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Protein

Carbamoyl-phosphate synthase arginine-specific small chain

Gene

carA

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.

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
Active sitei237 – 2371NucleophileBy similarity
Active sitei322 – 3221By similarity
Active sitei324 – 3241By similarity

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, Nucleotide-binding

Enzyme and pathway databases

BioCyciBSUB:BSU11230-MONOMER.
SABIO-RKP36838.
UniPathwayiUPA00068; UER00171.

Protein family/group databases

MEROPSiC26.963.

Names & Taxonomyi

Protein namesi
Recommended name:
Carbamoyl-phosphate synthase arginine-specific small chain (EC:6.3.5.5)
Alternative name(s):
Carbamoyl-phosphate synthetase glutamine chain
Gene namesi
Name:carA
Synonyms:cpaA
Ordered Locus Names:BSU11230
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 – 353353Carbamoyl-phosphate synthase arginine-specific small chainPRO_0000112256Add
BLAST

Proteomic databases

PaxDbiP36838.

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

STRINGi224308.Bsubs1_010100006206.

Structurei

3D structure databases

ProteinModelPortaliP36838.
SMRiP36838. Positions 162-343.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini163 – 349187Glutamine amidotransferase type-1Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 159159CPSaseAdd
BLAST

Sequence similaritiesi

Belongs to the CarA family.Curated

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

eggNOGiENOG4105C1M. Bacteria.
COG0505. LUCA.
HOGENOMiHOG000038087.
InParanoidiP36838.
KOiK01956.
OMAiSEWIFDD.
OrthoDBiEOG61ZTH6.
PhylomeDBiP36838.

Family and domain databases

Gene3Di3.40.50.880. 1 hit.
3.50.30.20. 1 hit.
HAMAPiMF_01209. CPSase_S_chain.
InterProiIPR006274. CarbamoylP_synth_ssu.
IPR002474. CarbamoylP_synth_ssu_N.
IPR029062. Class_I_gatase-like.
IPR017926. GATASE.
[Graphical view]
PfamiPF00988. CPSase_sm_chain. 1 hit.
PF00117. GATase. 1 hit.
[Graphical view]
SMARTiSM01097. CPSase_sm_chain. 1 hit.
[Graphical view]
SUPFAMiSSF52021. SSF52021. 1 hit.
SSF52317. SSF52317. 1 hit.
TIGRFAMsiTIGR01368. CPSaseIIsmall. 1 hit.
PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P36838-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEGYLVLEDG TSFSGELDGH ENCTGEAVFF TGMTGYQEVL TDPSYKGQII
60 70 80 90 100
VFTYPLIGNY GINEKDFESK KPQVKAAVVY EACDHFSHYE AVYSLKEYLQ
110 120 130 140 150
KWNIPLLTHV DTRAVVKKIR ANGTMGATVT ASKEGAEIAL QPENVAEQAS
160 170 180 190 200
AQEISTFGDG NKHIALIDFG YKKSIASSLV KRGCKVTVVP YQQMEAVYNI
210 220 230 240 250
KPDGIVLSNG PGDPKAIQPY LGKIKSIISR FPTLGICLGH QLIALAFGGN
260 270 280 290 300
TFKLPFGHRG ANHPVIDRKT KRVFMTSQNH SYVVDEQSIN EEELTIRFHH
310 320 330 340 350
VNDTSVEGLA HKKLPVMSVQ FHPEAHPGPA ESEWIFDDYL KNVIPARREI

AHA
Length:353
Mass (Da):39,083
Last modified:June 16, 2009 - v2
Checksum:iD35F5120B230A0E0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti329 – 3291P → A in CAA81547 (PubMed:8025667).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z26919 Genomic DNA. Translation: CAA81547.1.
AL009126 Genomic DNA. Translation: CAB12964.2.
PIRiI40376.
RefSeqiNP_389005.2. NC_000964.3.
WP_003232984.1. NZ_JNCM01000035.1.

Genome annotation databases

EnsemblBacteriaiCAB12964; CAB12964; BSU11230.
GeneIDi936387.
KEGGibsu:BSU11230.
PATRICi18973956. VBIBacSub10457_1172.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z26919 Genomic DNA. Translation: CAA81547.1.
AL009126 Genomic DNA. Translation: CAB12964.2.
PIRiI40376.
RefSeqiNP_389005.2. NC_000964.3.
WP_003232984.1. NZ_JNCM01000035.1.

3D structure databases

ProteinModelPortaliP36838.
SMRiP36838. Positions 162-343.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100006206.

Protein family/group databases

MEROPSiC26.963.

Proteomic databases

PaxDbiP36838.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB12964; CAB12964; BSU11230.
GeneIDi936387.
KEGGibsu:BSU11230.
PATRICi18973956. VBIBacSub10457_1172.

Phylogenomic databases

eggNOGiENOG4105C1M. Bacteria.
COG0505. LUCA.
HOGENOMiHOG000038087.
InParanoidiP36838.
KOiK01956.
OMAiSEWIFDD.
OrthoDBiEOG61ZTH6.
PhylomeDBiP36838.

Enzyme and pathway databases

UniPathwayiUPA00068; UER00171.
BioCyciBSUB:BSU11230-MONOMER.
SABIO-RKP36838.

Family and domain databases

Gene3Di3.40.50.880. 1 hit.
3.50.30.20. 1 hit.
HAMAPiMF_01209. CPSase_S_chain.
InterProiIPR006274. CarbamoylP_synth_ssu.
IPR002474. CarbamoylP_synth_ssu_N.
IPR029062. Class_I_gatase-like.
IPR017926. GATASE.
[Graphical view]
PfamiPF00988. CPSase_sm_chain. 1 hit.
PF00117. GATase. 1 hit.
[Graphical view]
SMARTiSM01097. CPSase_sm_chain. 1 hit.
[Graphical view]
SUPFAMiSSF52021. SSF52021. 1 hit.
SSF52317. SSF52317. 1 hit.
TIGRFAMsiTIGR01368. CPSaseIIsmall. 1 hit.
PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of the citrulline biosynthetic operon argC-F from Bacillus subtilis."
    O'Reilly M., Devine K.M.
    Microbiology 140:1023-1025(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  3. "From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
    Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
    Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION TO 329.

Entry informationi

Entry nameiCARX_BACSU
AccessioniPrimary (citable) accession number: P36838
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 16, 2009
Last modified: February 17, 2016
This is version 123 of the entry and version 2 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.