CARA_ECOLI
ID CARA_ECOLI Reviewed; 382 AA.
AC P0A6F1; P00907;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Carbamoyl-phosphate synthase small chain;
DE EC=6.3.5.5;
DE AltName: Full=Carbamoyl-phosphate synthetase glutamine chain;
GN Name=carA; Synonyms=pyrA; OrderedLocusNames=b0032, JW0030;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6330744; DOI=10.1073/pnas.81.13.4134;
RA Piette J., Nyunoya H., Lusty C.J., Cunin R., Weyens G., Crabeel M.,
RA Charlier D.R.M., Glansdorff N., Pierard A.;
RT "DNA sequence of the carA gene and the control region of carAB: tandem
RT promoters, respectively controlled by arginine and the pyrimidines,
RT regulate the synthesis of carbamoyl-phosphate synthetase in Escherichia
RT coli K-12.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:4134-4138(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6377309; DOI=10.1073/pnas.81.13.4139;
RA Bouvier J., Patte J.-C., Stragier P.;
RT "Multiple regulatory signals in the control region of the Escherichia coli
RT carAB operon.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:4139-4143(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1630901; DOI=10.1093/nar/20.13.3305;
RA Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K.,
RA Mizobuchi K., Nakata A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 0-
RT 2.4 min region.";
RL Nucleic Acids Res. 20:3305-3308(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 361-382.
RX PubMed=6308632; DOI=10.1073/pnas.80.15.4629;
RA Nyunoya H., Lusty C.J.;
RT "The carB gene of Escherichia coli: a duplicated gene coding for the large
RT subunit of carbamoyl-phosphate synthetase.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:4629-4633(1983).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
RC STRAIN=K12;
RX PubMed=1334233; DOI=10.1038/360606a0;
RA Wang M.X., Church G.M.;
RT "A whole genome approach to in vivo DNA-protein interactions in E. coli.";
RL Nature 360:606-610(1992).
RN [8]
RP PROTEIN SEQUENCE OF 1-12.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [9]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX PubMed=9174345; DOI=10.1021/bi970503q;
RA Thoden J.B., Holden H.M., Wesenberg G., Raushel F.M., Rayment I.;
RT "Structure of carbamoyl phosphate synthetase: a journey of 96 A from
RT substrate to product.";
RL Biochemistry 36:6305-6316(1997).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=9636022; DOI=10.1021/bi9807761;
RA Thoden J.B., Miran S.G., Phillips J.C., Howard A.J., Raushel F.M.,
RA Holden H.M.;
RT "Carbamoyl phosphate synthetase: caught in the act of glutamine
RT hydrolysis.";
RL Biochemistry 37:8825-8831(1998).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), AND SUBUNIT.
RX PubMed=10089390; DOI=10.1107/s0907444998006234;
RA Thoden J.B., Raushel F.M., Benning M.M., Rayment I., Holden H.M.;
RT "The structure of carbamoyl phosphate synthetase determined to 2.1-A
RT resolution.";
RL Acta Crystallogr. D 55:8-24(1999).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX PubMed=10029528; DOI=10.1021/bi982517h;
RA Thoden J.B., Wesenberg G., Raushel F.M., Holden H.M.;
RT "Carbamoyl phosphate synthetase: closure of the B-domain as a result of
RT nucleotide binding.";
RL Biochemistry 38:2347-2357(1999).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=10587438; DOI=10.1021/bi991741j;
RA Thoden J.B., Huang X., Raushel F.M., Holden H.M.;
RT "The small subunit of carbamoyl phosphate synthetase: snapshots along the
RT reaction pathway.";
RL Biochemistry 38:16158-16166(1999).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX PubMed=10428826; DOI=10.1074/jbc.274.32.22502;
RA Thoden J.B., Raushel F.M., Wesenberg G., Holden H.M.;
RT "The binding of inosine monophosphate to Escherichia coli carbamoyl
RT phosphate synthetase.";
RL J. Biol. Chem. 274:22502-22507(1999).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP +
CC carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate;
CC Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359,
CC ChEBI:CHEBI:456216; EC=6.3.5.5;
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl
CC phosphate from bicarbonate: step 1/1.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 1/3.
CC -!- SUBUNIT: Composed of two chains; the small (or glutamine) chain
CC promotes the hydrolysis of glutamine to ammonia, which is used by the
CC large (or ammonia) chain to synthesize carbamoyl phosphate. Tetramer of
CC heterodimers (alpha,beta)4. {ECO:0000269|PubMed:10089390}.
CC -!- INTERACTION:
CC P0A6F1; P00968: carB; NbExp=14; IntAct=EBI-546107, EBI-546118;
CC P0A6F1; P22188: murE; NbExp=2; IntAct=EBI-546107, EBI-553061;
CC P0A6F1; P0AD21: yejG; NbExp=2; IntAct=EBI-546107, EBI-1127956;
CC -!- SIMILARITY: Belongs to the CarA family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; J01597; AAA23538.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73143.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96601.1; -; Genomic_DNA.
DR EMBL; X70017; CAA49615.1; -; Genomic_DNA.
DR PIR; A01128; SYECCS.
DR PIR; B85484; B85484.
DR RefSeq; NP_414573.1; NC_000913.3.
DR RefSeq; WP_000597260.1; NZ_STEB01000010.1.
DR PDB; 1A9X; X-ray; 1.80 A; B/D/F/H=2-380.
DR PDB; 1BXR; X-ray; 2.10 A; B/D/F/H=1-382.
DR PDB; 1C30; X-ray; 2.00 A; B/D/F/H=1-382.
DR PDB; 1C3O; X-ray; 2.10 A; B/D/F/H=1-382.
DR PDB; 1CE8; X-ray; 2.10 A; B/D/F/H=1-380.
DR PDB; 1CS0; X-ray; 2.00 A; B/D/F/H=1-382.
DR PDB; 1JDB; X-ray; 2.10 A; C/F/I/L=1-382.
DR PDB; 1KEE; X-ray; 2.10 A; B/D/F/H=1-382.
DR PDB; 1M6V; X-ray; 2.10 A; B/D/F/H=1-382.
DR PDB; 1T36; X-ray; 2.10 A; B/D/F/H=1-382.
DR PDBsum; 1A9X; -.
DR PDBsum; 1BXR; -.
DR PDBsum; 1C30; -.
DR PDBsum; 1C3O; -.
DR PDBsum; 1CE8; -.
DR PDBsum; 1CS0; -.
DR PDBsum; 1JDB; -.
DR PDBsum; 1KEE; -.
DR PDBsum; 1M6V; -.
DR PDBsum; 1T36; -.
DR AlphaFoldDB; P0A6F1; -.
DR SMR; P0A6F1; -.
DR BioGRID; 4263445; 52.
DR BioGRID; 853269; 2.
DR ComplexPortal; CPX-1937; Carbamoyl phosphate synthetase complex.
DR DIP; DIP-35412N; -.
DR IntAct; P0A6F1; 16.
DR STRING; 511145.b0032; -.
DR BindingDB; P0A6F1; -.
DR MEROPS; C26.954; -.
DR SWISS-2DPAGE; P0A6F1; -.
DR jPOST; P0A6F1; -.
DR PaxDb; P0A6F1; -.
DR PRIDE; P0A6F1; -.
DR EnsemblBacteria; AAC73143; AAC73143; b0032.
DR EnsemblBacteria; BAB96601; BAB96601; BAB96601.
DR GeneID; 66671678; -.
DR GeneID; 949025; -.
DR KEGG; ecj:JW0030; -.
DR KEGG; eco:b0032; -.
DR PATRIC; fig|1411691.4.peg.2252; -.
DR EchoBASE; EB0132; -.
DR eggNOG; COG0505; Bacteria.
DR HOGENOM; CLU_035901_1_1_6; -.
DR InParanoid; P0A6F1; -.
DR OMA; CFNTGMT; -.
DR PhylomeDB; P0A6F1; -.
DR BioCyc; EcoCyc:CARBPSYN-SMALL; -.
DR BioCyc; MetaCyc:CARBPSYN-SMALL; -.
DR SABIO-RK; P0A6F1; -.
DR UniPathway; UPA00068; UER00171.
DR UniPathway; UPA00070; UER00115.
DR EvolutionaryTrace; P0A6F1; -.
DR PRO; PR:P0A6F1; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005951; C:carbamoyl-phosphate synthase complex; IDA:EcoCyc.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IMP:EcoliWiki.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006526; P:arginine biosynthetic process; IMP:EcoliWiki.
DR GO; GO:0006541; P:glutamine metabolic process; IMP:EcoliWiki.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
DR CDD; cd01744; GATase1_CPSase; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.50.30.20; -; 1.
DR HAMAP; MF_01209; CPSase_S_chain; 1.
DR InterPro; IPR006274; CarbamoylP_synth_ssu.
DR InterPro; IPR002474; CarbamoylP_synth_ssu_N.
DR InterPro; IPR036480; CarbP_synth_ssu_N_sf.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR035686; CPSase_GATase1.
DR InterPro; IPR017926; GATASE.
DR Pfam; PF00988; CPSase_sm_chain; 1.
DR Pfam; PF00117; GATase; 1.
DR SMART; SM01097; CPSase_sm_chain; 1.
DR SUPFAM; SSF52021; SSF52021; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR TIGRFAMs; TIGR01368; CPSaseIIsmall; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding;
KW Direct protein sequencing; Glutamine amidotransferase; Ligase;
KW Nucleotide-binding; Pyrimidine biosynthesis; Reference proteome.
FT CHAIN 1..382
FT /note="Carbamoyl-phosphate synthase small chain"
FT /id="PRO_0000112274"
FT DOMAIN 193..380
FT /note="Glutamine amidotransferase type-1"
FT REGION 1..189
FT /note="CPSase"
FT ACT_SITE 269
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 353
FT /evidence="ECO:0000250"
FT ACT_SITE 355
FT /evidence="ECO:0000250"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 14..19
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 23..33
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 39..43
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 98..104
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 108..113
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 115..125
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 128..137
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 140..149
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:1T36"
FT HELIX 159..162
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:1A9X"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 192..200
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 203..211
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 214..220
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 225..229
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 234..238
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 242..245
FT /evidence="ECO:0007829|PDB:1CE8"
FT HELIX 249..258
FT /evidence="ECO:0007829|PDB:1A9X"
FT TURN 259..262
FT /evidence="ECO:0007829|PDB:1JDB"
FT STRAND 265..268
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 270..278
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 283..299
FT /evidence="ECO:0007829|PDB:1A9X"
FT TURN 300..303
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 304..316
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:1CS0"
FT STRAND 325..331
FT /evidence="ECO:0007829|PDB:1A9X"
FT TURN 332..334
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 337..352
FT /evidence="ECO:0007829|PDB:1A9X"
FT STRAND 357..359
FT /evidence="ECO:0007829|PDB:1A9X"
FT TURN 362..364
FT /evidence="ECO:0007829|PDB:1A9X"
FT HELIX 365..379
FT /evidence="ECO:0007829|PDB:1A9X"
SQ SEQUENCE 382 AA; 41431 MW; 60BC26366417443F CRC64;
MIKSALLVLE DGTQFHGRAI GATGSAVGEV VFNTSMTGYQ EILTDPSYSR QIVTLTYPHI
GNVGTNDADE ESSQVHAQGL VIRDLPLIAS NFRNTEDLSS YLKRHNIVAI ADIDTRKLTR
LLREKGAQNG CIIAGDNPDA ALALEKARAF PGLNGMDLAK EVTTAEAYSW TQGSWTLTGG
LPEAKKEDEL PFHVVAYDFG AKRNILRMLV DRGCRLTIVP AQTSAEDVLK MNPDGIFLSN
GPGDPAPCDY AITAIQKFLE TDIPVFGICL GHQLLALASG AKTVKMKFGH HGGNHPVKDV
EKNVVMITAQ NHGFAVDEAT LPANLRVTHK SLFDGTLQGI HRTDKPAFSF QGHPEASPGP
HDAAPLFDHF IELIEQYRKT AK
