ID A0A0F2NIS3_9FIRM Unreviewed; 1076 AA. AC A0A0F2NIS3; DT 24-JUN-2015, integrated into UniProtKB/TrEMBL. DT 24-JUN-2015, sequence version 1. DT 02-DEC-2020, 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=VR68_05885 {ECO:0000313|EMBL:KJS01020.1}; OS Peptococcaceae bacterium BRH_c4a. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae. OX NCBI_TaxID=1629716 {ECO:0000313|EMBL:KJS01020.1, ECO:0000313|Proteomes:UP000033439}; RN [1] {ECO:0000313|EMBL:KJS01020.1, ECO:0000313|Proteomes:UP000033439} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BRH_c4a {ECO:0000313|EMBL:KJS01020.1}; RA Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F., RA Leupin O.X., Schwyn B., Bernier-Latmani R.; RT "Microbial metabolic network in the subsurface."; RL Submitted (MAR-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. {ECO:0000256|HAMAP- CC 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|ARBA:ARBA00011275, 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:KJS01020.1}. 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; LADN01000039; KJS01020.1; -; Genomic_DNA. DR PATRIC; fig|1629716.3.peg.156; -. DR UniPathway; UPA00068; UER00171. DR UniPathway; UPA00070; UER00115. DR Proteomes; UP000033439; 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:InterPro. 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 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; 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 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 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..327 FT /note="ATP-grasp" FT /evidence="ECO:0000259|PROSITE:PS50975" FT DOMAIN 673..863 FT /note="ATP-grasp" FT /evidence="ECO:0000259|PROSITE:PS50975" FT DOMAIN 932..1076 FT /note="MGS-like" FT /evidence="ECO:0000259|PROSITE:PS51855" FT REGION 1..401 FT /note="Carboxyphosphate synthetic domain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01210" FT REGION 549..931 FT /note="Carbamoyl phosphate synthetic domain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01210" FT REGION 932..1076 FT /note="Allosteric domain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01210" SQ SEQUENCE 1076 AA; 116730 MW; 93D315D8934A959D CRC64; MPRHKDIKKV LVIGSGPIVI GQAAEFDYAG TQACKALSEE GAEVALINSN PATIMTDPGI AHQVYIEPLT WQSVAGVIKR ERPDGLLPTL GGQTGLNLAV ELADRGVLKK YGVKLLGTSL EAIKKAEDRQ LFKETMLAIG EPVPDSIIAL NLDHAREFVS RVGFPVIVRP AYTLGGTGGG IVGNDAELAD IVTRGLKLSM IGQVLLERSV AGWKEIEYEV MRDGAGNCIT ICNMENIDPI GVHTGDSIVV APSQTLADRE YQMLRTASLK IIRALKVEGG CNVQFALDPY SYNYYVIEVN PRVSRSSALA SKATGYPIAK MAAKIAVGLN LDEIVNPVTG KTTACFEPAL DYVVVKIPRW PFDKFGSADR TLGTQMKATG EVMAIDRSFE GALMKAVRSL EIGVDSLKLK GSASWSEMEL EERLARPNDE RLFVMAEAFR RFWAMREVSQ LTRIDYFFLE KIKNIVVTEG ELKNRRGPVD LETLARAKTL GISDSQVARL TRTTVGEVRA LRKEYGLTPS YKVVDTCSAE FESATPYYYS TYDSQDEVEV SGRKKALVLG SGPIRIGQGI EFDYCSVHSV WGLQAENVES VIVNNNPETV STDFDTSDKL YFEPLTLEDV LNIIDKEKPD GVIVQFGGQT AINLAGELDK QGVGILGTPV ECIDAAEDRE KFGDLLRSLN IPQTEGGTAF NVRGALEIAD KVGYPVLVRP SYVLGGRAME IVHSDQELLK YMETAVQITP KHPVLVDKYV LGKEVEVDAI GDGKDIFIPG IMEHVERAGV HSGDSIAVYP PQTLSDRETA GIVEYTLRIG RALKICGLMN IQYVVGKNGI FVLEVNPRAS RTVPVLSKVT GIPMVQVATR AMLGRSLESM GYGSGLGPTP NLVTVKAPVF SFEKLGLVET SLGPEMKSTG EVMGIDRTFP LALYKAMVSS GLKIVTGGDL LVSLSDRDKE EALPIIRCYV DMGFKLYATG GTASALAGAG LAVEDAANAE TMIRSGRISL VINTPTRGKI PGRPGFMMRR AASEYRVPCL TSLDTAQALA VMLQSIGRGE EPEPVNMRDF TSFTSFTSLA YRRAAI //