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D1ED56

- D1ED56_NEIGO

UniProt

D1ED56 - D1ED56_NEIGO

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Protein

Amino-acid acetyltransferase

Gene

argA

Organism
Neisseria gonorrhoeae SK-93-1035
Status
Unreviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate.UniRule annotationSAAS annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei46 – 461SulfateImported

GO - Molecular functioni

  1. acetyl-CoA:L-glutamate N-acetyltransferase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. arginine biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

AcyltransferaseUniRule annotationSAAS annotation, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Arginine biosynthesisUniRule annotationSAAS annotation

Enzyme and pathway databases

UniPathwayiUPA00068; UER00106.

Names & Taxonomyi

Protein namesi
Recommended name:
Amino-acid acetyltransferaseUniRule annotation (EC:2.3.1.-UniRule annotation, EC:2.3.1.1UniRule annotation)
Alternative name(s):
N-acetylglutamate synthaseUniRule annotation
Gene namesi
Name:argAUniRule annotation
ORF Names:NGLG_00316Imported
OrganismiNeisseria gonorrhoeae SK-93-1035Imported
Taxonomic identifieri528360 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

CytoplasmUniRule annotation

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4I49X-ray2.75A1-436[»]
ProteinModelPortaliD1ED56.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini287 – 436150N-acetyltransferaseUniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni265 – 2673Sulfate bindingImported

Sequence similaritiesi

Belongs to the acetyltransferase family. ArgA subfamily.UniRule annotation
Contains 1 N-acetyltransferase domain.UniRule annotation
Contains N-acetyltransferase domain.SAAS annotation

Family and domain databases

Gene3Di3.40.1160.10. 1 hit.
3.40.630.30. 1 hit.
HAMAPiMF_01105. N_acetyl_glu_synth.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR001048. Asp/Glu/Uridylate_kinase.
IPR000182. GNAT_dom.
IPR010167. NH2A_AcTrfase_ArgA.
[Graphical view]
PfamiPF00696. AA_kinase. 1 hit.
PF00583. Acetyltransf_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000423. ArgA. 1 hit.
SUPFAMiSSF53633. SSF53633. 1 hit.
SSF55729. SSF55729. 1 hit.
TIGRFAMsiTIGR01890. N-Ac-Glu-synth. 1 hit.
PROSITEiPS51186. GNAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

D1ED56-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNAPDSFVAH FREAAPYIRQ MRGTTLVAGI DGRLLEGGTL NKLAADIGLL
60 70 80 90 100
SQLGIRLVLI HGAYHFLDRL AAAQGRTPHY CRGLRVTDET SLGQAQQFAG
110 120 130 140 150
TVRSRFEAAL CGSVSGFARA PSVPLVSGNF LTARPIGVID GTDMEYAGVI
160 170 180 190 200
RKTDTAALRF QLDAGNIVWM PPLGHSYGGK TFNLDMVQAA ASVAVSLQAE
210 220 230 240 250
KLVYLTLSDG ISRPDGTLAE TLSAQEAQSL AEHAASETRR LISSAVAALE
260 270 280 290 300
GGVHRVQILN GAADGSLLQE LFTRNGIGTS IAKEAFVSIR QAHSGDIPHI
310 320 330 340 350
AALIRPLEEQ GILLHRSREY LENHISEFSI LEHDGNLYGC AALKTFAEAD
360 370 380 390 400
CGEIACLAVS PQAQDGGYGE RLLAHIIDKA RGIGISRLFA LSTNTGEWFA
410 420 430
ERGFQTASED ELPETRRKDY RSNGRNSHIL VRRLHR
Length:436
Mass (Da):47,006
Last modified:January 19, 2010 - v1
Checksum:iE29044A0B76C7B02
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
EQ973086 Genomic DNA. Translation: EEZ58476.1.

Genome annotation databases

EnsemblBacteriaiEEZ58476; EEZ58476; NGLG_00316.
PATRICi28195341. VBINeiGon43547_0285.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
EQ973086 Genomic DNA. Translation: EEZ58476.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4I49 X-ray 2.75 A 1-436 [» ]
ProteinModelPortali D1ED56.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai EEZ58476 ; EEZ58476 ; NGLG_00316 .
PATRICi 28195341. VBINeiGon43547_0285.

Enzyme and pathway databases

UniPathwayi UPA00068 ; UER00106 .

Family and domain databases

Gene3Di 3.40.1160.10. 1 hit.
3.40.630.30. 1 hit.
HAMAPi MF_01105. N_acetyl_glu_synth.
InterProi IPR016181. Acyl_CoA_acyltransferase.
IPR001048. Asp/Glu/Uridylate_kinase.
IPR000182. GNAT_dom.
IPR010167. NH2A_AcTrfase_ArgA.
[Graphical view ]
Pfami PF00696. AA_kinase. 1 hit.
PF00583. Acetyltransf_1. 1 hit.
[Graphical view ]
PIRSFi PIRSF000423. ArgA. 1 hit.
SUPFAMi SSF53633. SSF53633. 1 hit.
SSF55729. SSF55729. 1 hit.
TIGRFAMsi TIGR01890. N-Ac-Glu-synth. 1 hit.
PROSITEi PS51186. GNAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: SK-93-1035Imported.
  2. "Structure of the complex of Neisseria gonorrhoeae N-acetyl-L-glutamate synthase with a bound bisubstrate analog."
    Zhao G., Allewell N.M., Tuchman M., Shi D.
    Biochem. Biophys. Res. Commun. 430:1253-1258(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS).

Entry informationi

Entry nameiD1ED56_NEIGO
AccessioniPrimary (citable) accession number: D1ED56
Entry historyi
Integrated into UniProtKB/TrEMBL: January 19, 2010
Last sequence update: January 19, 2010
Last modified: October 29, 2014
This is version 26 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structureImported

External Data

Dasty 3