ID A0A0M3AJB2_9SPHN Unreviewed; 1115 AA. AC A0A0M3AJB2; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 07-APR-2021, entry version 29. 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 ORFNames=YP76_21725 {ECO:0000313|EMBL:KKW90068.1}; OS Sphingobium chungbukense. OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Sphingobium. OX NCBI_TaxID=56193 {ECO:0000313|EMBL:KKW90068.1, ECO:0000313|Proteomes:UP000033874}; RN [1] {ECO:0000313|EMBL:KKW90068.1, ECO:0000313|Proteomes:UP000033874} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DJ77 {ECO:0000313|EMBL:KKW90068.1, RC ECO:0000313|Proteomes:UP000033874}; RA Kim Y.-C., Chae J.-C.; RT "Genome sequence of aromatic hydrocarbons-degrading Sphingobium RT chungbukense DJ77."; RL Submitted (APR-2015) 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: Lacks conserved residue(s) required for the propagation of CC feature annotation. {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:KKW90068.1}. 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; LBIC01000012; KKW90068.1; -; Genomic_DNA. DR RefSeq; WP_046765689.1; NZ_LBIC01000012.1. DR EnsemblBacteria; KKW90068; KKW90068; YP76_21725. DR PATRIC; fig|56193.3.peg.4569; -. DR UniPathway; UPA00068; UER00171. DR UniPathway; UPA00070; UER00115. DR Proteomes; UP000033874; 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; 1. 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}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01210}; KW 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}; 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 714..909 FT /note="ATP-grasp" FT /evidence="ECO:0000259|PROSITE:PS50975" FT DOMAIN 976..1115 FT /note="MGS-like" FT /evidence="ECO:0000259|PROSITE:PS51855" FT REGION 1..402 FT /note="Carboxyphosphate synthetic domain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01210" FT REGION 976..1115 FT /note="Allosteric domain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01210" SQ SEQUENCE 1115 AA; 119967 MW; C8115F2D77F99920 CRC64; MPKRTDISSI LIIGAGPIII GQACEFDYSG TQAVKALKEE GYRIILVNSN PATIMTDPEF ADATYVEPIT PEIVAKIIEK ERPDAVLPTM GGQTALNTAL ALFNDGTLEK YGVKMIGADA QAIDKAEDRL KFRDAMDKIG LESARSRIAH TMEEAMEALE FTGLPSIIRP SFTLGGTGGG VAYNKEEFKR IVSEGLDASP TTEVLIEESL LGWKEYEMEV VRDRNDNAII ICSIENVDPM GVHTGDSITV APALTLTDKE YQIMRNASIA VLREIGVETG GSNVQFAVNP KDGRLIVIEM NPRVSRSSAL ASKATGFPIA KVAAKLAVGY TLDEIENDIT GATPASFEPT IDYVVTKIPR FAFEKFKGSE PLLGTAMKSV GEVMAIGRNI HESMQKALRG LETGLCGFNE VDHLVGAPKD DIIAALAQPT PDRLLVAAQA LREGLTVAEI HTIAKFDPWF LERIKEIVDA EAEILANGLP QDADGMRRLK SMGFADKRLA YLALKSANLR GMERGIARGS GLIHDAIKAM TGGVTEDEVR ALRHKLGVRP VFKRIDTCAA EFEARTPYMY STYEAPIFGE AENEAQPSDR KKVVILGGGP NRIGQGIEFD YCCVHACFAL SEAGYETIMV NCNPETVSTD YDTSDRLYFE PLTAEDVLEI LSVEMSNGTL AGVIVQFGGQ TPLKLAQALE DAGIPILGTS PDAIDLAEDR ERFAALIDKL KLKQPANGIA RSREEAIAVA NRIGYPVLMR PSYVLGGRAM EIVDGQAQLE EYIATAVQVS GDSPVLIDQY LRDAVEVDVD ALCDGDDVVV AGVLQHIEEA GVHSGDSACS LPPYSLSDDI IAEIERQADV LARALSVRGL MNIQFAVKDG PEGQTVYLIE VNPRASRTVP FVAKAIGTPI AKIASRVMAG EKLKNLPKID RNAISHIAVK EAVFPFARFP GVDPVLSPEM KSTGEVMGID SDFATAFAKS QLGGGTVLPK SGTVFVSVKD SDKPVILPAV RKMADLGFTI IATGGTARYL EEQGIAVHPV NKVAEGRPHI VDKIIDGDVD LIFNTTEGWQ SLKDSKEIRT SALRAKVASF TTAAASVAAA DAIEALRGHA LEVRSLQSYY PVSQA //