ID I2SLM0_ECOLX Unreviewed; 1073 AA. AC I2SLM0; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 06-MAR-2013, entry version 7. DE RecName: Full=Carbamoyl-phosphate synthase large chain; DE EC=6.3.5.5; DE AltName: Full=Carbamoyl-phosphate synthetase ammonia chain; GN Name=carB; ORFNames=EC12264_0032; OS Escherichia coli 1.2264. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=869675; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=1.2264; RA Brinkac L., Radune D., Sanka R., Selengut J., DebRoy C., Feng P., RA Fratamico P.M., Kapur V., Kariyawasam S., Losada L., Nierman W.C., RA Nelson K.; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2 CC ADP + phosphate + L-glutamate + carbamoyl phosphate. CC -!- COFACTOR: Binds 4 magnesium or manganese ions per subunit (By CC similarity). CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; CC carbamoyl phosphate from bicarbonate: step 1/1. CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo CC pathway; (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 CC the large (or ammonia) chain to synthesize carbamoyl phosphate (By CC similarity). CC -!- SIMILARITY: Belongs to the CarB family. CC -!- SIMILARITY: Contains 2 ATP-grasp domains. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. 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; AEZO02000031; EIH21691.1; -; Genomic_DNA. DR ProteinModelPortal; I2SLM0; -. DR OMA; PMANLAT; -. DR UniPathway; UPA00068; UER00171. DR UniPathway; UPA00070; UER00115. DR GO; GO:0005524; F:ATP binding; IEA:HAMAP. DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP. DR GO; GO:0030145; F:manganese ion binding; IEA:HAMAP. DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006526; P:arginine biosynthetic process; IEA:HAMAP. DR Gene3D; 1.10.1030.10; -; 1. DR Gene3D; 3.30.1490.20; -; 2. DR Gene3D; 3.30.470.20; -; 2. DR Gene3D; 3.40.50.1380; -; 1. DR Gene3D; 3.40.50.20; -; 2. 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; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR013816; ATP_grasp_subdomain_2. DR InterPro; IPR006275; CarbamoylP_synth_lsu. DR InterPro; IPR005481; CarbamoylP_synth_lsu_N. DR InterPro; IPR005480; CarbamoylP_synth_lsu_oligo. 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; IPR016185; PreATP-grasp_dom. DR Pfam; PF00289; CPSase_L_chain; 2. 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; CarbamoylP_synth_lsu_oligo; 1. DR SUPFAM; SSF52335; MGS-like_dom; 1. DR SUPFAM; SSF52440; PreATP-grasp-like; 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; KW Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; Ligase; KW Magnesium; Manganese; Metal-binding; Nucleotide-binding; KW Pyrimidine biosynthesis; Repeat. FT DOMAIN 133 328 ATP-grasp 1 (By similarity). FT DOMAIN 679 870 ATP-grasp 2 (By similarity). FT NP_BIND 159 216 ATP (By similarity). FT NP_BIND 705 762 ATP (By similarity). FT REGION 1 403 Carboxyphosphate synthetic domain (By FT similarity). FT REGION 404 553 Oligomerization domain (By similarity). FT REGION 554 936 Carbamoyl phosphate synthetic domain (By FT similarity). FT REGION 937 1073 Allosteric domain (By similarity). FT METAL 285 285 Magnesium or manganese 1 (By similarity). FT METAL 299 299 Magnesium or manganese 1 (By similarity). FT METAL 299 299 Magnesium or manganese 2 (By similarity). FT METAL 301 301 Magnesium or manganese 2 (By similarity). FT METAL 829 829 Magnesium or manganese 3 (By similarity). FT METAL 841 841 Magnesium or manganese 3 (By similarity). FT METAL 841 841 Magnesium or manganese 4 (By similarity). FT METAL 843 843 Magnesium or manganese 4 (By similarity). SQ SEQUENCE 1073 AA; 117870 MW; A9B02AF34675026B CRC64; MPKRTDIKSI LILGAGPIVI GQACEFDYSG AQACKALREE GYRVILVNSN PATIMTDPEM ADATYIEPIH WEVVRKIIEK ERPDAVLPTM GGQTALNCAL ELERQGVLEE FGVTMIGATA DAIDKAEDRR RFDVAMKKIG LETARSGIAH TMEEALAVAA DVGFPCIIRP 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 ANATVTAIEM 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 //