P26265

PR
Gene name
cpdB (STM4403)
Protein name
2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase
Names
Species
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
KEGG Pathway
stm:STM4403
EC number
3.1.3.6: Phosphoric monoester hydrolases
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

287-360 (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 P26265

Entry ID Method Resolution Chain Position Source
AF-P26265-F1 Predicted AlphaFoldDB

No variants for P26265

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P26265

No associated diseases with P26265

5 regional properties for P26265

Type Name Position InterPro Accession
domain Calcineurin-like phosphoesterase domain, ApaH type 24 - 259 IPR004843
conserved_site 5'-Nucleotidase, conserved site 24 - 36 IPR006146-1
conserved_site 5'-Nucleotidase, conserved site 109 - 120 IPR006146-2
domain 5'-Nucleotidase, C-terminal 356 - 550 IPR008334
domain CpdB, N-terminal metallophosphatase domain 24 - 321 IPR041827

Functions

Description
EC Number 3.1.3.6 Phosphoric monoester hydrolases
Subcellular Localization
  • Periplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
outer membrane-bounded periplasmic space The region between the inner (cytoplasmic or plasma) membrane and outer membrane of organisms with two membranes such as Gram negative bacteria. These periplasmic spaces are relatively thick and contain a thin peptidoglycan layer (PGL), also referred to as a thin cell wall.

4 GO annotations of molecular function

Name Definition
2',3'-cyclic-nucleotide 2'-phosphodiesterase activity Catalysis of the reaction: nucleoside 2',3'-cyclic phosphate + H2O = nucleoside 3'-phosphate.
3'-nucleotidase activity Catalysis of the reaction: a 3'-ribonucleotide + H2O = a ribonucleoside + phosphate.
metal ion binding Binding to a metal ion.
nucleotide binding Binding to a nucleotide, any compound consisting of a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose or deoxyribose.

1 GO annotations of biological process

Name Definition
nucleotide catabolic process The chemical reactions and pathways resulting in the breakdown 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).

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MIKFSATLLA TLIAASVNAA TVDLRIMETT DLHSNMMDFD YYKDTATEKF GLVRTASLIH
70 80 90 100 110 120
AARNEVKNSV LVDNGDLIQG SPLGDYMAAK GLKDGDVHPV YKALNTLDYA VGNLGNHEFN
130 140 150 160 170 180
YGLDYLHNAL AGAKFPYVNA NIIDVKTQKP LFTPYLIKET SVIDKDGNPQ TLKIGYIGFV
190 200 210 220 230 240
PPQIMIWDKA NLSGKVTVND ITETARKYVP EMREKGADIV VVIAHSGLSA DPYHSMAENS
250 260 270 280 290 300
VYYLSEVPGV DAIMFGHAHA VFPGKDFADI KGADIAKGTL NGIPAVMPGM WGDHLGVVDL
310 320 330 340 350 360
VLNNDSGKWQ VTQAKAEARP IYDAAAKKSL AAEDSKLVGI LKADHDATRE FVSKPIGKSA
370 380 390 400 410 420
DNMYSYLALV QDDPTVQVVN NAQKAYVEHF IQGDPDLAKL PVLSAAAPFK VGGRKNDPAS
430 440 450 460 470 480
FVEVEKGQLT FRNAADLYLY PNTLVVVKAS GKEVKEWLEC SAGQFNQIDI HSNKPQSLIN
490 500 510 520 530 540
WDGFRTYNFD VIDGVNYQID VSQPARYDGE CQMVNPQAER IKNLTFNGKP VDPNATFLVA
550 560 570 580 590 600
TNNYRAYGGK FAGTGDSHIA FASPDENRAV LAAWIGAESK RAGEIHPAAD NNWRLAPIHS
610 620 630 640
DTALDIRFET SPGDKAAAFI KAKGQYPMKK VAVDDIGFAI YQVDLSK