P22572

PR
Gene name
arg-2 (cpa1, NCU07732)
Protein name
Carbamoyl-phosphate synthase arginine-specific small chain, mitochondrial
Names
CPS-A, Arginine-specific carbamoyl-phosphate synthetase, glutamine chain
Species
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
KEGG Pathway
ncr:NCU07732
EC number
6.3.5.5: Carbon--nitrogen ligases with glutamine as amido-N-donor
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

1-72 (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 P22572

Entry ID Method Resolution Chain Position Source
AF-P22572-F1 Predicted AlphaFoldDB

No variants for P22572

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P22572

No associated diseases with P22572

3 regional properties for P22572

Type Name Position InterPro Accession
domain Carbamoyl-phosphate synthase small subunit, N-terminal domain 53 - 192 IPR002474
domain Glutamine amidotransferase 236 - 411 IPR017926
domain Carbamoyl-phosphate synthase small subunit, GATase1 domain 234 - 411 IPR035686

Functions

Description
EC Number 6.3.5.5 Carbon--nitrogen ligases with glutamine as amido-N-donor
Subcellular Localization
  • Mitochondrion matrix
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
carbamoyl-phosphate synthase complex A protein complex that catalyzes the formation of carbamoyl phosphate; comprises a small subunit that binds and cleaves glutamine, and a large subunit that accepts the ammonia group cleaved from glutamine, binds all of the remaining substrates and effectors, and carries out all of the other catalytic events.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
mitochondrial matrix The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation.

2 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity Catalysis of the reaction: 2 ATP + L-glutamine + CO2 + H2O = 2 ADP + phosphate + glutamate + carbamoyl phosphate.

4 GO annotations of biological process

Name Definition
'de novo' pyrimidine nucleobase biosynthetic process The chemical reactions and pathways resulting in the formation of pyrimidine nucleobases, 1,3-diazine, organic nitrogenous bases, beginning with the synthesis of a pyrimidine ring from simpler precursors.
arginine biosynthetic process The chemical reactions and pathways resulting in the formation of arginine, 2-amino-5-(carbamimidamido)pentanoic acid.
glutamine metabolic process The chemical reactions and pathways involving glutamine, 2-amino-4-carbamoylbutanoic acid.
nitrogen compound metabolic process The chemical reactions and pathways involving organic or inorganic compounds that contain nitrogen.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MFSRLAARLP KASALNGVAA RQVRNLSQPA ITGSKGRNMP AREPRTTAAA TGAEATFTIR
70 80 90 100 110 120
DGPVFQGTAF GANTNISGEA VFTTSLVGYP ESMTDPSYRG QILVFTQPLI GNYGVPSNER
130 140 150 160 170 180
DEFNLLKYFE SPHIQCAGIV VSDVATQYSH WTAVQSLGEW CASEGIPAIS GVDTRAIVTY
190 200 210 220 230 240
LREQGSSLAR ISIGDEYDAD EDEGFIDPGQ INLVKRVSTK APFVVTNPNA KFHVALIDCG
250 260 270 280 290 300
VKENILRSLV SRGASVTVFP YNYPIHKVAE NFDGVFISNG PGDPTHCQET VYNLAKLMET
310 320 330 340 350 360
SPIPIMGICL GHQLLALAVG AKTIKLKYGN RAHNIPALDL TTGQCHITSQ NHGYAVDIST
370 380 390 400 410 420
LPSDFKEYFV NLNDGSNEGM MHKTRPIFST QFHPEAKGGP MDSSYLFDKY MENVELFKSN
430 440 450
SQVYRDNRPT QFMIDILSKE RVGVEPTPLS NAA