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Q819S2 (CARA_BACCR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:BC_3887
OrganismBacillus cereus (strain ATCC 14579 / DSM 31)
Taxonomic identifier226900 [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.

Sequence similarities

Belongs to the CarA family.

Contains 1 glutamine amidotransferase type-1 domain.

Sequence caution

The sequence AAP10808.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 365365Carbamoyl-phosphate synthase small chain HAMAP MF_01209
PRO_0000112249

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
Q819S2 [UniParc].

Last modified March 1, 2005. Version 2.
Checksum: 0C08E19086E4665A

FASTA36540,362
        10         20         30         40         50         60 
MKRQLILEDG TVLIGTGFGG EIEKSGEVVF TTGMTGYQET LSDPSYCGQI VTFTYPLIGN 

        70         80         90        100        110        120 
YGINRDDFES IHPSVNGLIV NEICNHPSNF 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 
DLEITHVALN DGTVEGLRHK KFPAFTVQYH PEASAGPEDA NDLFEDFLTM IENFKKEGEE 


LCQNA 

« Hide

References

[1]"Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis."
Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G. expand/collapse author list , Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.
Nature 423:87-91(2003) [PubMed: 12721630] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 14579 / DSM 31.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016877 Genomic DNA. Translation: AAP10808.1. Different initiation.
RefSeqNP_833607.1. NC_004722.1.

3D structure databases

ProteinModelPortalQ819S2.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ819S2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000033695; EBBACP00000032901; EBBACG00000033686.
GeneID1206232.
GenomeReviewsGene locus BC_3887 in contig AE016877_GR.
KEGGbce:BC3887.
PATRIC32603811. VBIBacCer54481_4009.

Phylogenomic databases

eggNOGCOG0505.
GeneTreeEBGT00070000032080.
HOGENOMHBG286341.
OMAFTYPELG.
PhylomeDBQ819S2.
ProtClustDBPRK12564.

Enzyme and pathway databases

BioCycBCER226900:BC_3887-MONOMER.

Family and domain databases

HAMAPMF_01209. CPSase_S_chain.
[Tree]
InterProIPR006274. CarbamoylP_synth_ssu.
IPR002474. CarbamoylP_synth_ssu_N.
IPR017926. GATASE_1.
[Graphical view]
Gene3DG3DSA:3.50.30.20. G3DSA:3.50.30.20. 1 hit.
KOK01956.
PANTHERPTHR11405:SF4. CarA_synth_small. 1 hit.
PfamPF00988. CPSase_sm_chain. 1 hit.
PF00117. GATase. 1 hit.
[Graphical view]
SMARTSM01097. CPSase_sm_chain. 1 hit.
[Graphical view]
SUPFAMSSF52021. CP_synthsmall. 1 hit.
TIGRFAMsTIGR01368. CPSaseIIsmall. 1 hit.
PROSITEPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCARA_BACCR
AccessionPrimary (citable) accession number: Q819S2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: March 1, 2005
Last modified: January 25, 2012
This is version 68 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families