_acetyl_glu_synth.
[Tree]
InterProIPR000182. AcTrfase_GCN5-related_dom.
IPR016181. Acyl_CoA_acyltransferase.
IPR001048. Asp/Glu/Uridylate_kinase.
IPR010167. NH2A_AcTrfase_ArgA.
[Graphical view]
Gene3DG3DSA:3.40.1160.10. Aa_kinase. 1 hit.
G3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 1 hit.
KOK14682.
PfamPF00696. AA_kinase. 1 hit.
PF00583. Acetyltransf_1. 1 hit.
[Graphical view]
PIRSFPIRSF000423. ArgA. 1 hit.
SUPFAMSSF53633. Aa_kinase. 1 hit.
SSF55729. Acyl_CoA_acyltransferase. 1 hit.
TIGRFAMsTIGR01890. N-Ac-Glu-synth. 1 hit.
PROSITEPS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameB1Y3G6_LEPCP
AccessionPrimary (citable) accession number: B1Y3G6
Entry history
Integrated into UniProtKB/TrEMBL: May 20, 2008
Last sequence update: May 20, 2008
Last modified: December 14, 2011
This is version 25 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