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 Q2KCZ1

Entry ID Method Resolution Chain Position Source
AF-Q2KCZ1-F1 Predicted AlphaFoldDB

No variants for Q2KCZ1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q2KCZ1

No associated diseases with Q2KCZ1

2 regional properties for Q2KCZ1

Type Name Position InterPro Accession
domain Phosphoribosyltransferase domain 64 - 185 IPR000836
domain Orotate phosphoribosyl transferase domain 19 - 180 IPR004467

Functions

Description
EC Number 2.4.2.10 Pentosyltransferases
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

2 GO annotations of molecular function

Name Definition
magnesium ion binding Binding to a magnesium (Mg) ion.
orotate phosphoribosyltransferase activity Catalysis of the reaction: orotidine 5'-phosphate + diphosphate = orotate + 5-phospho-alpha-D-ribose 1-diphosphate.

1 GO annotations of biological process

Name Definition
'de novo' UMP biosynthetic process The chemical reactions and pathways resulting in the formation of UMP, uridine monophosphate, starting with the synthesis of (S)-dihydroorotate from bicarbonate; UMP biosynthesis may either occur via reduction by quinone, NAD(+) or oxygen.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MIQTTFPDRA LMAELVAKML WEIKAVHFNA AQPYKLSSGM ASPVYIDCRK LLSYPRIRST
70 80 90 100 110 120
VMDFAASTLL RDAGFEQFDC IAGGETAGIP FAALLADRLG LPMIYVRKQP KGHGRNAQIE
130 140 150 160 170 180
GNMPEGSRVL VIEDLTTAGG SMFKFIDAVR AAGGIVDHGI ALFFYDIFGQ QRFTDGKVRL
190 200 210 220
HHIATWRNVL AVARAQQLFD DKTLAEVEAF LDAPLAWSGR NGGVSELSL