B1XIA1

PR
Gene name
argC
Protein name
N-acetyl-gamma-glutamyl-phosphate reductase
Names
AGPR, N-acetyl-glutamate semialdehyde dehydrogenase, NAGSA dehydrogenase
Species
Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum quadruplicatum)
KEGG Pathway
syp:SYNPCC7002_A2102
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)

150-227 (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 B1XIA1

Entry ID Method Resolution Chain Position Source
AF-B1XIA1-F1 Predicted AlphaFoldDB

No variants for B1XIA1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B1XIA1

No associated diseases with B1XIA1

3 regional properties for B1XIA1

Type Name Position InterPro Accession
domain Semialdehyde dehydrogenase, NAD-binding 8 - 147 IPR000534
domain Semialdehyde dehydrogenase, dimerisation domain 164 - 323 IPR012280
active_site N-acetyl-gamma-glutamyl-phosphate reductase, active site 150 - 166 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
MSSSEKVSVG IVGASGYGGM QLVRLLSDHP QVELTYLGGN SSAGKPYAEL YPHVGHRIKM
70 80 90 100 110 120
IVEPIDLDVI ASRCQVVFLG LPNGLACDLA PQLIERGCKV LDLSADYRFK DLDTYQAWYK
130 140 150 160 170 180
TERTDQDTNA IAVYGLPELY RDDIRRAQLV GCPGCYVTAS LLALAPLFKQ GLIQPETAII
190 200 210 220 230 240
DAKSGTSGGG RQGKINLLLA EADASLGAYG VASHRHTPEI EQICSKLASQ DIRVQFTPHL
250 260 270 280 290 300
IPMPRGILAT VYATLRDPGL VRDDLLTIYS AFYRAAPCVE VLPNGVYPQT KWACGTNLCY
310 320 330 340 350
LGIEVDHRTG RVIVMSAIDN LLKGQSGQAV QCMNIMLGWE ETAGLPQLAF YP