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 Q047M8

Entry ID Method Resolution Chain Position Source
AF-Q047M8-F1 Predicted AlphaFoldDB

No variants for Q047M8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q047M8

No associated diseases with Q047M8

No regional properties for Q047M8

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q047M8

Functions

Description
EC Number 6.3.4.16 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

3 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity Catalysis of the reaction: 2 ATP + L-glutamine + CO2 + H2O = 2 ADP + phosphate + glutamate + carbamoyl phosphate.
metal ion binding Binding to a metal ion.

2 GO annotations of biological process

Name Definition
'de novo' UMP biosynthetic process The chemical reactions and pathways resulting in the formation of UMP, uridine monophosphate, starting with the synthesis of (S)-dihydroorotate from bicarbonate; UMP biosynthesis may either occur via reduction by quinone, NAD(+) or oxygen.
arginine biosynthetic process The chemical reactions and pathways resulting in the formation of arginine, 2-amino-5-(carbamimidamido)pentanoic acid.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MPKRTDIHKI MVIGSGPIII GQAAEFDYSG TQACLALRDE GYEVVLVNSN PATIMTDTTI
70 80 90 100 110 120
ADKVYIEPLT VDSVSRIIRQ EYPDAILPTL GGQVGLNMAL ALAKTGILDE LHIELLGTKL
130 140 150 160 170 180
ASIEQAEDRE KFKELCQKLG EPVPPSKTVK IVEDALAFGD EIGYPIIVRP AFTMGGTGGG
190 200 210 220 230 240
ICHNHDELAE IAKNGLELSP VTECLIEKSI AGYKEIEFEV MRDSSDNAMI VCCMENFDPV
250 260 270 280 290 300
GIHTGDSIVF SPSQTLSDKE YQMLRDCSLK LIRALKIEGG CNVQLALDPN SLDYDVIEVN
310 320 330 340 350 360
PRVSRSSALA SKATGYPIAK MAAKIAIGMT LDEIKNPVTG TTYAEFEPAL DYVVCKIPRF
370 380 390 400 410 420
PFDKFPKADR VLGTQMKATG EVMAIGRTAE EAMQKAVQSL EIDEKDLYSA KAHKASDDEI
430 440 450 460 470 480
EQKLVRPQDD RLFYLAEAFR RGYSLEDVHE LTKINFYFLD VVKHMVEMEK EIEANPDDLD
490 500 510 520 530 540
VLRLAKKYGF SDQTIAKLWH EYPDQVRDLR KANGIVPVYK MVDTCAAEFE STTPYFYSTY
550 560 570 580 590 600
DGENESRKSG KKSVIVIGSG PIRIGQGVEF DYATVHSVKA LQKMGYEAIV INSNPETVST
610 620 630 640 650 660
DFSVSDKLYF EPLTLEDVLN VCDLEQPEGV IVQFGGQTSI NLAAGLERHG VKILGTTVKD
670 680 690 700 710 720
LDRAEDREEF DQIIKSLHLH QPQGLTATTH EGVMKAADQL GYPVLVRPSY VLGGKAMEIV
730 740 750 760 770 780
YSKDELEEYL HDHADIAEDH PILVDDYLDG RECDVDAISD GKTVLLPGIM EHIEHAGVHS
790 800 810 820 830 840
GDSMAVYPPQ TFSDEVEEKI TDVTKKLALA LNCKGIMNIQ FIVRDGDVYV IEVNPRASRT
850 860 870 880 890 900
VPFLSKITGI EMAQVATRVI MGESLEQQGY ADGLAPEPEM ISVKAPVFSF SKLADVDSYL
910 920 930 940 950 960
GPEMKSTGEV MGSDHTFAKA LYKAFAGAKM QLPENGNVLL TIEDRDKEKI LPIAKRFARI
970 980 990 1000 1010 1020
GYRIFATKGT ANFLKKNDLH VELVTKVHED EQADDNILNE LRDGKIDLVI NTMGHDIEKN
1030 1040 1050 1060
SDGFIIRQMA IQQNVPLLTA LDTADALLKS LENRSFATDA LK