Q8CWR0

PR
Gene name
carB
Protein name
Carbamoyl-phosphate synthase large chain
Names
Carbamoyl-phosphate synthetase ammonia chain
Species
Streptococcus pneumoniae (strain ATCC BAA-255 / R6)
KEGG Pathway
spr:spr1153
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)

94-172 (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 Q8CWR0

Entry ID Method Resolution Chain Position Source
AF-Q8CWR0-F1 Predicted AlphaFoldDB

No variants for Q8CWR0

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8CWR0

No associated diseases with Q8CWR0

14 regional properties for Q8CWR0

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
MPKRTDIQKI MVIGSGPIII GQAAEFDYAG TQACFSLKEE GYEVVLVNSN PATIMTDKEI
70 80 90 100 110 120
ADKVYIEPIT LEFVTRILRK EGPDALLPTL GGQTGLNMAM ELSKNGILDE LGVELLGTKL
130 140 150 160 170 180
SAIDQAEDRD LFKQLMEELE QPIPESEIVN TVEEAVAFAA TIGYPVIVRP AFTLGGTGGG
190 200 210 220 230 240
MCANEKELRE ITENGLKLSP VTQCLIERSI AGFKEIEYEV MRDSADNALV VCNMENFDPV
250 260 270 280 290 300
GIHTGDSIVF APAQTMSDYE NQMLRDASLS IIRALKIEGG CNVQLALDPN SFKYYVIEVN
310 320 330 340 350 360
PRVSRSSALA SKATGYPIAK LAAKIAVGLT LDEVINPVTG STYAMFEPAL DYVVAKIPRF
370 380 390 400 410 420
PFDKFEKGER RLGTQMKATG EVMAIGRNIE ESLLKACRSL EIGVHHNEIP ELAAVSDDAL
430 440 450 460 470 480
IEKVVKAQDD RLFYVSEAIR RGYTPEEIAE LTKIDIFYLD KLLHIFEIEQ ELGAHPQDLE
490 500 510 520 530 540
VLKTAKLNGF SDRKIAELWG TTDDKVRQLR LENKIVPVYK MVDTCAAEFD SETPYFYSTY
550 560 570 580 590 600
GWENESIRSD KESVLVLGSG PIRIGQGVEF DYATVHSVKA IQAAGYEAII MNSNPETVST
610 620 630 640 650 660
DFSVSDKLYF EPLTFEDVMN VIDLEQPKGV IVQFGGQTAI NLAEPLAKAG VTILGTQVAD
670 680 690 700 710 720
LDRAEDRDLF EQALKELDIP QPPGQTATNE EEAALAARKI GFPVLVRPSY VLGGRAMEIV
730 740 750 760 770 780
ENEEDLRSYM RTAVKASPDH PVLVDSYIVG QECEVDAISD GKNVLIPGIM EHIERAGVHS
790 800 810 820 830 840
GDSMAVYPPQ TLSQKVQETI ADYTKRLAIG LHCLGMMNIQ FVIKDEKVYV IEVNPRASRT
850 860 870 880 890 900
VPFLSKVTNI PMAQVATKLI LGQSLSELGY QNGLYPESTR VHIKAPVFSF TKLAKVDSLL
910 920 930 940 950 960
GPEMKSTGEV MGSDATLEKA LYKAFEASYL HLPTFGNVVF TIADDAKEEA LNLARRFQNI
970 980 990 1000 1010 1020
GYGILATEGT AAFFASHGLQ AQPVGKIGDD DKDIPSFVRK GRIQAIINTV GTKRTADEDG
1030 1040 1050
EQIRRSAIEH GVPLFTALDT ANAMLKVLES RSFVTEAI