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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei154 – 1541UniRule annotation

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella
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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 334334N-acetyl-gamma-glutamyl-phosphate reductasePRO_0000112446Add
BLAST

Proteomic databases

PaxDbiP59310.

Interactioni

Protein-protein interaction databases

STRINGi198214.SF4035.

Structurei

Secondary structure

1
334
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 76Combined sources
Turni8 – 103Combined sources
Helixi12 – 2312Combined sources
Beta strandi27 – 359Combined sources
Turni39 – 424Combined sources
Helixi45 – 484Combined sources
Helixi50 – 523Combined sources
Turni53 – 553Combined sources
Beta strandi59 – 657Combined sources
Helixi66 – 683Combined sources
Beta strandi74 – 785Combined sources
Helixi82 – 9413Combined sources
Beta strandi98 – 1014Combined sources
Beta strandi107 – 1093Combined sources
Helixi111 – 1177Combined sources
Beta strandi118 – 1203Combined sources
Helixi125 – 1306Combined sources
Turni136 – 1383Combined sources
Helixi141 – 1444Combined sources
Beta strandi147 – 1504Combined sources
Helixi154 – 16815Combined sources
Beta strandi179 – 1846Combined sources
Helixi186 – 1894Combined sources
Helixi199 – 2013Combined sources
Beta strandi203 – 2064Combined sources
Turni209 – 2113Combined sources
Helixi214 – 2229Combined sources
Beta strandi227 – 23711Combined sources
Beta strandi239 – 2479Combined sources
Helixi253 – 26412Combined sources
Beta strandi270 – 2723Combined sources
Beta strandi274 – 2763Combined sources
Helixi280 – 2823Combined sources
Turni283 – 2853Combined sources
Beta strandi289 – 2968Combined sources
Beta strandi299 – 3068Combined sources
Turni308 – 3136Combined sources
Helixi314 – 32512Combined sources
Turni329 – 3335Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DR3X-ray2.00A1-334[»]
ProteinModelPortaliP59310.
SMRiP59310. Positions 1-334.
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.
OrthoDBiEOG6XSZS3.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00150. ArgC_type1.
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_LM651928.1.

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_LM651928.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DR3X-ray2.00A1-334[»]
ProteinModelPortaliP59310.
SMRiP59310. Positions 1-334.
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.
OrthoDBiEOG6XSZS3.

Enzyme and pathway databases

UniPathwayiUPA00068; UER00108.

Miscellaneous databases

EvolutionaryTraceiP59310.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00150. ArgC_type1.
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...

Publicationsi

  1. "Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157."
    Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y.
    , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.
    Nucleic Acids Res. 30:4432-4441(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 301 / Serotype 2a.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700930 / 2457T / Serotype 2a.

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: July 6, 2016
This is version 102 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.