Carbamoyl-phosphate synthase small chain - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot P0A6F1 (CARA_ECOLI)

Last modified June 16, 2009. Version 52. History...

Clusters with 100%, 90%, 50% identity |

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

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Names and origin

Protein names

Recommended name:
    Carbamoyl-phosphate synthase small chain
    EC=6.3.5.5
Alternative name(s):
    Carbamoyl-phosphate synthetase glutamine chain

Gene names

Name:	carA
Synonyms:	pyrA
Ordered Locus Names:	b0032, JW0030

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	382 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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 HCO(3)(-): step 1/1. HAMAP MF_01209 Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from HCO(3)(-): step 1/6. 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. Tetramer of heterodimers (alpha,beta)4. HAMAP MF_01209
Sequence similarities	Belongs to the carA family. Contains 1 glutamine amidotransferase type-1 domain.

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Ontologies

Keywords
Biological process	Amino-acid biosynthesis Arginine biosynthesis Pyrimidine biosynthesis
Domain	Glutamine amidotransferase
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	arginine biosynthetic process Inferred from electronic annotation. Source: HAMAP glutamine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW pyrimidine nucleotide biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity Inferred from electronic annotation. Source: HAMAP protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
carB	P00968	2	EBI-546107,EBI-546118
murE	P22188	1	EBI-546107,EBI-553061
yggM	P46142	1	EBI-546107,EBI-1125200

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 382

382

Carbamoyl-phosphate synthase small chain HAMAP MF_01209

PRO_0000112274

Regions

Domain

193 – 380

188

Glutamine amidotransferase type-1

Region

1 – 189

189

CPSase HAMAP MF_01209

Sites

Active site

269

Nucleophile By similarity

Active site

353

By similarity

Active site

355

By similarity

Secondary structure

382

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P0A6F1-1 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 60BC26366417443F
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FASTA

382

41,431

        10         20         30         40         50         60 
MIKSALLVLE DGTQFHGRAI GATGSAVGEV VFNTSMTGYQ EILTDPSYSR QIVTLTYPHI 

        70         80         90        100        110        120 
GNVGTNDADE ESSQVHAQGL VIRDLPLIAS NFRNTEDLSS YLKRHNIVAI ADIDTRKLTR 

       130        140        150        160        170        180 
LLREKGAQNG CIIAGDNPDA ALALEKARAF PGLNGMDLAK EVTTAEAYSW TQGSWTLTGG 

       190        200        210        220        230        240 
LPEAKKEDEL PFHVVAYDFG AKRNILRMLV DRGCRLTIVP AQTSAEDVLK MNPDGIFLSN 

       250        260        270        280        290        300 
GPGDPAPCDY AITAIQKFLE TDIPVFGICL GHQLLALASG AKTVKMKFGH HGGNHPVKDV 

       310        320        330        340        350        360 
EKNVVMITAQ NHGFAVDEAT LPANLRVTHK SLFDGTLQGI HRTDKPAFSF QGHPEASPGP 

       370        380 
HDAAPLFDHF IELIEQYRKT AK

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"DNA sequence of the carA gene and the control region of carAB: tandem promoters, respectively controlled by arginine and the pyrimidines, regulate the synthesis of carbamoyl-phosphate synthetase in Escherichia coli K-12." Piette J., Nyunoya H., Lusty C.J., Cunin R., Weyens G., Crabeel M., Charlier D.R.M., Glansdorff N., Pierard A. Proc. Natl. Acad. Sci. U.S.A. 81:4134-4138(1984) [PubMed: 6330744] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Multiple regulatory signals in the control region of the Escherichia coli carAB operon." Bouvier J., Patte J.-C., Stragier P. Proc. Natl. Acad. Sci. U.S.A. 81:4139-4143(1984) [PubMed: 6377309] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region." Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A. Nucleic Acids Res. 20:3305-3308(1992) [PubMed: 1630901] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"The carB gene of Escherichia coli: a duplicated gene coding for the large subunit of carbamoyl-phosphate synthetase." Nyunoya H., Lusty C.J. Proc. Natl. Acad. Sci. U.S.A. 80:4629-4633(1983) [PubMed: 6308632] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 361-382.
[7]	"A whole genome approach to in vivo DNA-protein interactions in E. coli." Wang M.X., Church G.M. Nature 360:606-610(1992) [PubMed: 1334233] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16. Strain: K12.
[8]	"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed: 9298646] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-12. Strain: K12 / EMG2.
[9]	"Structure of carbamoyl phosphate synthetase: a journey of 96 A from substrate to product." Thoden J.B., Holden H.M., Wesenberg G., Raushel F.M., Rayment I. Biochemistry 36:6305-6316(1997) [PubMed: 9174345] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[10]	"Carbamoyl phosphate synthetase: caught in the act of glutamine hydrolysis." Thoden J.B., Miran S.G., Phillips J.C., Howard A.J., Raushel F.M., Holden H.M. Biochemistry 37:8825-8831(1998) [PubMed: 9636022] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[11]	"The structure of carbamoyl phosphate synthetase determined to 2.1-A resolution." Thoden J.B., Raushel F.M., Benning M.M., Rayment I., Holden H.M. Acta Crystallogr. D 55:8-24(1999) [PubMed: 10089390] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[12]	"Carbamoyl phosphate synthetase: closure of the B-domain as a result of nucleotide binding." Thoden J.B., Wesenberg G., Raushel F.M., Holden H.M. Biochemistry 38:2347-2357(1999) [PubMed: 10029528] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[13]	"The small subunit of carbamoyl phosphate synthetase: snapshots along the reaction pathway." Thoden J.B., Huang X., Raushel F.M., Holden H.M. Biochemistry 38:16158-16166(1999) [PubMed: 10587438] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[14]	"The binding of inosine monophosphate to Escherichia coli carbamoyl phosphate synthetase." Thoden J.B., Raushel F.M., Wesenberg G., Holden H.M. J. Biol. Chem. 274:22502-22507(1999) [PubMed: 10428826] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).

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Cross-references

Sequence databases

J01597 Genomic DNA. Translation: AAA23538.1.
U00096 Genomic DNA. Translation: AAC73143.1.
AP009048 Genomic DNA. Translation: BAB96601.1.
X70017 Genomic DNA. Translation: CAA49615.1.

PIR

SYECCS. A01128.
B85484.

RefSeq

AP_000696.1.
NP_414573.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A9X	X-ray	1.80	B/D/F/H	2-380	[»]
1BXR	X-ray	2.10	B/D/F/H	1-382	[»]
1C30	X-ray	2.00	B/D/F/H	1-382	[»]
1C3O	X-ray	2.10	B/D/F/H	1-382	[»]
1CE8	X-ray	2.10	B/D/F/H	1-382	[»]
1CS0	X-ray	2.00	B/D/F/H	1-382	[»]
1JDB	X-ray	2.10	C/F/I/L	1-382	[»]
1KEE	X-ray	2.10	B/D/F/H	1-382	[»]
1M6V	X-ray	2.10	B/D/F/H	1-382	[»]
1T36	X-ray	2.10	B/D/F/H	1-382	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P0A6F1. 14 interactions.

2-D gel databases

SWISS-2DPAGE

P0A6F1.

ECO2DBASE

G041.4. 6TH EDITION.

Genome annotation databases

GeneID

949025.

GenomeReviews

Gene locus JW0030 in contig AP009048_GR.
Gene locus b0032 in contig U00096_GR.

KEGG

ecj:JW0030.
eco:b0032.

Organism-specific databases

EchoBASE

EB0132.

EcoGene

EG10134. carA.

CMR

Search...

Phylogenomic databases

HOGENOM

P0A6F1.

OMA

P0A6F1. LFDGSNC.

Enzyme and pathway databases

BioCyc

EcoCyc:CARBPSYN-SMALL.
MetaCyc:CARBPSYN-SMALL.

Family and domain databases

HAMAP

MF_01209.
[Tree]

InterPro

IPR006220. 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]

PANTHER

PTHR11405:SF4. CarA_synth_small. 1 hit.

Pfam

PF00988. CPSase_sm_chain. 1 hit.
PF00117. GATase. 1 hit.
[Graphical view]

PRINTS

PR00097. ANTSNTHASEII.
PR00099. CPSGATASE.
PR00096. GATASE.

TIGRFAMs

TIGR01368. CPSaseIIsmall. 1 hit.

PROSITE

PS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]

ProtoNet

Search...

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Entry information

Entry name

CARA_ECOLI

Accession

Primary (citable) accession number: P0A6F1
Secondary accession number(s): P00907

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	June 16, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2-D gel databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents