Q5M5F6

PR
Gene name
carB
Protein name
Carbamoyl-phosphate synthase large chain
Names
Carbamoyl-phosphate synthetase ammonia chain
Species
Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311)
KEGG Pathway
stl:stu0527
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)

93-171 (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 Q5M5F6

Entry ID Method Resolution Chain Position Source
AF-Q5M5F6-F1 Predicted AlphaFoldDB

No variants for Q5M5F6

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5M5F6

No associated diseases with Q5M5F6

5 regional properties for Q5M5F6

Type Name Position InterPro Accession
domain HNH nuclease 821 - 871 IPR003615
domain CRISPR-associated endonuclease Cas9, PAM-interacting domain 1081 - 1335 IPR032237
domain CRISPR-associated endonuclease Cas9, bridge helix 62 - 94 IPR032239
domain CRISPR-associated endonuclease Cas9, REC lobe 181 - 713 IPR032240
domain Cas9-type HNH domain 770 - 921 IPR033114

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
MPKRSDIKKI MVIGSGPIII GQAAEFDYAG TQACLALKEE GYSVVLVNSN PATIMTDKEI
70 80 90 100 110 120
ADKVYIEPIT LEFVTRILRK ERPDALLPTL GGQTGLNMAM ELSKAGILDE LGVELLGTKL
130 140 150 160 170 180
SAIDQAEDRD LFKQLMEELE QPIPESEIVN TVEEAVAFAT EIGYPVIVRP AFTLGGTGGG
190 200 210 220 230 240
MCANEEELRE IAENGLKLSP VTQCLIERSI AGFKEIEYEV MRDAEDNALV VCNMENFDPV
250 260 270 280 290 300
GIHTGDSIVF APTQTLSDIE NQMLRDASLK IIRALKIEGG CNVQLALDPH SFKYYVIEVN
310 320 330 340 350 360
PRVSRSSALA SKATGYPIAK LAAKIAVGLT LDEMINPVTG TTYAMFEPAL DYVVAKIPRF
370 380 390 400 410 420
PFDKFEHGER RLGTQMKATG EVMAIGRNIE ESLLKACRSL EIGVYHNEMS ELAEVTDDAL
430 440 450 460 470 480
VEKVVKAQDD RLFYISEAIR RGYTIEELSE LTKIDIFFLD KLLHIFELEQ ELAAHVGDVD
490 500 510 520 530 540
VLKEAKRNGF SDRKIADLWN QTANQVRATR LENNIVPVYK MVDTCAAEFE SSTPYFYSTY
550 560 570 580 590 600
EWENESIKSD KESVIVLGSG PIRIGQGVEF DYATVHSVKA IQAAGYEAII MNSNPETVST
610 620 630 640 650 660
DFSVSDKLYF EPLTFEDVMN VIELEQPKGV VVQFGGQTAI NLAEPLSKAG VKILGTQVAD
670 680 690 700 710 720
LDRAEDRDLF EQALKDLDIP QPPGQTATNE EEAVEAARKI GFPVLVRPSY VLGGRAMEIV
730 740 750 760 770 780
ENEDDLRSYM RTAVKASPDH PVLVDSYIIG RECEVDAISD GKDVLIPGIM EHIERAGVHS
790 800 810 820 830 840
GDSMAVYPPQ TLSKKIQETI ADYTKRLAIG LNCIGMMNIQ FVIKDETVYV IEVNPRASRT
850 860 870 880 890 900
VPFLSKVTDI PMAQVATNLI LGKSLAEQGY KDGLYPESNH VHVKAPVFSF TKLAQVDSLL
910 920 930 940 950 960
GPEMKSTGEV MGTDVTLEKA LYKAFEASYL HLPTFGNVIF TIHDDTKEEA LDLARRFDAI
970 980 990 1000 1010 1020
GYGIYATEGT AKFLNEHGVH ATLVNKLGEN DDNDIPALVR TGKAQAIINT VGNKRTYDED
1030 1040 1050
GAAIRSSAIE AGIPLFTALD TADAMVRVLE SRSFTTEAI