B8DTW3
Gene name |
carB |
Protein name |
Carbamoyl-phosphate synthase large chain |
Names |
Carbamoyl-phosphate synthetase ammonia chain |
Species |
Bifidobacterium animalis subsp lactis (strain AD011) |
KEGG Pathway |
bla:BLA_1154 |
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)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for B8DTW3
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-B8DTW3-F1 | Predicted | AlphaFoldDB |
No variants for B8DTW3
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for B8DTW3 | |||||
No associated diseases with B8DTW3
3 regional properties for B8DTW3
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | CASTOR, ACT domain | 72 - 140 | IPR027795-1 |
| domain | CASTOR, ACT domain | 262 - 322 | IPR027795-2 |
| domain | CASTOR1, N-terminal | 9 - 69 | IPR040778 |
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 |
| MPKRTDIKSV | MVIGSGPIVI | GQAAEFDYSG | TQACRVLREE | GVRVILVNSN | PATIMTDPEM |
| 70 | 80 | 90 | 100 | 110 | 120 |
| ADATYIDPIS | TPILEKIIAK | ERPDALLPTL | GGQTALNAAV | ALGEAGVLKK | YNVELIGASL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| EAIDRGEDRE | SFKKVVKEAG | AESARSDIAH | TLEEVDAIAE | RFGFPLVVRP | SFTMGGLGSG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| IAHDTEELHR | IAGAGIHYSP | TDEVLIEEGI | EGWKEYELEL | MRDRNDNVVV | VCPIENVDPV |
| 250 | 260 | 270 | 280 | 290 | 300 |
| GVHTGDSITV | APVFTLTDRE | YQKLRDIGIA | IIRGVGVDTG | GCNIQFAIHP | DTGRIIVIEM |
| 310 | 320 | 330 | 340 | 350 | 360 |
| NPRVSRSSAL | ASKATGFPIA | KIATKLALGY | TLDEIQNDIT | RSTPASFEPT | IDYVVTKVPR |
| 370 | 380 | 390 | 400 | 410 | 420 |
| FAFEKFPGAD | PTLTTSMKSV | GEAMALAGNF | QESLGKAMRS | IDKRHMGFSW | DGEKPSEGEV |
| 430 | 440 | 450 | 460 | 470 | 480 |
| HELLEQMRIP | TEHRYLQVMR | AIWGGATPEQ | IFNATKIDPW | FIDQFFQINA | TAMQVRGAET |
| 490 | 500 | 510 | 520 | 530 | 540 |
| LSKRLLRKAK | LAGLSDVQIA | HLRRLGDEGE | NTIRELRWNY | GLHPVFKTVD | TCAAEFAAQT |
| 550 | 560 | 570 | 580 | 590 | 600 |
| PYYYSCYADE | TELRKREREA | VIILGSGPNR | IGQGIEFDYT | CVHAVQELGK | DYDTIMVNCN |
| 610 | 620 | 630 | 640 | 650 | 660 |
| PETVSTDYDM | SDRLYFEPLT | FEDVLEIYEA | EKKQGPIKGV | IVQLGGQTPL | SLAARLKAAG |
| 670 | 680 | 690 | 700 | 710 | 720 |
| VPILGTTPEA | IDLAENRELF | GEVLRQEHLN | APRFGTALSL | EEAREAAHNI | GYPVLVRPSY |
| 730 | 740 | 750 | 760 | 770 | 780 |
| VLGGRGMEIV | YDDAQLETYV | NRALSEAKAD | TVVSGRLPSP | LLIDKFLQDA | IEIDVDALFD |
| 790 | 800 | 810 | 820 | 830 | 840 |
| GEELYIGGIM | EHIEEAGVHS | GDAACTLPPS | TLSDDQIRRL | REATLAIAKG | CQVRGLMNVQ |
| 850 | 860 | 870 | 880 | 890 | 900 |
| YAFMANTLYV | IEANPRASRT | VPFASKATGV | ALAKAAARIM | AGETIEQQRE | NGLLLPYGDG |
| 910 | 920 | 930 | 940 | 950 | 960 |
| GDVRLGQQVA | VKESVLPFKR | FRTPVGKTVD | ILLGPEMRST | GEVMGFDRDF | PHAFAKSQLA |
| 970 | 980 | 990 | 1000 | 1010 | 1020 |
| SYEGGLPTNG | NVFISVNDTD | KRQLPLFAVR | LVELGFEIWA | TEGTASVLRR | YGIESKIVDK |
| 1030 | 1040 | 1050 | 1060 | 1070 | 1080 |
| IHSRVDTDPE | HPIEIQHAAG | SVGKNVVELI | EEGQIDLILN | TPNSRGSRSD | GYSIRAAAIA |
| 1090 | 1100 | 1110 | 1120 | 1130 | |
| ADIPQYTTMT | EFSAVLLAIE | AVKKNDYEVM | SIQEHSRELY | ELERKHKEEG | EEARAQ |