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A4SYB2 (A4SYB2_POLSQ) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 31. 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:Pnuc_1262
OrganismPolynucleobacter sp. (strain QLW-P1DMWA-1) [Complete proteome] [HAMAP] EMBL ABP34476.1
Taxonomic identifier312153 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Polynucleobacter

Protein attributes

Sequence length454 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 ABP34476.1
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

Domain309 – 453145N-acetyltransferase By similarity HAMAP MF_01105

Sequences

Sequence LengthMass (Da)Tools
A4SYB2 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: 1C9BA6C8B2B0159F

FASTA45449,952
        10         20         30         40         50         60 
MPTNAPNLAP SAEESASNFP FVGWLRDVAP YIHSFREKTF VIAFAGELVQ EIGLENLIED 

        70         80         90        100        110        120 
IAMLHAMGMR IVLVHGIRPQ IEEQLMLRKI KSKFGKSTMH SYRITDAAAL ECVKEAAGEL 

       130        140        150        160        170        180 
RLDIEAAFSR GLPNTPMAGS RISVISGNFI TAMPVGVVEG IDYIHTGLVR KVDSSSIKQS 

       190        200        210        220        230        240 
LDSNKIVLLS PLGFSPTGQA FNLAYEDVAA STAAALKADK LIFLSPYPGL KDAEGDIITE 

       250        260        270        280        290        300 
LSLPQLQEYV SQNKEMEIGM KGLLNIAGKA IRAGVSRVHF LPSNQDGALL EELFTHDGIG 

       310        320        330        340        350        360 
MMLASSDIEN LREASQDDVG GILQLTMPLE DEGILAARGQ DVIERDIQRF SVIEHDRVLF 

       370        380        390        400        410        420 
GCAALFPFPN GVGELACLAV DPDVQGSGDG ERLLKRIEMR AKQEGIKKLF VLTTRTEHWF 

       430        440        450 
LKRGFKRATV DDLPEERKQI YNWDRKSMVL TKDL

« Hide

References

[1]"Complete sequence of Polynucleobacter sp. QLW-P1DMWA-1."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Meincke L., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Mikhailova N., Poeckl M., Wu Q.L., Hahn M., Richardson P.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: QLW-P1DMWA-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000655 Genomic DNA. Translation: ABP34476.1.
RefSeqYP_001156040.1. NC_009379.1.

3D structure databases

ProteinModelPortalA4SYB2.
ModBaseSearch...

Protein-protein interaction databases

STRINGA4SYB2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5052450.
GenomeReviewsGene locus Pnuc_1262 in contig CP000655_GR.
KEGGpnu:Pnuc_1262.
PATRIC22967005. VBIPolNec12025_1311.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0548.
HOGENOMHBG545264.
OMAAFNLAME.
PhylomeDBA4SYB2.
ProtClustDBPRK05279.

Enzyme and pathway databases

BioCycPSP312153:PNUC_1262-MONOMER.

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 nameA4SYB2_POLSQ
AccessionPrimary (citable) accession number: A4SYB2
Entry history
Integrated into UniProtKB/TrEMBL: May 15, 2007
Last sequence update: May 15, 2007
Last modified: December 14, 2011
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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