A4W6Q7

PR
Gene name
dgt
Protein name
Deoxyguanosinetriphosphate triphosphohydrolase
Names
dGTP triphosphohydrolase, dGTPase
Species
Enterobacter sp (strain 638)
KEGG Pathway
ent:Ent638_0700
EC number
3.1.5.1: Triphosphoric monoester hydrolases
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

1-53 (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 A4W6Q7

Entry ID Method Resolution Chain Position Source
AF-A4W6Q7-F1 Predicted AlphaFoldDB

No variants for A4W6Q7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A4W6Q7

No associated diseases with A4W6Q7

3 regional properties for A4W6Q7

Type Name Position InterPro Accession
domain HD/PDEase domain 62 - 282 IPR003607
domain HD domain 66 - 273 IPR006674
domain Phosphohydrolase-associated domain 476 - 499 IPR026875

Functions

Description
EC Number 3.1.5.1 Triphosphoric monoester hydrolases
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
dGTPase activity Catalysis of the reaction: dGTP + H(2)O = 2'-deoxyguanosine + 2 H(+) + triphosphate.
magnesium ion binding Binding to a magnesium (Mg) ion.

1 GO annotations of biological process

Name Definition
dGTP catabolic process The chemical reactions and pathways resulting in the breakdown of dGTP, guanosine triphosphate.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MAPIDFRNKI NWHRRFRSPQ GSKSEHEILR IFESDRGRII NSPAIRRLQQ KTQVFPLERN
70 80 90 100 110 120
AAVRTRLTHS MEVQQVGRYI AKEILSRLKE QRLLETYGLD ELTGPFESIV EMACLMHDIG
130 140 150 160 170 180
NPPFGHFGEA AINDWFKQRL FPLDAASQPQ SDDRCIVRDL RLREGEEPLN DLRRKVRQDL
190 200 210 220 230 240
CQFEGNAQGI RLVHSLMRMN LTWAQVGCIL KYTRPAWWMG EPPASHSYLM KKPGYYLSEE
250 260 270 280 290 300
AYIERLRKEL SLTPHGRFPL TWIMEAADDI SYCVADLEDA VEKRIFSVEE LYQHLYDAWG
310 320 330 340 350 360
THEKGSLFSQ VVENAWDKSR SNTLSRSTED QFFMYLRVNT LNKLVPYSAA RFIDNLPAIF
370 380 390 400 410 420
SGDFNHALLE DDSSFSQLLE LYKNVAIRHV FSHPDVEQLE LQGYRVISGL LDIYQPLLKL
430 440 450 460 470 480
SVEEFTELVE TDLMKRLPIE TRLLHKLSTR HRLAYVEAVS KIDRTTAQWP VMEYYYRCRL
490 500
IQDYISGMTD LYAWDEYRRL MAVE