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 Q55756

Entry ID Method Resolution Chain Position Source
AF-Q55756-F1 Predicted AlphaFoldDB

No variants for Q55756

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q55756

No associated diseases with Q55756

14 regional properties for Q55756

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 - 1058 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 - 1046 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

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
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.

4 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.
glutamine metabolic process The chemical reactions and pathways involving glutamine, 2-amino-4-carbamoylbutanoic acid.
nitrogen compound metabolic process The chemical reactions and pathways involving organic or inorganic compounds that contain nitrogen.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MPRRNDLNKI MILGAGPIVI GQACEFDYSG TQACKALKEE GYEVVLVNSN PASIMTDPEL
70 80 90 100 110 120
ADRTYIEPLI PEIVEKIIEK ERPDAVLPTM GGQTALNLAV SLSKSGVLEK YGVELIGAKL
130 140 150 160 170 180
PAIEMGEDRE LFKEAMARIG VPVCPSGIAS SIEEARQVAH EIGSYPLIIR PAFTLAGTGG
190 200 210 220 230 240
GIAYNQEEYE EMVQYGLDQS PMSQILVEKS LLGWKEYELE VMRDLADNVV IICSIENFDP
250 260 270 280 290 300
MGVHTGDSIT VAPAQTLTDK EYQRLRDYSI AIIREIGVET GGSNIQFSVN PANGDVIVIE
310 320 330 340 350 360
MNPRVSRSSA LASKATGFPI AKFAAKLAVG YTLNEISNDI TKKTPASFEP TIDYVVTKIP
370 380 390 400 410 420
RFAFEKFPGA EPILNTQMKS VGEAMAIGRT FQESFQKALR SLETGRFGFG CDRHETLPTL
430 440 450 460 470 480
SHLRSQLRTP NPERVFSLHH AFNLGMTVEE IHELTAIDPW FLDKLEDLVK TEKYMKQRSL
490 500 510 520 530 540
KDLTAADLRY IKQQGFGDRQ IAFATKTTED EVRAYRKSLG ITPVYKVVDT CAAEFEAFTP
550 560 570 580 590 600
YYYSTYEPEE CEVLPSDKPK VMILGGGPNR IGQGIEFDYC CCHAAFSLSD AGYETIMVNS
610 620 630 640 650 660
NPETVSTDYD TSDRLYFEPL TKEDVLNIIE AENPVGIIIQ FGGQTPLKLA VPLQKYLNSP
670 680 690 700 710 720
DCPVQTKIWG TSPDSIDTAE DRERFEKILH ELEISQPPNG IARDYEESRV VANRISYPVV
730 740 750 760 770 780
VRPSYVLGGR AMEIVYSDEE LERYMTYAVQ IEPDHPILID KFLENAIEVD VDSLTDSTGK
790 800 810 820 830 840
VVIGSIMEHI EEAGIHSGDS ACSIPYTSLS DNVLTTIRQW TEQLARALNV VGLMNIQYAV
850 860 870 880 890 900
QGDQVYILEA NPRASRTVPY VSKATGRPLA KIASLVMSGK TLEELGVTEE FIPQHVAVKE
910 920 930 940 950 960
AVLPFSKFPG ADTLLGPEMR STGEVMGIDS DFGKAFAKAE LGAGVILATT GTVFVSMSDR
970 980 990 1000 1010 1020
TKEAAVPVVR ELIDLGFKVV ATSGTQKVLR EHGIEGVEVV LKLHEGRPHV IDWIKNGQIQ
1030 1040 1050 1060 1070 1080
FIINTPSGEE SQLDGRTIRR AALDYKLPII TTIAGGKATV AALRSLQDHP LDVKALQDYL
G