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 Q9SFV7

Entry ID Method Resolution Chain Position Source
AF-Q9SFV7-F1 Predicted AlphaFoldDB

25 variants for Q9SFV7

Variant ID(s) Position Change Description Diseaes Association Provenance
tmp_3_2315515_T_G 22 I>S No 1000Genomes
ENSVATH00310992 36 Q>K No 1000Genomes
ENSVATH10540622 67 R>L No 1000Genomes
ENSVATH05789778 81 V>I No 1000Genomes
tmp_3_2316137_G_A 160 R>H No 1000Genomes
ENSVATH05789780 170 Q>K No 1000Genomes
ENSVATH02121105 194 L>V No 1000Genomes
tmp_3_2316265_C_T,A 203 R>C No 1000Genomes
tmp_3_2316265_C_T,A 203 R>S No 1000Genomes
tmp_3_2316286_G_A 210 V>I No 1000Genomes
ENSVATH05789782 219 D>Y No 1000Genomes
tmp_3_2316317_A_G 220 E>G No 1000Genomes
ENSVATH05789783 237 V>I No 1000Genomes
tmp_3_2316437_C_T 260 S>F No 1000Genomes
tmp_3_2316446_C_T 263 S>L No 1000Genomes
ENSVATH05789784 278 L>V No 1000Genomes
ENSVATH10540624 286 L>W No 1000Genomes
tmp_3_2316555_A_T 299 K>N No 1000Genomes
tmp_3_2316580_A_C 308 N>H No 1000Genomes
tmp_3_2316609_C_A 317 N>K No 1000Genomes
tmp_3_2316649_C_A 331 H>N No 1000Genomes
ENSVATH05789785 337 P>L No 1000Genomes
tmp_3_2316988_G_T 444 A>S No 1000Genomes
tmp_3_2317007_A_C 450 D>A No 1000Genomes
tmp_3_2317037_C_T 460 T>I No 1000Genomes

No associated diseases with Q9SFV7

2 regional properties for Q9SFV7

Type Name Position InterPro Accession
domain GTP cyclohydrolase I domain 35 - 187 IPR020602-1
domain GTP cyclohydrolase I domain 272 - 452 IPR020602-2

Functions

Description
EC Number 3.5.4.16 In cyclic amidines
Subcellular Localization
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.

3 GO annotations of molecular function

Name Definition
GTP binding Binding to GTP, guanosine triphosphate.
GTP cyclohydrolase I activity Catalysis of the reaction: GTP + H2O = formate + 7,8-dihydroneopterin 3'-triphosphate.
zinc ion binding Binding to a zinc ion (Zn).

3 GO annotations of biological process

Name Definition
7,8-dihydroneopterin 3'-triphosphate biosynthetic process The chemical reactions and pathways resulting in the formation of 7,8-dihydroneopterin 3'-triphosphate.
tetrahydrobiopterin biosynthetic process The chemical reactions and pathways resulting in the formation of tetrahydrobiopterin, the reduced form of biopterin (2-amino-4-hydroxy-6-(1,2-dihydroxypropyl)-pteridine). It functions as a hydroxylation coenzyme, e.g. in the conversion of phenylalanine to tyrosine.
tetrahydrofolate biosynthetic process The chemical reactions and pathways resulting in the formation of tetrahydrofolate, 5,6,7,8-tetrahydrofolic acid, a folate derivative bearing additional hydrogens on the pterin group.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MGALDEGCLN LELDIGMKNG CIELAFEHQP ETLAIQDAVK LLLQGLHEDV NREGIKKTPF
70 80 90 100 110 120
RVAKALREGT RGYKQKVKDY VQSALFPEAG LDEGVGQAGG VGGLVVVRDL DHYSYCESCL
130 140 150 160 170 180
LPFHVKCHIG YVPSGQRVLG LSKFSRVTDV FAKRLQDPQR LADDICSALQ HWVKPAGVAV
190 200 210 220 230 240
VLECSHIHFP SLDLDSLNLS SHRGFVKLLV SSGSGVFEDE SSNLWGEFQS FLMFKGVKTQ
250 260 270 280 290 300
ALCRNGSSVK EWCPSVKSSS KLSPEVDPEM VSAVVSILKS LGEDPLRKEL IATPTRFLKW
310 320 330 340 350 360
MLNFQRTNLE MKLNSFNPAK VNGEVKEKRL HCELNMPFWS MCEHHLLPFY GVVHIGYFCA
370 380 390 400 410 420
EGSNPNPVGS SLMKAIVHFY GFKLQVQERM TRQIAETLSP LVGGDVIVVA EAGHTCMISR
430 440 450 460
GIEKFGSSTA TIAVLGRFSS DNSARAMFLD KIHTTNALKT ESSSPF