C0MEH1

PR
Gene name
carB
Protein name
Carbamoyl-phosphate synthase large chain
Names
Carbamoyl-phosphate synthetase ammonia chain
Species
Streptococcus equi subsp zooepidemicus (strain H70)
KEGG Pathway
seq:SZO_08480
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)

98-170 (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 C0MEH1

Entry ID Method Resolution Chain Position Source
AF-C0MEH1-F1 Predicted AlphaFoldDB

No variants for C0MEH1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for C0MEH1

No associated diseases with C0MEH1

14 regional properties for C0MEH1

Type Name Position InterPro Accession
domain Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain 128 - 335 IPR005479-1
domain Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain 681 - 884 IPR005479-2
domain Carbamoyl-phosphate synthetase, large subunit oligomerisation domain 423 - 546 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 169 - 181 IPR005483-3
domain Carbamoyl-phosphate synthase large subunit, CPSase domain 205 - 224 IPR005483-4
domain Carbamoyl-phosphate synthase large subunit, CPSase domain 240 - 257 IPR005483-5
domain Carbamoyl-phosphate synthase large subunit, CPSase domain 298 - 327 IPR005483-6
domain Carbamoyl-phosphate synthase large subunit, CPSase domain 380 - 398 IPR005483-7
domain Methylglyoxal synthase-like domain 945 - 1081 IPR011607
domain ATP-grasp fold 133 - 329 IPR011761-1
domain ATP-grasp fold 686 - 878 IPR011761-2
domain Carbamoyl-phosphate synthase large chain, methylglyoxal synthase-like domain 951 - 1060 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
MAKRTDIKKI MVIGSGPIVI GQAAEFDYAG TQACLALKEE GYQVVLVNSN PATIMTDKEV
70 80 90 100 110 120
ADKVYIEPLT LAFVSRILRK ERPDALLPTL GGQTGLNLAM ELSKAGILQE LGVELLGTPL
130 140 150 160 170 180
SAIDQAEDRD LFKQLMKELG EPIPESEIVT TVEGAISFAN AIGYPVIVRP AFTLGGTGGG
190 200 210 220 230 240
ICTNEEALRD IVENGLKLSP VTQCLIERSI AGFKEIEYEV MRDAADNALV VCSMENFDPV
250 260 270 280 290 300
GIHTGDSIVF APTQTLSDVE NQLLRDASLR IIRALKIEGG CNVQLALDPN SFSYYVIEVN
310 320 330 340 350 360
PRVSRSSALA SKATGYPIAK IAAKIAVGLR LDDMLNPVTG TTYAMFEPAL DYVVAKLPRF
370 380 390 400 410 420
PFDKFEQGER RLGTQMKATG EVMAIGRRIE ECLLKACRSL EIGVDHNELK GLDTVSDHEL
430 440 450 460 470 480
VAHIVRAQDD RLFYLSEALR RGYSIEELAG LTKIDLFFLD KLRHIVELEQ ELVKKPVDID
490 500 510 520 530 540
LLTEAKRYGF SDQKIAELWQ TDAASIRRLR RAYRVLPVYK MVDTCAAEFD SQTPYFYSTY
550 560 570 580 590 600
EWENESIKSE KESVIVLGSG PIRIGQGVEF DYATVHSVKA IQAAGYEAII MNSNPETVST
610 620 630 640 650 660
DFSISDKLYF EPLTFEEVMN VIELEQPKGV ILQFGGQTAI NLAEQLTKAG VPILGTQLED
670 680 690 700 710 720
LDRAEDRKLF EKALKDLGIP QPPGKTATNE AEALEAARAI GFPVLVRPSY VLGGRAMEIV
730 740 750 760 770 780
ENEDDLRSYM KTAVKASPEH PVLIDSYILG KECEVDAISD GQSVLIPGIM EHIERAGVHS
790 800 810 820 830 840
GDSMAVYPPQ HLSKQVQDKI VDYTKRLAIG LNCIGMMNIQ FVIQNEQVYV IEVNPRASRT
850 860 870 880 890 900
VPFLSKVTNI PMAQVATKLI LDQTLKDLGY QDGLYPESSL VHIKAPVFSF AKLAKVDSLL
910 920 930 940 950 960
GPEMKSTGEV MGSDLTLEKA LYKAFEASYL HMPEYGTIVF TIADDHKPEA LALARRFSAI
970 980 990 1000 1010 1020
GYQVMATEGT AAFFADQGLD SQLVGKIGGN AHDIPALLRK GQIQAIINTV GAKRVADQDG
1030 1040 1050
QVIRSSAIEQ GVPLFTALDT AAAMLRVLES RTFSIEAI