ID A0A2M8ND49_9CHLR Unreviewed; 1062 AA. AC A0A2M8ND49; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 02-DEC-2020, entry version 9. 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:PJF23233.1}; GN ORFNames=CUN56_01980 {ECO:0000313|EMBL:PJF23233.1}; OS Candidatus Thermofonsia Clade 2 bacterium. OC Bacteria; Chloroflexi; Candidatus Thermofonsia; OC Candidatus Thermofonsia Clade 2. OX NCBI_TaxID=2364211 {ECO:0000313|EMBL:PJF23233.1, ECO:0000313|Proteomes:UP000229704}; RN [1] {ECO:0000313|EMBL:PJF23233.1, ECO:0000313|Proteomes:UP000229704} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JP1_20 {ECO:0000313|EMBL:PJF23233.1}; RA Ward L.M., Hemp J., Shih P.M., Mcglynn S.E., Fischer W.; RT "Evolution of Phototrophy in the Chloroflexi Phylum Driven by Horizontal RT Gene Transfer."; RL Submitted (NOV-2017) 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:PJF23233.1}. 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; PGTF01000024; PJF23233.1; -; Genomic_DNA. DR UniPathway; UPA00068; UER00171. DR UniPathway; UPA00070; UER00115. DR Proteomes; UP000229704; 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:PJF23233.1}; 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 668..858 FT /note="ATP-grasp" FT /evidence="ECO:0000259|PROSITE:PS50975" FT DOMAIN 925..1062 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 925..1062 FT /note="Allosteric domain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01210" SQ SEQUENCE 1062 AA; 115535 MW; D34F915B01E060F5 CRC64; MPKRTDIHTI MIIGSGPIVI GQASEFDYSG VQACKALRRL GYRIVLVNSN PATIMTDPEF ADATYIEPLT PEICERIIEQ EKPDALLPTV GGQTALNLAL ALEEQGILKK HNVELIGASM NSILLAEDRQ RFKDAMTEIN LKSPPSEVVT SVQAAVDAAE KMGYPVLVRP SFTLGGSGGG VAYDEVQLRE IARNGIKQSP VGQILVDYSL LGWKEYELEI MRDSAGNFVV VCAIENLDPM GVHTGDSITV APAQTLTDKE LQRLRDMARQ IFDKVGLATG GANVQYAINP DDGEVYVIEM NPRVSRSSAL ASKATGFPIA KIAALVAVGF TLDEIPNDIT RVTPASFEPS LDYVVVKIPR WDFEKFTTAD QVLGPQMKAV GEVMAIGRTF PEALQKAIRS LDIGVMGFGS SLEDVPAHAL KVPTARRLFQ VAANLFKGVS VEEVVENTRF DPWFVQQMAD IMAIHRRMIG KTRLSREDYL LLKQYGFADA YIAQLLGVDE FTVREQRKAL GVVTNYYRVD TCAAEFEAHT PYLYSTYEEG CEANPSTQRK VMILGGGPNR IGQGIEFDYC CVHACFALKQ LGYETIMVNC NPETVSTDYD TADRLYFEPL TAEDVLNIID KEKPDGVLVQ FGGQTPLNIA HALQQAGAPI WGTSVETIDL AEDRQRFNAL MAELDIMQPA GATVISREEA IHAAAAIGYP VLVRPSYVLG GRGMAIVFDE AQLIAWIDQH IQWTGHPVLI DQFLDDAFEV DVDALCDGER VTIGGVMQHI EEAGVHSGDS ACVLPPYKIS AYHLEIIREH THRIGLAMGV KGLFNIQFAI KDDEVYVLEV NPRASRTVPF VSKAIGVPLA SYAAQIAAGM TLDALGFTQE VPVDGFFVKE AVLPFQKFPG VDARLGPEMR STGEVMGHAS SFGHAFVKAQ IAARMTLPTS GTVFISVNDF DKGAVARIAR DLYNMGFKLM ATHGTARWLE MIGLPVEPVN KVAQGSPHVV DRMLAGDIDL VINTPLGGQA HEAGALIRGT AHLLGIPIIT TMSAAAASVQ GIKALKGKPL KVRSLQAHHK MT //