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 Q5XHA8

Entry ID Method Resolution Chain Position Source
AF-Q5XHA8-F1 Predicted AlphaFoldDB

No variants for Q5XHA8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5XHA8

No associated diseases with Q5XHA8

3 regional properties for Q5XHA8

Type Name Position InterPro Accession
domain CTP synthase, N-terminal 2 - 272 IPR017456
domain Glutamine amidotransferase 311 - 542 IPR017926
domain CTP synthase GATase domain 299 - 544 IPR033828

Functions

Description
EC Number 6.3.4.2 Other carbon--nitrogen ligases
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
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
CTP synthase activity Catalysis of the reaction: ATP + UTP + glutamine + H20= ADP + phosphate + CTP + glutamate.

3 GO annotations of biological process

Name Definition
'de novo' CTP biosynthetic process The chemical reactions and pathways resulting in the formation of cytidine 5'-triphosphate (CTP) from simpler components.
CTP biosynthetic process The chemical reactions and pathways resulting in the formation of CTP, cytidine 5'-triphosphate.
glutamine metabolic process The chemical reactions and pathways involving glutamine, 2-amino-4-carbamoylbutanoic acid.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MKYILVTGGV ISGIGKGVIA SSIGTILKSS NLHVTSIKID PYINIDAGTF SPYEHGEVFV
70 80 90 100 110 120
LDDGGEVDLD LGNYERFLDI RLTKDNNLTT GKIYQSVINK ERKGDYLGKT VQVVPHITDA
130 140 150 160 170 180
IQEWVMRQAL IPVDEDGIEP EVCVIELGGT VGDIESMPFV EAFRQFQFKV RRENFCNIHV
190 200 210 220 230 240
SLVPQPSATG EQKTKPTQNS VRELRGLGLS PDLVVCRCST PLDTSVKEKI SMFCHVEPQQ
250 260 270 280 290 300
VICVHDVSSI YRVPLLLEEQ GVVDYFRQRL DLPIGRQPRR LLMKWKEMAD RYERLLESCS
310 320 330 340 350 360
IALVGKYTKF SDSYASVIKA LEHSALAINH RLEIKYIDSA DLEQETLQEE PVRYHEAWQK
370 380 390 400 410 420
LCSSEGILVP GGFGVRGTEG KIQAIAWARK QKKPFLGVCL GMQLAVVEFA RDVLGWTDAN
430 440 450 460 470 480
STEFNPKTSH PVVIDMPEHN PGQMGGTMRL GKRRTIFHSQ NSIMKKLYGG HEYVEERHRH
490 500 510 520 530 540
RYEVNPELRR ELEVRGLKFV GQDTEGERME IVELEDHPYF VGVQYHPEFL SRPIKPSPPY
550 560 570 580 590
FGLLLASVGR LSQYIERGCR LSPRDTYSDR SENSSPDAEI AELKLPMIDH D