O50236

PR
Gene name
carB
Protein name
Carbamoyl-phosphate synthase large chain
Names
Carbamoyl-phosphate synthetase ammonia chain
Species
Zymomonas mobilis subsp mobilis (strain ATCC 31821 / ZM4 / CP4)
KEGG Pathway
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)

105-176 (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 O50236

Entry ID Method Resolution Chain Position Source
AF-O50236-F1 Predicted AlphaFoldDB

No variants for O50236

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for O50236

No associated diseases with O50236

14 regional properties for O50236

Type Name Position InterPro Accession
domain Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain 128 - 336 IPR005479-1
domain Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain 711 - 913 IPR005479-2
domain Carbamoyl-phosphate synthetase, large subunit oligomerisation domain 424 - 575 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 299 - 328 IPR005483-6
domain Carbamoyl-phosphate synthase large subunit, CPSase domain 381 - 399 IPR005483-7
domain Methylglyoxal synthase-like domain 973 - 1112 IPR011607
domain ATP-grasp fold 133 - 330 IPR011761-1
domain ATP-grasp fold 716 - 907 IPR011761-2
domain Carbamoyl-phosphate synthase large chain, methylglyoxal synthase-like domain 979 - 1079 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
MPKRTDLQSI MIIGAGPIVI GQACEFDYSG TQACKALREE GYRVILVNSN PATIMTDPDM
70 80 90 100 110 120
ADATYIEPIT PEVVARIIEK ERPDALLPTM GGQTALNTAL ALASDGTLEK FNCEMIGADA
130 140 150 160 170 180
TAIDKAEDRL KFRQAMDKIG LESPRSSVAH SLEEALDGLD YVGLPAIIRP SFTMGGTGGG
190 200 210 220 230 240
VAYNKEEFID IVSGGLSASP TQEVLIEESV IGWKEYEMEV VRDRHDNCII ICSIENIDPM
250 260 270 280 290 300
GVHTGDSITV APALTMTDKE YQIMRNASIA VLREIGVETG NGGSNVQFAL NPENGRLVVI
310 320 330 340 350 360
EMNPRVSRSS ALASKATGFP IAKVATKLAI GYTLDEITND ITGATPASFE PTIDYVVTKI
370 380 390 400 410 420
PRFAFEKFKN AKPLLTTAMK SVGEVMAIGR SFPESLQKAL RGLENGLSGL DPVEALVGAN
430 440 450 460 470 480
PSVIEAELAR PTPDRLLVAA QALREGLPAE KICEITHYDP WFIARLAEII AAENEVISNG
490 500 510 520 530 540
LPLEAAAFRR LKAMGFSDKR LADLALQSAH LRGLGKAQAK GSGIVHDALQ AMTGGVTEAE
550 560 570 580 590 600
VRTLRHSLNI RPVFKRIDSC AAEFEAKTPY MYSTYEAPFF GEPVCDSLPS NRKKVVILGG
610 620 630 640 650 660
GPNRIGQGLE FDYCCCHACF ALEAAGYETI MVNCNPETVS TDYDTSDRLY FEPLTGEDVL
670 680 690 700 710 720
EILHTEQKNG TLVGVIVQFG GQTPLKLAAE IEKAGIPILG TSPDAIDLAE DRERFSALVS
730 740 750 760 770 780
ELGLLQPANG IARSRDEAIS VADKIGYPIL IRPSYVLGGR AMEIIDGPSQ LDDYIHTAVK
790 800 810 820 830 840
VSGESPVLID QYLRDATEVD VDAVADGDDV VVAGILQHIE EAGIHSGDSA CSIPPYSLPA
850 860 870 880 890 900
SIIEEIKSQT DKLARALKVQ GLMNIQFAVK GDKVYLIEVN PRASRTVPFV AKADGRPVAQ
910 920 930 940 950 960
VAARVMAGEK LRNLPEISWP EGYTAVKEAV FPWARFPGVD PVLSPEMKST GEVMGIDIDF
970 980 990 1000 1010 1020
PMAFAKAQLA AGNALPRAGT FFISVKDSDK AQIVEPIKAL TDLGIKLVAT DGTARYLQSK
1030 1040 1050 1060 1070 1080
GVPVERVNKV REGRPHIVDL IKDGAISLVV NTTEGWQSLQ DSASIRSSVV LAPVPYFTTA
1090 1100 1110
AAAIVAAEAI VAIKARELEV RSLQSYHSMK HA