ID I2SLM0_ECOLX Unreviewed; 1073 AA. AC I2SLM0; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 02-DEC-2020, entry version 49. 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:EIH21691.1}; GN ORFNames=EC12264_0032 {ECO:0000313|EMBL:EIH21691.1}; OS Escherichia coli 1.2264. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=869675 {ECO:0000313|EMBL:EIH21691.1, ECO:0000313|Proteomes:UP000005354}; RN [1] {ECO:0000313|EMBL:EIH21691.1, ECO:0000313|Proteomes:UP000005354} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1.2264 {ECO:0000313|EMBL:EIH21691.1, RC ECO:0000313|Proteomes:UP000005354}; 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: 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 Evidence={ECO:0000256|ARBA:ARBA00001777, ECO:0000256|HAMAP- CC Rule:MF_01210}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|ARBA:ARBA00001936}; CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl CC phosphate from bicarbonate: step 1/1. {ECO:0000256|HAMAP- CC Rule:MF_01210}. CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; CC (S)-dihydroorotate from bicarbonate: step 1/3. CC {ECO:0000256|ARBA:ARBA00004812, ECO:0000256|HAMAP-Rule:MF_01210}. 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. CC {ECO:0000256|HAMAP-Rule:MF_01210}. CC -!- SIMILARITY: Belongs to the CarB family. {ECO:0000256|ARBA:ARBA00009799, CC ECO:0000256|HAMAP-Rule:MF_01210}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:EIH21691.1}. 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 RefSeq; WP_001126376.1; NZ_AEZO02000031.1. DR SMR; I2SLM0; -. DR EnsemblBacteria; EIH21691; EIH21691; EC12264_0032. DR GeneID; 48132682; -. DR UniPathway; UPA00068; UER00171. DR UniPathway; UPA00070; UER00115. DR Proteomes; UP000005354; Unassembled WGS sequence. 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. DR PROSITE; PS51855; MGS; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01210}; KW Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01210}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_01210, ECO:0000256|PROSITE-ProRule:PRU00409}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01210, KW ECO:0000313|EMBL:EIH21691.1}; Manganese {ECO:0000256|ARBA:ARBA00023211}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_01210, ECO:0000256|PROSITE-ProRule:PRU00409}; KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975, ECO:0000256|HAMAP- KW Rule:MF_01210}; KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_01210}. FT DOMAIN 133..328 FT /note="ATP-grasp" FT /evidence="ECO:0000259|PROSITE:PS50975" FT DOMAIN 679..870 FT /note="ATP-grasp" FT /evidence="ECO:0000259|PROSITE:PS50975" FT DOMAIN 937..1073 FT /note="MGS-like" FT /evidence="ECO:0000259|PROSITE:PS51855" FT REGION 1..403 FT /note="Carboxyphosphate synthetic domain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01210" FT REGION 404..553 FT /note="Oligomerization domain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01210" FT REGION 554..936 FT /note="Carbamoyl phosphate synthetic domain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01210" FT REGION 937..1073 FT /note="Allosteric domain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01210" 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 //