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A1TQ88 (A1TQ88_ACIAC) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 36. 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:
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:Aave_2553
OrganismAcidovorax citrulli (strain AAC00-1) (Acidovorax avenae subsp. citrulli) [Complete proteome] [HAMAP] EMBL ABM33126.1
Taxonomic identifier397945 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Comamonadaceae › Acidovorax

Protein attributes

Sequence length448 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 EMBL ABM33126.1
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

Domain302 – 438137N-acetyltransferase By similarity HAMAP MF_01105

Sequences

Sequence LengthMass (Da)Tools
A1TQ88 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 307FCF68CFF54E3C

FASTA44849,337
        10         20         30         40         50         60 
MSAVFNFTFV PWFRSVAPYI HKFRHQTFVI ALTGEAIAAG KLQAIAQDLA MIQAMGVKIV 

        70         80         90        100        110        120 
LVHGFRPQVN EQLAAKGHAA RYSHGIRITD SVALDCAQEA AGQLRYEIEA AFSQGLPNTP 

       130        140        150        160        170        180 
MAGSTVRVIS GNFITARPVG IVDGVDFKHS GLVRKVDVAG IRRSLEMDAL VLISPFGFSP 

       190        200        210        220        230        240 
TGEAFNLTME EVATSVSIAL KADKLVFVCE VPGIRTDPDQ PESEDNPIDT ELPLAQARQM 

       250        260        270        280        290        300 
LARVPPGQKP TDTAFYLQHC VKACQNGVER SHIIPFAVDG ALLLEIYVHD GIGTMVVDEK 

       310        320        330        340        350        360 
LEELREATPD DVGGILQLIE PFEKDGTLVK RDRTEIERDV ANYTIIEHDG VIFGCAALYP 

       370        380        390        400        410        420 
YPEAGTAEMA AVTVSPQSQG TGDGEKLLKR IEQRARAMGL KSLFVLTTRT MHWFIKRGFQ 

       430        440 
PVDPDWLPEA RKKKYNWDRR SQVLVKTL

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References

[1]"Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AAC00-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000512 Genomic DNA. Translation: ABM33126.1.
RefSeqYP_970900.1. NC_008752.1.

3D structure databases

ProteinModelPortalA1TQ88.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1TQ88.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4668511.
GenomeReviewsGene locus Aave_2553 in contig CP000512_GR.
KEGGaav:Aave_2553.
NMPDRfig|397945.5.peg.2188.
PATRIC20680255. VBIAciCit38535_2607.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0548.
HOGENOMHBG545264.
OMAAFNLAME.
PhylomeDBA1TQ88.
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 nameA1TQ88_ACIAC
AccessionPrimary (citable) accession number: A1TQ88
Entry history
Integrated into UniProtKB/TrEMBL: February 6, 2007
Last sequence update: February 6, 2007
Last modified: December 14, 2011
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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