P58944

PR
Gene name
carB
Protein name
Carbamoyl-phosphate synthase large chain
Names
Carbamoyl-phosphate synthetase ammonia chain
Species
Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia)
KEGG Pathway
mma:MM_0038
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)

100-182 (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 P58944

Entry ID Method Resolution Chain Position Source
AF-P58944-F1 Predicted AlphaFoldDB

No variants for P58944

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P58944

No associated diseases with P58944

2 regional properties for P58944

Type Name Position InterPro Accession
domain CobQ/CobB/MinD/ParA nucleotide binding domain 3 - 187 IPR002586
domain CobB/CobQ-like glutamine amidotransferase 244 - 428 IPR011698

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
MPKREDIKKV LLIGSGPITI GQAAEFDFSG SQACRSLKEE GVQVVLVNSN PATIMTDPEM
70 80 90 100 110 120
ADSVYIEPLD ARIIEKIIEK ERPDGIIAGI GGQTGLNITS ELAEMGVFEK YGVQILGTPV
130 140 150 160 170 180
EAIKNTEDRE LFKETMLSIG EKVPLSRAVH SLKEAEEVVE ELGLPLIIRP AYTLGGAGGG
190 200 210 220 230 240
IARTKEELLE ITERGLRRSR INQVLIEESV LGWAEVEYEV MRDANDTCIV ICNMENIDPM
250 260 270 280 290 300
GVHTGESAVV APSQTLSDEE HQMLRSASIK IIRALKIEGG CNIQYALKEG DYRIVEVNPR
310 320 330 340 350 360
VSRSSALASK ATGYPIARVT AKIAIGMTLD EIVNSVTKST PASFEPALDY VITKIPRWPF
370 380 390 400 410 420
DKFTTADKTL TTAMKSTGEI MAIGRTIEES LLKAFKSLDI DNQLGIKRWD EPEIKTLLKT
430 440 450 460 470 480
PTSERLFVIF HALERGMSIK EIAELTSINP FFISKMKKIV EMEKCIRTEE LTPEFLREVK
490 500 510 520 530 540
RMGFPDSRLA ELTGKTREQI SDFRHEEGIL ATFKMVDTCA AEFEAATPYY YSTYEDTCET
550 560 570 580 590 600
NSTDKKKILI LGAGPIRIGQ GIEFDYCTVH AVTALREEGI ETHIINNNPE TVSTDFDTSD
610 620 630 640 650 660
KLFFEPLTME YVMNVIERER PDGVLVQFGG QTSVNLALPL KKELKRRTDL NTVILGTDPE
670 680 690 700 710 720
DMDLAEDREK FYLLMQELGI PQPEGGYATS QQEAIEVAKR IGFPVLVRPS YVLGGRAMEI
730 740 750 760 770 780
VYDEIDLERY MKEAVRVSPE HPILIDDFLE AACEIDVDAV CDQIDVLIGA IMEHIEEAGV
790 800 810 820 830 840
HSGDSACVIP PQSLSKEVLD QVRDYTRKIA LGLRVKGLIN IQMAEKGGKV FVLEANPRSS
850 860 870 880 890 900
RTIPFVSKAV GIPLAKIAAK VIAGHSLKDL GYTDEPKPKH VSIKEVLLPF DKLPGADPVL
910 920 930 940 950 960
GPEMKSTGEV MGVDYDFGRA YYKAELAADN LLPLTGKVFL SIRNADKPEL VEAARKLQAA
970 980 990 1000 1010 1020
GLELMGTRGT VNYLAQHGIF MDTVKKVHDG SPNVIDMMRR DEVDLIINTP TSKMSRKDGY
1030 1040 1050 1060 1070
RIRRAAVDFK VPYITTIQAA VAAADAIETM KKGQDLTIKS INEYHKEMEQ KEE