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Protein

N-acetyl-gamma-glutamyl-phosphate reductase

Gene

argC

Organism
Shigella flexneri
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate = N-acetyl-5-glutamyl phosphate + NADPH.UniRule annotation

Pathwayi: L-arginine biosynthesis

This protein is involved in step 3 of the subpathway that synthesizes N(2)-acetyl-L-ornithine from L-glutamate.UniRule annotation
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Amino-acid acetyltransferase (argA)
  2. Acetylglutamate kinase (argB)
  3. N-acetyl-gamma-glutamyl-phosphate reductase (argC)
  4. Acetylornithine/succinyldiaminopimelate aminotransferase (argD)
This subpathway is part of the pathway L-arginine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes N(2)-acetyl-L-ornithine from L-glutamate, the pathway L-arginine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei154UniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Arginine biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

UniPathwayiUPA00068; UER00108.

Names & Taxonomyi

Protein namesi
Recommended name:
N-acetyl-gamma-glutamyl-phosphate reductaseUniRule annotation (EC:1.2.1.38UniRule annotation)
Short name:
AGPRUniRule annotation
Alternative name(s):
N-acetyl-glutamate semialdehyde dehydrogenaseUniRule annotation
Short name:
NAGSA dehydrogenaseUniRule annotation
Gene namesi
Name:argCUniRule annotation
Ordered Locus Names:SF4035, S3711
OrganismiShigella flexneri
Taxonomic identifieri623 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeShigella
Proteomesi
  • UP000002673 Componenti: Chromosome
  • UP000001006 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001124461 – 334N-acetyl-gamma-glutamyl-phosphate reductaseAdd BLAST334

Proteomic databases

PaxDbiP59310.

Interactioni

Protein-protein interaction databases

STRINGi198214.SF4035.

Structurei

Secondary structure

1334
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 7Combined sources6
Turni8 – 10Combined sources3
Helixi12 – 23Combined sources12
Beta strandi27 – 35Combined sources9
Turni39 – 42Combined sources4
Helixi45 – 48Combined sources4
Helixi50 – 52Combined sources3
Turni53 – 55Combined sources3
Beta strandi59 – 65Combined sources7
Helixi66 – 68Combined sources3
Beta strandi74 – 78Combined sources5
Helixi82 – 94Combined sources13
Beta strandi98 – 101Combined sources4
Beta strandi107 – 109Combined sources3
Helixi111 – 117Combined sources7
Beta strandi118 – 120Combined sources3
Helixi125 – 130Combined sources6
Turni136 – 138Combined sources3
Helixi141 – 144Combined sources4
Beta strandi147 – 150Combined sources4
Helixi154 – 168Combined sources15
Beta strandi179 – 184Combined sources6
Helixi186 – 189Combined sources4
Helixi199 – 201Combined sources3
Beta strandi203 – 206Combined sources4
Turni209 – 211Combined sources3
Helixi214 – 222Combined sources9
Beta strandi227 – 237Combined sources11
Beta strandi239 – 247Combined sources9
Helixi253 – 264Combined sources12
Beta strandi270 – 272Combined sources3
Beta strandi274 – 276Combined sources3
Helixi280 – 282Combined sources3
Turni283 – 285Combined sources3
Beta strandi289 – 296Combined sources8
Beta strandi299 – 306Combined sources8
Turni308 – 313Combined sources6
Helixi314 – 325Combined sources12
Turni329 – 333Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3DR3X-ray2.00A1-334[»]
ProteinModelPortaliP59310.
SMRiP59310.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP59310.

Family & Domainsi

Sequence similaritiesi

Belongs to the NAGSA dehydrogenase family. Type 1 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C0N. Bacteria.
COG0002. LUCA.
HOGENOMiHOG000254902.
KOiK00145.
OMAiTFVPHLT.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00150. ArgC_type1. 1 hit.
InterProiIPR023013. AGPR_AS.
IPR000706. AGPR_type-1.
IPR016040. NAD(P)-bd_dom.
IPR000534. Semialdehyde_DH_NAD-bd.
IPR012280. Semialdhyde_DH_dimer_dom.
[Graphical view]
PfamiPF01118. Semialdhyde_dh. 1 hit.
PF02774. Semialdhyde_dhC. 1 hit.
[Graphical view]
SMARTiSM00859. Semialdhyde_dh. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01850. argC. 1 hit.
PROSITEiPS01224. ARGC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P59310-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLNTLIVGAS GYAGAELVTY VNRHPHMNIT ALTVSAQSND AGKLISDLHP
60 70 80 90 100
QLKGIVELPL QPMSDISEFS PGVDVVFLAT AHEVSHDLAP QFLEAGCVVF
110 120 130 140 150
DLSGAFRVND ATFYEKYYGF THQYPELLEQ AAYGLAEWCG NKLKEANLIA
160 170 180 190 200
VPGCYPTAAQ LALKPLIDAD LLDLNQWPVI NATSGVSGAG RKAAISNSFC
210 220 230 240 250
EVSLQPYGVF THRHQPEIAT HLGADVIFTP HLGNFPRGIL ETITCRLKSG
260 270 280 290 300
VTQAQVAQAL QQAYAHKPLV RLYDKGVPAL KNVVGLPFCD IGFAVQGEHL
310 320 330
IIVATEDNLL KGAAAQAVQC ANIRFGYAET QSLI
Length:334
Mass (Da):35,938
Last modified:February 12, 2003 - v1
Checksum:i45FCA247E797257A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005674 Genomic DNA. Translation: AAN45465.1.
AE014073 Genomic DNA. Translation: AAP18737.1.
RefSeqiNP_709758.1. NC_004337.2.
WP_000935388.1. NZ_LVJC01000017.1.

Genome annotation databases

EnsemblBacteriaiAAN45465; AAN45465; SF4035.
AAP18737; AAP18737; S3711.
GeneIDi1026505.
KEGGisfl:SF4035.
sft:NCTC1_04369.
sfx:S3711.
PATRICi18709244. VBIShiFle31049_4048.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005674 Genomic DNA. Translation: AAN45465.1.
AE014073 Genomic DNA. Translation: AAP18737.1.
RefSeqiNP_709758.1. NC_004337.2.
WP_000935388.1. NZ_LVJC01000017.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3DR3X-ray2.00A1-334[»]
ProteinModelPortaliP59310.
SMRiP59310.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi198214.SF4035.

Proteomic databases

PaxDbiP59310.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAN45465; AAN45465; SF4035.
AAP18737; AAP18737; S3711.
GeneIDi1026505.
KEGGisfl:SF4035.
sft:NCTC1_04369.
sfx:S3711.
PATRICi18709244. VBIShiFle31049_4048.

Phylogenomic databases

eggNOGiENOG4105C0N. Bacteria.
COG0002. LUCA.
HOGENOMiHOG000254902.
KOiK00145.
OMAiTFVPHLT.

Enzyme and pathway databases

UniPathwayiUPA00068; UER00108.

Miscellaneous databases

EvolutionaryTraceiP59310.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00150. ArgC_type1. 1 hit.
InterProiIPR023013. AGPR_AS.
IPR000706. AGPR_type-1.
IPR016040. NAD(P)-bd_dom.
IPR000534. Semialdehyde_DH_NAD-bd.
IPR012280. Semialdhyde_DH_dimer_dom.
[Graphical view]
PfamiPF01118. Semialdhyde_dh. 1 hit.
PF02774. Semialdhyde_dhC. 1 hit.
[Graphical view]
SMARTiSM00859. Semialdhyde_dh. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01850. argC. 1 hit.
PROSITEiPS01224. ARGC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiARGC_SHIFL
AccessioniPrimary (citable) accession number: P59310
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 12, 2003
Last sequence update: February 12, 2003
Last modified: November 2, 2016
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.