Q9CEI4

PR
Gene name
prs2
Protein name
Putative ribose-phosphate pyrophosphokinase 2
Names
RPPK 2, 5-phospho-D-ribosyl alpha-1-diphosphate 2, Phosphoribosyl diphosphate synthase 2, Phosphoribosyl pyrophosphate synthase 2, P-Rib-PP synthase 2, PRPP synthase 2, PRPPase 2
Species
Lactococcus lactis subsp lactis (strain IL1403) (Streptococcus lactis)
KEGG Pathway
lla:L109335
EC number
2.7.6.1: Diphosphotransferases
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

1-64 (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 Q9CEI4

Entry ID Method Resolution Chain Position Source
AF-Q9CEI4-F1 Predicted AlphaFoldDB

No variants for Q9CEI4

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9CEI4

No associated diseases with Q9CEI4

4 regional properties for Q9CEI4

Type Name Position InterPro Accession
domain Helicase, C-terminal 399 - 553 IPR001650
domain Helicase/UvrB, N-terminal 166 - 332 IPR006935
domain Helicase superfamily 1/2, ATP-binding domain 162 - 361 IPR014001
domain Bacteriophage T5, Orf172 DNA-binding 5 - 77 IPR018306

Functions

Description
EC Number 2.7.6.1 Diphosphotransferases
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.

4 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
kinase activity Catalysis of the transfer of a phosphate group, usually from ATP, to a substrate molecule.
magnesium ion binding Binding to a magnesium (Mg) ion.
ribose phosphate diphosphokinase activity Catalysis of the reaction: D-ribose 5-phosphate + ATP = 5-phospho-alpha-D-ribose 1-diphosphate + AMP + 2 H(+).

4 GO annotations of biological process

Name Definition
5-phosphoribose 1-diphosphate biosynthetic process The chemical reactions and pathways resulting in the formation of 5-phosphoribose 1-diphosphate, also known as 5-phosphoribosyl-1-pyrophosphate.
nucleotide biosynthetic process The chemical reactions and pathways resulting in the formation of nucleotides, any nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the glycose moiety; may be mono-, di- or triphosphate; this definition includes cyclic-nucleotides (nucleoside cyclic phosphates).
phosphorylation The process of introducing a phosphate group into a molecule, usually with the formation of a phosphoric ester, a phosphoric anhydride or a phosphoric amide.
ribonucleoside monophosphate biosynthetic process The chemical reactions and pathways resulting in the formation of a ribonucleoside monophosphate, a compound consisting of a nucleobase linked to a ribose sugar esterified with phosphate on the sugar.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MVYSDSHLKL FALNSNPGLA EKISQFTGVP LGKLSSKQFS DGEIMINMEE SVRSQDIFIV
70 80 90 100 110 120
QSTSCPVNDH LWELLIMIDA CKRASARTIN VVIPYFGYAR QDRTATSREP ITAKLVADMI
130 140 150 160 170 180
VKAGADRLLT LDIHAVQVQG FFDIPVDNLF TVPLFADYYR KSGLFGDDVI VVAPKNSGIK
190 200 210 220 230 240
RARSLAEYLE SAIAIVDYED DDKNRENGYV IGNVSGKKVI LIDDILNTGV TFANAANVVR
250 260 270 280 290 300
EAGASEIYAV ASHGLFTSGA ADVLEKVDIK EILVTDSVVT NHRKPLNVKY LSAAEYLASA
310 320
ILRIHEGRPV SPLFEHEKPQ D