Q0W932

PR
Gene name
argC
Protein name
N-acetyl-gamma-glutamyl-phosphate reductase
Names
AGPR, N-acetyl-glutamate semialdehyde dehydrogenase, NAGSA dehydrogenase
Species
Methanocella arvoryzae (strain DSM 22066 / NBRC 105507 / MRE50)
KEGG Pathway
rci:LRC63
EC number
1.2.1.38: With NAD(+) or NADP(+) as acceptor
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

6-82 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q0W932

Entry ID Method Resolution Chain Position Source
AF-Q0W932-F1 Predicted AlphaFoldDB

No variants for Q0W932

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q0W932

No associated diseases with Q0W932

3 regional properties for Q0W932

Type Name Position InterPro Accession
domain Semialdehyde dehydrogenase, NAD-binding 3 - 138 IPR000534
domain Semialdehyde dehydrogenase, dimerisation domain 155 - 305 IPR012280
active_site N-acetyl-gamma-glutamyl-phosphate reductase, active site 140 - 156 IPR023013

Functions

Description
EC Number 1.2.1.38 With NAD(+) or NADP(+) as acceptor
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

3 GO annotations of molecular function

Name Definition
N-acetyl-gamma-glutamyl-phosphate reductase activity Catalysis of the reaction: N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate = N-acetyl-5-glutamyl phosphate + NADPH + H+.
NAD binding Binding to nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH.
protein dimerization activity The formation of a protein dimer, a macromolecular structure consists of two noncovalently associated identical or nonidentical subunits.

1 GO annotations of biological process

Name Definition
arginine biosynthetic process The chemical reactions and pathways resulting in the formation of arginine, 2-amino-5-(carbamimidamido)pentanoic acid.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MLKIGIVGGT GYTGGELLRL LSIHPLAEVT VVTSRKQAGQ PVDTVHPNLK SLTDLKFEDP
70 80 90 100 110 120
DPAKIAERCD VVFTAVPHGA AMAVVPELLK YGLRVIDLSA DYRLPTEKFE QVYNKKHLDP
130 140 150 160 170 180
REAVYGLPEL HPEVKDATLI ANPGCYPTGA NLACAPLIAQ GLVNRAVVDS KSGISGSGQD
190 200 210 220 230 240
PTEGTHYPNV TQNVRPYNLT THRHKAEIEQ EMLRLNNSTR IHFTPHVIPS TRGIMTTAHL
250 260 270 280 290 300
FVDEPLTTDQ VQTIYDEFYK NKPFVRLQKP SLANVRGSNF CDIAFEVEKD SDRIVVVSAI
310 320 330
DNMVKGASGQ AIQNMNLMYG FDERTGLWTS GLSP