(data stored in SCRATCH zone)

SWISSPROT: B7UI78_ECO27

ID   B7UI78_ECO27            Unreviewed;      1073 AA.
AC   B7UI78;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 72.
DE   RecName: Full=Carbamoyl-phosphate synthase large chain {ECO:0000256|HAMAP-Rule:MF_01210};
DE            EC=6.3.5.5 {ECO:0000256|HAMAP-Rule:MF_01210};
DE   AltName: Full=Carbamoyl-phosphate synthetase ammonia chain {ECO:0000256|HAMAP-Rule:MF_01210};
GN   Name=carB {ECO:0000256|HAMAP-Rule:MF_01210,
GN   ECO:0000313|EMBL:CAS07581.1};
GN   OrderedLocusNames=E2348C_0033 {ECO:0000313|EMBL:CAS07581.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS07581.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS07581.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
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; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01210, ECO:0000256|SAAS:SAAS01124510};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|SAAS:SAAS00981842};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|SAAS:SAAS00611658};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis;
CC       carbamoyl phosphate from bicarbonate: step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_01210, ECO:0000256|SAAS:SAAS00981844}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; (S)-dihydroorotate from bicarbonate: step 1/3.
CC       {ECO:0000256|HAMAP-Rule:MF_01210, ECO:0000256|SAAS:SAAS01000080}.
CC   -!- SUBUNIT: Composed of two chains; the small (or glutamine) chain
CC       promotes the hydrolysis of glutamine to ammonia, which is used by
CC       the large (or ammonia) chain to synthesize carbamoyl phosphate.
CC       {ECO:0000256|HAMAP-Rule:MF_01210, ECO:0000256|SAAS:SAAS00570548}.
CC   -!- SIMILARITY: Belongs to the CarB family. {ECO:0000256|HAMAP-
CC       Rule:MF_01210, ECO:0000256|SAAS:SAAS00570556}.
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DR   EMBL; FM180568; CAS07581.1; -; Genomic_DNA.
DR   RefSeq; WP_001126342.1; NC_011601.1.
DR   EnsemblBacteria; CAS07581; CAS07581; E2348C_0033.
DR   KEGG; ecg:E2348C_0033; -.
DR   HOGENOM; HOG000234582; -.
DR   KO; K01955; -.
DR   OMA; AVFPFNK; -.
DR   BioCyc; ECOL574521:E2348C_RS00175-MONOMER; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000008205; Chromosome.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01424; MGS_CPS_II; 1.
DR   Gene3D; 1.10.1030.10; -; 1.
DR   Gene3D; 3.40.50.1380; -; 1.
DR   HAMAP; MF_01210_A; CPSase_L_chain_A; 1.
DR   HAMAP; MF_01210_B; CPSase_L_chain_B; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR006275; CarbamoylP_synth_lsu.
DR   InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
DR   InterPro; IPR036897; CarbamoylP_synth_lsu_oligo_sf.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
DR   InterPro; IPR011607; MGS-like_dom.
DR   InterPro; IPR036914; MGS-like_dom_sf.
DR   InterPro; IPR033937; MGS_CPS_CarB.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   Pfam; PF02786; CPSase_L_D2; 2.
DR   Pfam; PF02787; CPSase_L_D3; 1.
DR   Pfam; PF02142; MGS; 1.
DR   PRINTS; PR00098; CPSASE.
DR   SMART; SM01096; CPSase_L_D3; 1.
DR   SMART; SM00851; MGS; 1.
DR   SUPFAM; SSF48108; SSF48108; 1.
DR   SUPFAM; SSF52335; SSF52335; 1.
DR   SUPFAM; SSF52440; SSF52440; 2.
DR   TIGRFAMs; TIGR01369; CPSaseII_lrg; 1.
DR   PROSITE; PS50975; ATP_GRASP; 2.
DR   PROSITE; PS00866; CPSASE_1; 2.
DR   PROSITE; PS00867; CPSASE_2; 2.
PE   3: Inferred from homology;
DR   PRODOM; B7UI78.
DR   SWISS-2DPAGE; B7UI78.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01210,
KW   ECO:0000256|SAAS:SAAS00981831};
KW   Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01210,
KW   ECO:0000256|SAAS:SAAS00981841};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01210, ECO:0000256|PROSITE-
KW   ProRule:PRU00409, ECO:0000256|SAAS:SAAS00710217};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01210,
KW   ECO:0000256|SAAS:SAAS00710245};
KW   Magnesium {ECO:0000256|SAAS:SAAS00981805};
KW   Manganese {ECO:0000256|SAAS:SAAS00459951};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00086100};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01210,
KW   ECO:0000256|PROSITE-ProRule:PRU00409, ECO:0000256|SAAS:SAAS00710285};
KW   Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01210,
KW   ECO:0000256|SAAS:SAAS01000143};
KW   Repeat {ECO:0000256|HAMAP-Rule:MF_01210,
KW   ECO:0000256|SAAS:SAAS00981845}.
FT   DOMAIN      133    328       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   DOMAIN      679    870       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   REGION        1    403       Carboxyphosphate synthetic domain.
FT                                {ECO:0000256|HAMAP-Rule:MF_01210}.
FT   REGION      404    553       Oligomerization domain.
FT                                {ECO:0000256|HAMAP-Rule:MF_01210}.
FT   REGION      554    936       Carbamoyl phosphate synthetic domain.
FT                                {ECO:0000256|HAMAP-Rule:MF_01210}.
FT   REGION      937   1073       Allosteric domain. {ECO:0000256|HAMAP-
FT                                Rule:MF_01210}.
SQ   SEQUENCE   1073 AA;  117900 MW;  13B30A1A3916A193 CRC64;
     MPKRTDIKSI LILGAGPIVI GQACEFDYSG AQACKALREE GYRVILVNSN PATIMTDPEM
     ADATYIEPIH WEVVRKIIEK ERPDAVLPTM GGQTALNCAL ELERQGVLEE FGVTMIGATA
     DAIDKAEDRR RFDVAMKKIG LETARSGIAH SMEEALAVAA EVGFPCIIRP SFTMGGSGGG
     IAYNREEFEE ICARGLDLSP TKELLIDESL IGWKEYEMEV VRDKNDNCII VCSIENFDAM
     GIHTGDSITV APAQTLTDKE YQIMRNASMA VLREIGVETG GSNVQFAVNP KNGRLIVIEM
     NPRVSRSSAL ASKATGFPIA KVAAKLAVGY TLDELMNDIT GGRTPASFEP SIDYVVTKIP
     RFNFEKFAGA NDRLTTQMKS VGEVMAIGRT QQESLQKALR GLEVGATGFD PKVSLDDPEA
     LTKIRRELKD AGAERIWYIA DAFRAGLSVD GVFNLTNIDR WFLVQIEELV RLEEKVAEVG
     ITGLNAEFLR QLKRKGFADA RLAKLAGVRE AEIRKLRDQY DLHPVYKRVD TCAAEFATDT
     AYMYSTYEEE CEANPSTDRE KIMVLGGGPN RIGQGIEFDY CCVHASLALR EDGYETIMVN
     CNPETVSTDY DTSDRLYFEP VTLEDVLEIV RIEKPKGVIV QYGGQTPLKL ARALEAAGVP
     VIGTSPDAID RAEDRERFQH AVERLKLKQP ANATVTTIEM AVEKAKEIGY PLVVRPSYVL
     GGRAMEIVYD EADLRRYFQT AVSVSNDAPV LLDHFLDDAV EVDVDAICDG EMVLIGGIME
     HIEQAGVHSG DSACSLPAYT LSQEIQDVMR QQVQKLAFEL QVRGLMNVQF AVKNNEVYLI
     EVNPRAARTV PFVSKATGVP LAKVAARVMA GKSLAEQGVT KEVIPPYYSV KEVVLPFNKF
     PGVDPLLGPE MRSTGEVMGV GRTFAEAFAK AQLGSNSTMK KHGRALLSVR EGDKERVVDL
     AAKLLKQGFE LDATHGTAIV LGEAGINPRL VNKVHEGRPH IQDRIKNGEY TYIINTTSGR
     RAIEDSRVIR RSALQYKVHY DTTLNGGFAT AMALNADATE KVISVQEMHA QIK
//

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