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Q8F6R2 (CARA_LEPIN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 70. 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:LA_1239
OrganismLeptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601)
Taxonomic identifier189518 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesLeptospiraceaeLeptospira

Protein attributes

Sequence length362 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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 362362Carbamoyl-phosphate synthase small chain HAMAP MF_01209
PRO_0000112289

Regions

Domain176 – 362187Glutamine amidotransferase type-1
Region1 – 172172CPSase HAMAP MF_01209

Sites

Active site2521Nucleophile By similarity
Active site3351 By similarity
Active site3371 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8F6R2 [UniParc].

Last modified August 10, 2010. Version 2.
Checksum: ECB2DC06136069AC

FASTA36240,130
        10         20         30         40         50         60 
MKAFLVLDNG TIFEGESFGY ETESVGEIVF NTSMAGYQEI LTDPSYCNQI ITLTYPMIGN 

        70         80         90        100        110        120 
YGIHPDNMES SKIQASGLIV KEYVDLPSNF KSEKTLSQFL KEYKIPAIQG IDTRKLTRFI 

       130        140        150        160        170        180 
RTNGSPNGGI FVASEYSPSF LEKVKSFPGI INADLAKVVT TSSKYIFGTH TGKKFKLAVY 

       190        200        210        220        230        240 
DYGVKTNILR LLDANGFAVT VYPAKTPSEE IMKEGTDAFF LSNGPGDPAP LDYAIASTQK 

       250        260        270        280        290        300 
IMEKRYPLFG ICLGHQIIGL SLGKKTEKMK FGHRGGNQPV KNLETGQVEI TSQNHGFAVI 

       310        320        330        340        350        360 
DDQKQDEPIS FLNLNDHTVE GILKSGYPLL TVQYHPESAP GPNDSRYLFQ KFYDLVEKTK 


KG 

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References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE010300 Genomic DNA. Translation: AAN48438.2.
RefSeqNP_711420.2. NC_004342.2.

3D structure databases

ProteinModelPortalQ8F6R2.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1150582.
GenomeReviewsGene locus LA_1239 in contig AE010300_GR.
KEGGlil:LA_1239.
NMPDRfig|189518.1.peg.1239.
PATRIC22383329. VBILepInt91350_1239.

Phylogenomic databases

HOGENOMHBG286341.
OMAGWNDEDS.
ProtClustDBPRK12564.

Enzyme and pathway databases

BioCycLINT189518:LA1239-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.
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_LEPIN
AccessionPrimary (citable) accession number: Q8F6R2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 6, 2003
Last sequence update: August 10, 2010
Last modified: January 25, 2012
This is version 70 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