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Reviewed, UniProtKB/Swiss-Prot P25993 (CARA_BACSU)

Last modified November 3, 2009. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 pyrimidine-specific small chain
    EC=6.3.5.5
Alternative name(s):
    Carbamoyl-phosphate synthetase glutamine chain
Gene names
Name: pyrAA
Ordered Locus Names: BSU15510
OrganismBacillus subtilis [Complete proteome] [HAMAP]
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length364 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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

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. 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 – 364364Carbamoyl-phosphate synthase pyrimidine-specific small chain HAMAP MF_01209
PRO_0000112255

Regions

Domain171 – 356186Glutamine amidotransferase type-1
Region1 – 167167CPSase HAMAP MF_01209

Sites

Active site2461Nucleophile By similarity
Active site3291 By similarity
Active site3311 By similarity

Sequences

Sequence LengthMass (Da)Tools
P25993-1 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: 676304F876709FC0

FASTA36440,119
        10         20         30         40         50         60 
MKRRLVLENG AVFEGEAFGS LEHNMGEVVF NTGMTGYQEI LSDPSYCGQI VTLTYPLIGN 

        70         80         90        100        110        120 
YGINRDDFES ITPFVKGLII KELCELPSNW RSAYTLDEYL KMKNIPGLQG IDTRKLTRMI 

       130        140        150        160        170        180 
RTAGALKGTF ASSDEDIEAV LKRLNETELP RNQVSQVSAK TAYPSPGRGK RIVLVDFGMK 

       190        200        210        220        230        240 
HGILRELNKR KCDVIVVPYN ITAEEVLQLK PDGIMLSNGP GDPKDVPEAI EMIKGVLGKV 

       250        260        270        280        290        300 
PLFGICLGHQ LFALACGANT EKMKFGHRGS NHPVKELATG KVALTSQNHG YTVSSISKTE 

       310        320        330        340        350        360 
LEVTHIAIND DTIEGLKHKT LPAFTVQYHP EASPGPEDAN HLFDRFIEMI ETTEKEGEAV 


CQNA 

« Hide

References

« Hide 'large scale' references
[1]"Functional organization and nucleotide sequence of the Bacillus subtilis pyrimidine biosynthetic operon."
Quinn C.L., Stephenson B.T., Switzer R.L.
J. Biol. Chem. 266:9113-9127(1991) [PubMed: 1709162] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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. expand/collapse author list , 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: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.

Cross-references

Sequence databases

M59757 Genomic DNA. Translation: AAA21269.1.
AL009126 Genomic DNA. Translation: CAB13425.1.
PIRE39845.
RefSeqNP_389434.1.

3D structure databases

HSSPHSSP built from PDB template 1A9X based on UniProtKB P00907.
ModBaseSearch...

Genome annotation databases

GeneID937368.
GenomeReviewsGene locus BSU15510 in contig AL009126_GR.
KEGGbsu:BSU15510.
NMPDRfig|224308.1.peg.1553.

Organism-specific databases

SubtiListBG10715. pyrAA. [Micado]
CMRSearch...

Phylogenomic databases

HOGENOMP25993.
OMALFDGSNC.

Enzyme and pathway databases

BioCycBSUB224308:BSU1553-MON.
BRENDA6.3.5.5. 150.

Family and domain databases

HAMAPMF_01209.
[Tree]
InterProIPR006220. Anth_synthII.
IPR001317. CarbamoylP_synth_GATase.
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_BACSU
AccessionPrimary (citable) accession number: P25993
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: November 3, 2009
This is version 77 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

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

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