Q834E2

PR
Gene name
carB
Protein name
Carbamoyl-phosphate synthase large chain
Names
Carbamoyl-phosphate synthetase ammonia chain
Species
Enterococcus faecalis (strain ATCC 700802 / V583)
KEGG Pathway
efa:EF1716
EC number
6.3.4.16: Other carbon--nitrogen ligases
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

97-169 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q834E2

Entry ID Method Resolution Chain Position Source
AF-Q834E2-F1 Predicted AlphaFoldDB

No variants for Q834E2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q834E2

No associated diseases with Q834E2

14 regional properties for Q834E2

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 - 1062 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 - 1049 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
MPKRTDIKKI MVIGSGPIII GQAAEFDYAG TQACLALKEE GYEVVLVNSN PATIMTDKEI
70 80 90 100 110 120
ADHVYIEPIT LEFVSRILRK ERPDALLPTL GGQTGLNMAM ELSESGILDE LNVELLGTKL
130 140 150 160 170 180
SAIDQAEDRD LFKQLMEELE QPIPESEIVN TVEQAVAFAK RIGYPIIVRP AFTLGGTGGG
190 200 210 220 230 240
MCDTEEELRQ IAENGLKLSP VTQCLIEKSI AGFKEIEYEV MRDSADNAIV VCNMENFDPV
250 260 270 280 290 300
GIHTGDSIVF APSQTLSDYE YQMLRDASLK IIRALKIEGG CNVQLALDPH SFNYYVIEVN
310 320 330 340 350 360
PRVSRSSALA SKATGYPIAK LAAKIAVGLT LDEMKNPVTG TTYAEFEPAL DYVVSKIPRW
370 380 390 400 410 420
PFDKFEKGAR ELGTQMKATG EVMAIGRNIE ESLLKAVRSL EIGAYHNELA ELSHVSDLEL
430 440 450 460 470 480
TKKMVHAQDD RLFYLSEAIR RGYSIEELQS LTKIDLFFLD KLLHIIEIET ALESHVDNVA
490 500 510 520 530 540
VLKEAKQNGF SDRKIAALWG QTEQAIADFR RANQIVPVYK MVDTCAAEFE SHTPYFYSTY
550 560 570 580 590 600
EVENESNVSK KPSVLVLGSG PIRIGQGVEF DYATVHSVKA IQAAGYEAII MNSNPETVST
610 620 630 640 650 660
DFSVSDKLYF EPLTLEDVMN VIDLENPIGV IVQFGGQTAI NLAEPLTKQG VKILGTTIED
670 680 690 700 710 720
LDRAENRDLF EQALQELAIP QPPGDTATSA EEAVVIADRI GYPVLVRPSY VLGGRAMEIV
730 740 750 760 770 780
ENQKDLEDYM RHAVKASPEH PVLVDSYLLG QECEVDAICD GETVLIPGIM EHIERAGVHS
790 800 810 820 830 840
GDSMAVYPPQ YLSQEIQATI ADYTKKLALG LNCVGMMNIQ FVIHENRVYV IEVNPRASRT
850 860 870 880 890 900
VPFLSKITGI PMAQVATKAI LGEKLTDLGY QDGLYPESKQ VHVKAPVFSF TKLQKVDTYL
910 920 930 940 950 960
GPEMKSTGEV MGSDYYLEKA LYKAFEASGL HLPSYGAVLF TIADETKEEA LEIAKRFSAI
970 980 990 1000 1010 1020
GYSLVATEGT ADFLAKHQLP VKKVTKISNP EGETVLDVIR NGNAQVVIST MDKNRSSANQ
1030 1040 1050
DGFSIRREAV EHGIPLFTSL DTANAILKVL ESRAFTTEAI