Gene Details


gene name: carA


locus tag k12ECK0033 Crenarchaeota Euryarchaeota Nanoarcheota Alphaproteobacteria Betaproteobacteria Gammaproteobacteria Deltaproteobacteria Epsilonproteobacteria Cyanobacteria Actinobacteridae Firmicutes Spirochaetes others Protist Microsporidia Fungi Metazoa Plantae
information on phylogenetic profile
locus tag mg1655b0032
locus tag w3110JW0030
gene name k12carA
locus namecarA
synonyms of locus namearg+ura, cap, pyrA, arg

scop id52317; 52021
superfamilyClass I glutamine amidotransferase-like; Carbamoyl phosphate synthetase, small subunit N-terminal domain
pfam idPF00117; PF00988
pfam domainGlutamine amidotransferase class-I; Carbamoyl-phosphate synthase small ch
tigrfam idTIGR01368
nameCPSaseIIsmall
functioncarbamoyl-phosphate synt

swissprot nameCARA_ECOLI
descriptionCarbamoyl-phosphate synthase small chain (EC 6.3.5.5) (Carbamoyl-|phosphate synthetase glutamine chain).
seq length382
fastaseq

go idGO:0006526; GO:0006221; GO:0006221
go termarginine biosynthesis; pyrimidine nucleotide biosynthesis; pyrimidine nucleotide biosynthesis

gene product descriptioncarbamoyl phosphate synthetase small subunit, glutamine amidotransferase
comment gene product description
evidenceE
context
gene product descEnzyme
cell locationCytoplasmic
featuresCDS

functional category codeE; F
functional categoryAmino acid transport and metabolism ; Nucleotide transport and metabolism

reference #1Domain structure of the large subunit of Escherichia coli carbamoyl phosphate synthetase. Location of the binding site for the allosteric inhibitor UMP in the COOH-terminal domain.

Rubio V., Cervera J., Lusty C., Bendala E., Britton H. (Biochemistry. 1991 Jan 29; 30(4):1068-75)
reference #2Alterations in the energetics of the carbamoyl phosphate synthetase reaction by site-directed modification of the essential sulfhydryl group.

Mullins L., Lusty C., Raushel F. (J Biol Chem. 1991 May 5; 266(13):8236-40)
reference #3Quantifying the allosteric properties of Escherichia coli carbamyl phosphate synthetase: determination of thermodynamic linked-function parameters in an ordered kinetic mechanism.

Braxton B., Mullins L., Raushel F., Reinhart G. (Biochemistry. 1992 Mar 3; 31(8):2309-16)
reference #4Carbamoyl phosphate synthetase: closure of the B-domain as a result of nucleotide binding.

Thoden J., Wesenberg G., Raushel F., Holden H. (Biochemistry. 1999 Feb 23; 38(8):2347-57)
reference #5The structure of carbamoyl phosphate synthetase determined to 2.1 A resolution.

Thoden J., Raushel F., Benning M., Rayment I., Holden H. (Acta Crystallogr D Biol Crystallogr. 1999 Jan; 55(Pt 1):8-24)
reference #6The binding of inosine monophosphate to Escherichia coli carbamoyl phosphate synthetase.

Thoden J., Raushel F., Wesenberg G., Holden H. (J Biol Chem. 1999 Aug 6; 274(32):22502-7)
reference #7The small subunit of carbamoyl phosphate synthetase: snapshots along the reaction pathway.

Thoden J., Huang X., Raushel F., Holden H. (Biochemistry. 1999 Dec 7; 38(49):16158-66)
reference #8A whole genome approach to in vivo DNA-protein interactions in E. coli.

Wang M., Church G. (Nature. 1992 Dec 10; 360(6404):606-10)
reference #9The carB gene of Escherichia coli: a duplicated gene coding for the large subunit of carbamoyl-phosphate synthetase.

Nyunoya H., Lusty C. (Proc Natl Acad Sci U S A. 1983 Aug; 80(15):4629-33)
reference #10DNA 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., Cunin R., Weyens G., Crabeel M., Charlier D., Glansdorff N., Piérard A. (Proc Natl Acad Sci U S A. 1984 Jul; 81(13):4134-8)
reference #11Multiple regulatory signals in the control region of the Escherichia coli carAB operon.

Bouvier J., Patte J., Stragier P. (Proc Natl Acad Sci U S A. 1984 Jul; 81(13):4139-43)
reference #12Structure of carbamoyl phosphate synthetase: a journey of 96 A from substrate to product.

Thoden J., Holden H., Wesenberg G., Raushel F., Rayment I. (Biochemistry. 1997 May 27; 36(21):6305-16)
reference #13Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.

Link A., Robison K., Church G. (Electrophoresis. 1997 Aug; 18(8):1259-313)
reference #14Carbamoyl phosphate synthetase: caught in the act of glutamine hydrolysis.

Thoden J., Miran S., Phillips J., Howard A., Raushel F., Holden H. (Biochemistry. 1998 Jun 23; 37(25):8825-31)

phylogenetic profile
 
69 233 208 205 307 218 263 281 286 291 276 276 186 83 221 54 178 186 1 290
307 290 293 289 288 273 276 289 306 289 313 320 298 256 256 367 372 377 381 385
386 376 382 392 1 1 1 372 311 466 466 482 489 489 513 504 503 447 506 354
362 307 339 331 336 364 349 254 357 311 383 277 308 256 266 290 300 300 299 307
316 302 291 310 52 322 274 306 301 299 301 307 301 307 1 1 1 1 1 1
1 1 312 1 294 294 294 294 294 298 298 298 308 308 306 304 306 306 306 289
1 551 456 429 521 523 458 666 764 771 770 54 420 418 511 507 496 659 547 539
535 729 738 731 597 766 767 642 635 640 389 483 490 467 466 675 675 676 345 262
249 1 1 1 1 1 1 372 317 301 59 364 241 314 312 1 337 1 1 338
229 230 257 243 256 238 246 264 244 233 224 229 241 234 1 342 254 1 119