Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Carbamoyl-phosphate synthase arginine-specific large chain

Gene

carB

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

2 ATP + L-glutamine + HCO3- + H2O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate.

Cofactori

Mg2+By similarity, Mn2+By similarityNote: Binds 4 Mg2+ or Mn2+ ions per subunit.By similarity

Pathwayi: L-arginine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes carbamoyl phosphate from bicarbonate.
Proteins known to be involved in this subpathway in this organism are:
  1. Carbamoyl-phosphate synthase arginine-specific small chain (carA), Carbamoyl-phosphate synthase arginine-specific large chain (carB)
This subpathway is part of the pathway L-arginine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes carbamoyl phosphate from bicarbonate, the pathway L-arginine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi284 – 2841Magnesium or manganese 1By similarity
Metal bindingi298 – 2981Magnesium or manganese 1By similarity
Metal bindingi298 – 2981Magnesium or manganese 2By similarity
Metal bindingi300 – 3001Magnesium or manganese 2By similarity
Metal bindingi822 – 8221Magnesium or manganese 3By similarity
Metal bindingi834 – 8341Magnesium or manganese 3By similarity
Metal bindingi834 – 8341Magnesium or manganese 4By similarity
Metal bindingi836 – 8361Magnesium or manganese 4By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi159 – 21658ATPBy similarityAdd
BLAST
Nucleotide bindingi701 – 75656ATPBy similarityAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Amino-acid biosynthesis, Arginine biosynthesis

Keywords - Ligandi

ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciBSUB:BSU11240-MONOMER.
SABIO-RKP18185.
UniPathwayiUPA00068; UER00171.

Names & Taxonomyi

Protein namesi
Recommended name:
Carbamoyl-phosphate synthase arginine-specific large chain (EC:6.3.5.5)
Alternative name(s):
Carbamoyl-phosphate synthetase ammonia chain
Gene namesi
Name:carB
Synonyms:cpaB
Ordered Locus Names:BSU11240
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10301030Carbamoyl-phosphate synthase arginine-specific large chainPRO_0000144992Add
BLAST

Proteomic databases

PaxDbiP18185.

Interactioni

Subunit structurei

Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate.

Protein-protein interaction databases

IntActiP18185. 1 interaction.
MINTiMINT-8366347.
STRINGi224308.Bsubs1_010100006211.

Structurei

3D structure databases

ProteinModelPortaliP18185.
SMRiP18185. Positions 1-1023.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini133 – 327195ATP-grasp 1Add
BLAST
Domaini675 – 863189ATP-grasp 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 401401Carboxyphosphate synthetic domainAdd
BLAST
Regioni402 – 548147Oligomerization domainAdd
BLAST
Regioni549 – 928380Carbamoyl phosphate synthetic domainAdd
BLAST
Regioni929 – 1030102Allosteric domainAdd
BLAST

Sequence similaritiesi

Belongs to the CarB family.Curated
Contains 2 ATP-grasp domains.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0458. LUCA.
HOGENOMiHOG000234582.
InParanoidiP18185.
KOiK01955.
OMAiSSHAIQD.
PhylomeDBiP18185.

Family and domain databases

Gene3Di1.10.1030.10. 1 hit.
3.30.1490.20. 2 hits.
3.30.470.20. 2 hits.
3.40.50.20. 2 hits.
HAMAPiMF_01210_B. CPSase_L_chain_B. 1 hit.
InterProiIPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR006275. CarbamoylP_synth_lsu.
IPR005480. CarbamoylP_synth_lsu_oligo.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR005483. CbamoylP_synth_lsu_CPSase_dom.
IPR016185. PreATP-grasp_dom.
[Graphical view]
PfamiPF02786. CPSase_L_D2. 2 hits.
PF02787. CPSase_L_D3. 1 hit.
[Graphical view]
PRINTSiPR00098. CPSASE.
SMARTiSM01096. CPSase_L_D3. 1 hit.
[Graphical view]
SUPFAMiSSF48108. SSF48108. 1 hit.
SSF52440. SSF52440. 2 hits.
TIGRFAMsiTIGR01369. CPSaseII_lrg. 1 hit.
PROSITEiPS50975. ATP_GRASP. 2 hits.
PS00866. CPSASE_1. 2 hits.
PS00867. CPSASE_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P18185-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKDTSISSI LVIGSGPIII GQAAEFDYSG TQGCIALKEE GYRVILVNSN
60 70 80 90 100
PATIMTDEAF ADEIYFEPLT AESLTAIIKK ERPDGLLANL GGQTALNLAV
110 120 130 140 150
ELEETGVLKE HGVKLLGTSV ETIQKGEDRE KFRSLMNELK QPVPESEIVD
160 170 180 190 200
NEADALHFAE SIGFPVIIRP AYTLGGKGGG IAPDKEAFTA MIKQALLASP
210 220 230 240 250
INQCLVEKSI AGFKEIEYEV MRDSNNTCIT VCNMENIDPV GVHTGDSIVV
260 270 280 290 300
APSQTLTDED YQMLRTASLT IISALDVVGG CNIQFALDPF SKQYYVIEVN
310 320 330 340 350
PRVSRSSALA SKATGYPIAK MAAKLAVGYT LDELKNPLTG STYASFEPAL
360 370 380 390 400
DYVIVKFPRW PFDKFKNADR KLGTKMKATG EVMAIERNLE AAIQKAAASL
410 420 430 440 450
ELKNIGTHLP ELSGLSIDTL WDLAITPDDR RFFVVMELLS RSVSIDDIHE
460 470 480 490 500
KTKIDPFFLH TFDNIIKLEN RLMEAGSDLS FELLKKAKEK GFSDATIASL
510 520 530 540 550
ISKTEEEVRA LRKEMGITPS FKIVDTCAAE FDAKTNYFYS TYFGETDGDI
560 570 580 590 600
SRKEKKRALI IGSGPIRIGQ GVEFDYSAVH GVLTLQELGF ETIMINNNPE
610 620 630 640 650
TVSTDYEIAD RLYFEPMTTE HIVNVAEQEN IDFAIVQFGG QTAINAAEAL
660 670 680 690 700
EKAGITLLGT SFQTLDVLED RDQFYQLLDE LGLKHAKGEI AYTKEEAASK
710 720 730 740 750
ASEIGYPVLI RPSYVIGGMG MIIVDSQAQL SQLLNDEDSM PYPILIDQYV
760 770 780 790 800
SGKEVEIDLI SDGEEVFIPT YTEHIERAGV HSGDSFAILP GPSITSGLQQ
810 820 830 840 850
GMKDAAQKIA RKLSFKGIMN IQFVIDNGNI LVLEVNPRAS RTVPVVSKVM
860 870 880 890 900
GVPMIPLATR LLAGASLKDL NPAVQNHHGV AVKFPVFSSH AIQDVDVKLG
910 920 930 940 950
PEMKSTGEGM CVAYDSNSAL KKIYTRVWSQ KGSIYLQNVP EDVKELAENA
960 970 980 990 1000
GFTIHEGTFA SWMEQEGNSL HINLSGSEEA RKERLEAMTH GIPVFTEEET
1010 1020 1030
VRAFLQSGSG HPQPVSLKDL YKKEVASCTQ
Length:1,030
Mass (Da):112,798
Last modified:July 28, 2009 - v4
Checksum:i73508761F7E25C9E
GO

Sequence cautioni

The sequence CAA37443 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti397 – 3971A → G in CAA81548 (PubMed:8025667).Curated
Sequence conflicti510 – 5101A → R in CAA81548 (PubMed:8025667).Curated
Sequence conflicti626 – 6261A → R in CAA81548 (PubMed:8025667).Curated
Sequence conflicti854 – 8574MIPL → R in CAA81548 (PubMed:8025667).Curated
Sequence conflicti879 – 8791G → A in CAA37443 (PubMed:2117745).Curated
Sequence conflicti913 – 9131A → R in CAA37443 (PubMed:2117745).Curated
Sequence conflicti1004 – 10041F → S in CAA37443 (PubMed:2117745).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z26919 Genomic DNA. Translation: CAA81548.1.
AL009126 Genomic DNA. Translation: CAB12965.3.
X53360 Genomic DNA. Translation: CAA37443.1. Different initiation.
PIRiI40377.
RefSeqiNP_389006.3. NC_000964.3.
WP_003232982.1. NZ_JNCM01000035.1.

Genome annotation databases

EnsemblBacteriaiCAB12965; CAB12965; BSU11240.
GeneIDi939353.
KEGGibsu:BSU11240.
PATRICi18973958. VBIBacSub10457_1173.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z26919 Genomic DNA. Translation: CAA81548.1.
AL009126 Genomic DNA. Translation: CAB12965.3.
X53360 Genomic DNA. Translation: CAA37443.1. Different initiation.
PIRiI40377.
RefSeqiNP_389006.3. NC_000964.3.
WP_003232982.1. NZ_JNCM01000035.1.

3D structure databases

ProteinModelPortaliP18185.
SMRiP18185. Positions 1-1023.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP18185. 1 interaction.
MINTiMINT-8366347.
STRINGi224308.Bsubs1_010100006211.

Proteomic databases

PaxDbiP18185.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB12965; CAB12965; BSU11240.
GeneIDi939353.
KEGGibsu:BSU11240.
PATRICi18973958. VBIBacSub10457_1173.

Phylogenomic databases

eggNOGiCOG0458. LUCA.
HOGENOMiHOG000234582.
InParanoidiP18185.
KOiK01955.
OMAiSSHAIQD.
PhylomeDBiP18185.

Enzyme and pathway databases

UniPathwayiUPA00068; UER00171.
BioCyciBSUB:BSU11240-MONOMER.
SABIO-RKP18185.

Family and domain databases

Gene3Di1.10.1030.10. 1 hit.
3.30.1490.20. 2 hits.
3.30.470.20. 2 hits.
3.40.50.20. 2 hits.
HAMAPiMF_01210_B. CPSase_L_chain_B. 1 hit.
InterProiIPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR006275. CarbamoylP_synth_lsu.
IPR005480. CarbamoylP_synth_lsu_oligo.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR005483. CbamoylP_synth_lsu_CPSase_dom.
IPR016185. PreATP-grasp_dom.
[Graphical view]
PfamiPF02786. CPSase_L_D2. 2 hits.
PF02787. CPSase_L_D3. 1 hit.
[Graphical view]
PRINTSiPR00098. CPSASE.
SMARTiSM01096. CPSase_L_D3. 1 hit.
[Graphical view]
SUPFAMiSSF48108. SSF48108. 1 hit.
SSF52440. SSF52440. 2 hits.
TIGRFAMsiTIGR01369. CPSaseII_lrg. 1 hit.
PROSITEiPS50975. ATP_GRASP. 2 hits.
PS00866. CPSASE_1. 2 hits.
PS00867. CPSASE_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCARY_BACSU
AccessioniPrimary (citable) accession number: P18185
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: July 28, 2009
Last modified: September 7, 2016
This is version 131 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.