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 A8AX83

Entry ID Method Resolution Chain Position Source
AF-A8AX83-F1 Predicted AlphaFoldDB

No variants for A8AX83

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A8AX83

No associated diseases with A8AX83

14 regional properties for A8AX83

Type Name Position InterPro Accession
domain Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain 128 - 333 IPR005479-1
domain Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain 666 - 867 IPR005479-2
domain Carbamoyl-phosphate synthetase, large subunit oligomerisation domain 420 - 540 IPR005480
domain Carbamoyl-phosphate synthase large subunit, CPSase domain 19 - 33 IPR005483-1
domain Carbamoyl-phosphate synthase large subunit, CPSase domain 48 - 58 IPR005483-2
domain Carbamoyl-phosphate synthase large subunit, CPSase domain 168 - 180 IPR005483-3
domain Carbamoyl-phosphate synthase large subunit, CPSase domain 204 - 223 IPR005483-4
domain Carbamoyl-phosphate synthase large subunit, CPSase domain 239 - 256 IPR005483-5
domain Carbamoyl-phosphate synthase large subunit, CPSase domain 296 - 325 IPR005483-6
domain Carbamoyl-phosphate synthase large subunit, CPSase domain 378 - 396 IPR005483-7
domain Methylglyoxal synthase-like domain 930 - 1059 IPR011607
domain ATP-grasp fold 133 - 327 IPR011761-1
domain ATP-grasp fold 671 - 861 IPR011761-2
domain Carbamoyl-phosphate synthase large chain, methylglyoxal synthase-like domain 936 - 1047 IPR033937

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
MPKRKDIQKI MVIGSGPIVI GQAAEFDYAG TQACLSLKEE GYSVVLVNSN PATIMTDKEI
70 80 90 100 110 120
ADRVYIEPIT LEFVARILRK ERPDALLPTL GGQTGLNMAM ELSKSGLLEE LGVELLGTKL
130 140 150 160 170 180
SAIDQAEDRD LFKQLMEELG QPIPESEIVN TVDEALEFAA GIGYPVIVRP AFTLGGTGGG
190 200 210 220 230 240
ICSNEGELQE IAENGLKISP VTQCLIERSI AGFKEIEYEV MRDGADNALV VCNMENFDPV
250 260 270 280 290 300
GIHTGDSIVF APSQTISDYE YQMLRDASLK IIRALKIEGG CNVQLALDPN SFKYYVIEVN
310 320 330 340 350 360
PRVSRSSALA SKATGYPIAK LAAKIAVGLT LDEIINPVTG STYAMFEPAL DYVVAKIPRF
370 380 390 400 410 420
PFDKFEHGER RLGTQMKATG EVMAIGRNIE ESLLKACRSL EVGVDHNELP ALSQVSDDEL
430 440 450 460 470 480
MRKIVKVQDD RLFYISEAIR RGYSPDEIAE LTKIDVFFLD KLLHIYEIEQ ELASHIGDSY
490 500 510 520 530 540
VLKKAKQNGF ADTKIATLWD MTAQQVRRIR QDQKIMPVYK MVDTCAAEFE SATPYFYSTY
550 560 570 580 590 600
GFENESVKSS KESVLVLGSG PIRIGQGVEF DYATVHSVKA IQAAGYEAII MNSNPETVST
610 620 630 640 650 660
DFSVSDKLYF EPLTFEDVMN VIDLEQPKGV IVQFGGQTAI NLAEPLSKAG VKILGTQVAD
670 680 690 700 710 720
LDRAEDRDLF EQALKELDIP QPPGQTATNE EEAIEAARKI GFPVLVRPSY VLGGRAMEIV
730 740 750 760 770 780
ENEADLRSYM RTAVKASPDH PVLVDSYIVG DECEVDAISD GRQVLIPGIM EHIERAGVHS
790 800 810 820 830 840
GDSMAAYPPQ TLSQKVKDTI ADYTKRLALG LNCIGMMNIQ FVIKDEQVYV IEVNPRASRT
850 860 870 880 890 900
VPFLSKVTDI PMAQVATRLI LGETLAELDY EDGLHPESFM VHIKAPVFSF SKLAKVDSLL
910 920 930 940 950 960
GPEMKSTGEV MGSDRTLEKA LYKAFEASYL HLPNFGNVVF TIADDSKEEA LQLAQRFANI
970 980 990 1000 1010 1020
GYGIWATKGT ASYFENHGLH VRLVEKIGSD DDKDIPAYIR KGKIQAIINT VGTKRTADKH
1030 1040 1050
GQIIRSSAIE HGVPLFTALD TADAMLKVLE SRSFTTEAI