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P58893 (CARA_CORGL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 76. 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:Cgl1610, cg1814
OrganismCorynebacterium glutamicum (Brevibacterium flavum)
Taxonomic identifier1718 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length393 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 – 393393Carbamoyl-phosphate synthase small chain HAMAP MF_01209
PRO_0000112271

Regions

Domain195 – 390196Glutamine amidotransferase type-1
Region1 – 194194CPSase HAMAP MF_01209

Sites

Active site2731Nucleophile By similarity
Active site3631 By similarity
Active site3651 By similarity

Sequences

Sequence LengthMass (Da)Tools
P58893 [UniParc].

Last modified July 11, 2002. Version 1.
Checksum: 96329ACE03A27C95

FASTA39342,134
        10         20         30         40         50         60 
MSKDTTTYQG VTEIGSVPAY LVLADGRTFT GFGFGAIGTT LGEAVFTTAM TGYQETMTDP 

        70         80         90        100        110        120 
SYHRQIVVAT APQIGNTGWN DEDNESRDGK IWVAGLVIRD LAARVSNWRA TTSLQQEMAG 

       130        140        150        160        170        180 
QGIVGIGGID TRALVRHLRN EGSIAAGIFS GADAQRPVEE LVEIVKNQPA MTGANLSVEV 

       190        200        210        220        230        240 
SADETYVIEA EGEERHTVVA YDLGIKQNTP RRFSARGVRT VIVPAETPFE DIKQYNPSGV 

       250        260        270        280        290        300 
FISNGPGDPA AADVMVDIVR EVLEADIPFF GICFGNQILG RAFGMETYKL KFGHRGINVP 

       310        320        330        340        350        360 
VKNHITGKID ITAQNHGFAL KGEAGQEFET DFGTAIVTHT CLNDGVVEGI ALKSGRAYSV 

       370        380        390 
QYHPEAAAGP NDASPLFDQF VELMDADAQK KGA 

« Hide

References

[1]"Complete genomic sequence of Corynebacterium glutamicum ATCC 13032."
Nakagawa S.
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[2]"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins."
Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. expand/collapse author list , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.
J. Biotechnol. 104:5-25(2003) [PubMed: 12948626] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000036 Genomic DNA. Translation: BAB99003.1.
BX927152 Genomic DNA. Translation: CAF21619.1.
RefSeqNP_600824.1. NC_003450.3.
YP_225895.1. NC_006958.1.

3D structure databases

ProteinModelPortalP58893.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1019578.
3343549.
GenomeReviewsGene locus Cgl1610 in contig BA000036_GR.
Gene locus cg1814 in contig BX927147_GR.
KEGGcgb:cg1814.
cgl:NCgl1548.
PATRIC21495257. VBICorGlu203724_1572.

Phylogenomic databases

HOGENOMHBG286341.
OMAGWNDEDS.
PhylomeDBP58893.
ProtClustDBPRK12564.

Enzyme and pathway databases

BioCycCGLU196627:CG1814-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_CORGL
AccessionPrimary (citable) accession number: P58893
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: July 11, 2002
Last modified: January 25, 2012
This is version 76 of the entry and version 1 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