B1I4M8

PR
Gene name
carB
Protein name
Carbamoyl-phosphate synthase large chain
Names
Carbamoyl-phosphate synthetase ammonia chain
Species
Desulforudis audaxviator (strain MP104C)
KEGG Pathway
dau:Daud_1302
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)

646-729 (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 B1I4M8

Entry ID Method Resolution Chain Position Source
AF-B1I4M8-F1 Predicted AlphaFoldDB

No variants for B1I4M8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B1I4M8

No associated diseases with B1I4M8

14 regional properties for B1I4M8

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 681 - 882 IPR005479-2
domain Carbamoyl-phosphate synthetase, large subunit oligomerisation domain 420 - 555 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 945 - 1082 IPR011607
domain ATP-grasp fold 133 - 327 IPR011761-1
domain ATP-grasp fold 686 - 876 IPR011761-2
domain Carbamoyl-phosphate synthase large chain, methylglyoxal synthase-like domain 951 - 1061 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
MPKDKALKKV MVIGSGPIII GQAAEFDYAG TQACRALREE GLEVVLINSN PATIMTDANM
70 80 90 100 110 120
ADRIYIEPLT PEFVAKVISQ ERPDALLPTL GGQTGLNLAK QVADAGILDQ YGVRLLGTPL
130 140 150 160 170 180
ESIKRAEDRE HFKNMCLEIG EPVPESSIIS DVDAAVAFAR KIGYPVVVRP AYTLGGTGGG
190 200 210 220 230 240
VAFSEDELRE IAVRGLTMSI IHQVLVEKCV LGWKEIEYEV MRDAAGNCIT ICSMENIDPM
250 260 270 280 290 300
GIHTGDSIVV APTQTLSDRE HQMLRSASLK IIRALGVEGG CNVQFALDPE SYDYYVIEVN
310 320 330 340 350 360
PRLSRSSALA SKATGYPIAK VATKVAVGLT LDEIKNAVTG KTYACFEPAL DYVVVKYPRW
370 380 390 400 410 420
PFDKFSLANR NLGTQMKSTG EVMAIGRTFE EALLKAVRSL ETGVTGMNLP ELREWDNDRL
430 440 450 460 470 480
RARMARPDDL RLFLVAEALR RGFPVNEIFE LTRIDRFFLD KIKNITEAEE LVRAARPTDV
490 500 510 520 530 540
GTPTGVGAPA GLTPELLRRV KRIGLSDTTI AELVGTTSRE VHRLRRELGV EPVYKMVDTC
550 560 570 580 590 600
AGEFEATTPY YYSTYEDEDE AEPQAVRKVV VLGSGPIRIG QGIEFDYCSV HSVWALKEQG
610 620 630 640 650 660
VKAIIINNNP ETVSTDFDTA DRLYFEPLVP EDVMNILHKE KPDGVIVQFG GQTAINLARP
670 680 690 700 710 720
VEKAGFNILG TSVADIDRAE DRERFDQLVA ELGIPRPPGG TGFSVEEAQR IAEQVGFPVL
730 740 750 760 770 780
VRPSYVLGGR AMEIVYNSQE LLEYMADAVR VTPKHPVLVD KYLLGKELEV DAVCDGETVL
790 800 810 820 830 840
VPGIMEHVER AGIHSGDSIA VFPPQTLTPE IKEQLFEYTQ QIARALKIRG LVNIQFVLHE
850 860 870 880 890 900
GRVFVLEVNP RSSRTVPYLS KVTGIPMVNL ATRICLGATL PELGYRGGLY EETRNIAVKA
910 920 930 940 950 960
PVFSFAKLLD VDVCLGPEMK STGEVMGVSK DYALALYKAC LSAGYTLPSS GKAVVTIADR
970 980 990 1000 1010 1020
DKDEALPLVR SLVNLGFEIV ATEGTAAFLR SRAITVEVAR KVHEGSPNIV DLIRENRIHL
1030 1040 1050 1060 1070 1080
VVNTLTKGKL TTRDGFRIRR AAVEMGVPCL TSLDTARVVI EVMRARQRGE TMPLIPLQEY
VS