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Reviewed, UniProtKB/Swiss-Prot Q732I2 (CARA_BACC1)

Last modified February 9, 2010. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Carbamoyl-phosphate synthase small chain
    EC=6.3.5.5
Alternative name(s):
    Carbamoyl-phosphate synthetase glutamine chain
Gene names
Name: carA
Ordered Locus Names: BCE_3932
OrganismBacillus cereus (strain ATCC 10987) [Complete proteome] [HAMAP]
Taxonomic identifier222523 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length365 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

2 ATP + L-glutamine + HCO3- + H2O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate. HAMAP MF_01209

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1. HAMAP MF_01209

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3. HAMAP MF_01209

Subunit structure

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 By similarity. HAMAP MF_01209

Sequence similarities

Belongs to the carA family.

Contains 1 glutamine amidotransferase type-1 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 365365Carbamoyl-phosphate synthase small chain HAMAP MF_01209
PRO_0000112247

Regions

Domain170 – 357188Glutamine amidotransferase type-1
Region1 – 166166CPSase HAMAP MF_01209

Sites

Active site2451Nucleophile By similarity
Active site3301 By similarity
Active site3321 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q732I2-1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 0F31591333FA2CBA

FASTA36540,377
        10         20         30         40         50         60 
MKRQLILEDG TVLIGTGFGG EIEKSGEVVF TTGMTGYQET LSDPSYCGQI VTFTYPLIGN 

        70         80         90        100        110        120 
YGINRDDFES IHPSVNGLIV NEICDHPSNF RNEISLNDYL KERNIPGLAG IDTRKLTRKI 

       130        140        150        160        170        180 
RQYGTLRGRL CNMDADVEYI VSQLKATVFT DHVKRVSTKD PYPSPGRGHR VVLVDFGMKH 

       190        200        210        220        230        240 
GILRELNKRD CDVIVVPYNT TAEEILRLSP DGIMLSNGPG DPKDVPEAIE MLKDIIGKVP 

       250        260        270        280        290        300 
LFGICLGHQL FALASGANTS KLKFGHRGLN HPVKNLATGK VAITSQNHGY AVEEESVENT 

       310        320        330        340        350        360 
ELEITHVALN DGTVEGLRHK KFPAFTVQYH PEASAGPEDA NDLFEDFLTM IENFKKEGEE 


LCQNA 

« Hide

References

[1]"The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1."
Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.
Nucleic Acids Res. 32:977-988(2004) [PubMed: 14960714] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017194 Genomic DNA. Translation: AAS42835.1.
RefSeqNP_980227.1.

3D structure databases

SMRQ732I2. Positions 1-356.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ732I2.

Genome annotation databases

GeneID2751846.
GenomeReviewsGene locus BCE_3932 in contig AE017194_GR.
KEGGbca:BCE_3932.
NMPDRfig|222523.1.peg.3899.
TIGRBCE_3932.

Phylogenomic databases

eggNOGCOG0505.
HOGENOMHBG286341.
OMAFTYPELG.

Family and domain databases

HAMAPMF_01209_B. CPSase_S_chain_B.
[Tree]
InterProIPR006220. Anth_synthII.
IPR001317. CarbamoylP_synth_GATase_dom.
IPR006274. CarbamoylP_synth_ssu.
IPR002474. CarbamoylP_synth_ssu_N.
IPR011702. GATASE.
IPR017926. GATASE_1.
IPR000991. GATase_class1_C.
[Graphical view]
PANTHERPTHR11405:SF4. CarA_synth_small. 1 hit.
PfamPF00988. CPSase_sm_chain. 1 hit.
PF00117. GATase. 1 hit.
[Graphical view]
PRINTSPR00097. ANTSNTHASEII.
PR00099. CPSGATASE.
PR00096. GATASE.
TIGRFAMsTIGR01368. CPSaseIIsmall. 1 hit.
PROSITEPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCARA_BACC1
AccessionPrimary (citable) accession number: Q732I2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: July 5, 2004
Last modified: February 9, 2010
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents