Descriptions

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

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q033U7

Entry ID Method Resolution Chain Position Source
AF-Q033U7-F1 Predicted AlphaFoldDB

No variants for Q033U7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q033U7

No associated diseases with Q033U7

2 regional properties for Q033U7

Type Name Position InterPro Accession
conserved_site Argininosuccinate synthase, conserved site 8 - 16 IPR018223-1
conserved_site Argininosuccinate synthase, conserved site 116 - 127 IPR018223-2

Functions

Description
EC Number 6.3.4.5 Other carbon--nitrogen ligases
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.

2 GO annotations of molecular function

Name Definition
argininosuccinate synthase activity Catalysis of the reaction: ATP + L-citrulline + L-aspartate = AMP + diphosphate + (N(omega)-L-arginino)succinate.
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.

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
MTEKIVLAYS GGLDTSVAIP WLKDKGYEVI AVVLNVGQPN ADFDAIQQKA LNVGALDSIV
70 80 90 100 110 120
VDAQDEFADH YVAPVIKANA LYEGDYPLVS ALSRPLIIEH LVKIAHAQNA TAIAHGSTGK
130 140 150 160 170 180
GNDQVRFEAA IHALDPEMKI EAPIRDFHWS REEEIDYAKE HNVPVPIGKK SPYSIDANLW
190 200 210 220 230 240
GRANEAGILE NPWNQAPDDA WGMTVSPEAA PDDPTFIDLT FKQGVPVALN DEPMALATMI
250 260 270 280 290 300
KELNKLAGDN GIGRIDKIEN RLVGIKSREV YEAPAAAVIM AAHHDLENLT LERDVQHFKP
310 320 330 340 350 360
TIEDKITNMI YEAQWISPLF DALMAFIDKT QAVVNGTVKM KLYKGNATAV ARKSAHNSLY
370 380 390 400
DEDLATYTSA DSFDQEAAAG FIKLWTLPTT VFEQVNHVHS EEKQHD