Q1IPK2

PR
Gene name
carB
Protein name
Carbamoyl-phosphate synthase large chain
Names
Carbamoyl-phosphate synthetase ammonia chain
Species
Koribacter versatilis (strain Ellin345)
KEGG Pathway
aba:Acid345_2197
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)

644-728 (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 Q1IPK2

Entry ID Method Resolution Chain Position Source
AF-Q1IPK2-F1 Predicted AlphaFoldDB

No variants for Q1IPK2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q1IPK2

No associated diseases with Q1IPK2

14 regional properties for Q1IPK2

Type Name Position InterPro Accession
domain Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain 136 - 342 IPR005479-1
domain Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain 683 - 885 IPR005479-2
domain Carbamoyl-phosphate synthetase, large subunit oligomerisation domain 425 - 553 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 176 - 188 IPR005483-3
domain Carbamoyl-phosphate synthase large subunit, CPSase domain 212 - 231 IPR005483-4
domain Carbamoyl-phosphate synthase large subunit, CPSase domain 247 - 264 IPR005483-5
domain Carbamoyl-phosphate synthase large subunit, CPSase domain 305 - 334 IPR005483-6
domain Carbamoyl-phosphate synthase large subunit, CPSase domain 387 - 405 IPR005483-7
domain Methylglyoxal synthase-like domain 952 - 1092 IPR011607
domain ATP-grasp fold 141 - 336 IPR011761-1
domain ATP-grasp fold 688 - 879 IPR011761-2
domain Carbamoyl-phosphate synthase large chain, methylglyoxal synthase-like domain 958 - 1067 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
MPRRNDISKI LIIGSGPIVI GQSAEFDYSG AQACKALKAE GYEVVLANSN PATIMTDPEM
70 80 90 100 110 120
ADRTYIEPLT PEFLEEIIRI EAAMMPAGAG KFALLPTVGG QTALNLAVDL ADSGVLDKYS
130 140 150 160 170 180
VILIGAQLGA IKKAEDRLLF KDAMAKIGLD VPRSALINNL KDGLEFSGKI GFPLVLRPSF
190 200 210 220 230 240
TLGGSGGGIA YNREELMDLL GKGLDLSPVH EVLLEESVLG WKEYELELMR DLADNVIVIC
250 260 270 280 290 300
SIENFDPMGV HTGDSITVAP AQTLSDREYQ IMRDAAIKVI REIGVETGGS NIQFATNPEN
310 320 330 340 350 360
GRMIVIEMNP RVSRSSALAS KATGFPIAKI AARLAVGYTL DEITNDITRK TPACFEPTLD
370 380 390 400 410 420
YVVVKIPKWQ FEKFPGADAS LGPQMKSVGE AMAIGRTFKE ALMKGIRSLE TGKSIASEKV
430 440 450 460 470 480
EERIITKRLV TAHPERLQYV RHALLHGWSV EKVHSLTKID PWFLYQLKEI AQAHAHTEQH
490 500 510 520 530 540
TMDEVGPDEL RDLKRMGFSD ERLAHLWKAK NGKGASRLVY EKRHASGIRP VYKRVDTCAA
550 560 570 580 590 600
EFESFTPYLY STYEEEDEAA PTDKKKVIIL GSGPNRIGQG IEFDYCCCHA AFALRDDGYE
610 620 630 640 650 660
TIMVNCNPET VSTDYDTSDR LYFEPLTYED VMEIYEHEAS GGAPIGVIVQ FGGQTPLNLA
670 680 690 700 710 720
LPLKASGVPV IGTSPESIDL AEDRKRFNKL LEELDIPQPP GSTATSLEEA VANANKIGYP
730 740 750 760 770 780
VLVRPSYVLG GRAMMICYEQ EEVERYMRQA VEYSQERPVL IDHFLEEATE VDVDCLSDGE
790 800 810 820 830 840
DCVIGGIMQH IEEAGIHSGD SSCVLPSVDL SEQVLKTIRE YTFKLARALK VIGLMNVQYA
850 860 870 880 890 900
IQREKVYVIE VNPRASRTVP YVSKATGVPM AKIAARLMTG RKLREFLPQN IEQGADLATG
910 920 930 940 950 960
NCYYVKSPVF PWGKFPGVDT VLGPEMKSTG EVMGVADNFG EAFAKAQLAA GQKLPTKGTV
970 980 990 1000 1010 1020
FISLNKRDKQ HAAALAKKFV DLGFKIVATH GTADEMEDGG IEVERVFKVK EGRPNVVDLI
1030 1040 1050 1060 1070 1080
KGDRIQMIIN TPQGAEPWFD EKAIRRAAIT ARIPTITTLS AARAAVEGIA ALQRGKTTVY
1090 1100
ALQELHRERR QGMPGQQVNG LR