ID A0A350M1G9_9BACT Unreviewed; 1069 AA. AC A0A350M1G9; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 08-MAY-2019, entry version 6. 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=DCX16_06780 {ECO:0000313|EMBL:HAW50636.1}; OS bacterium. OC Bacteria. OX NCBI_TaxID=1869227 {ECO:0000313|EMBL:HAW50636.1}; RN [1] {ECO:0000313|EMBL:HAW50636.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=UBA9088 {ECO:0000313|EMBL:HAW50636.1}; RX PubMed=30148503; DOI=10.1038/nbt.4229; RA Parks D.H., Chuvochina M., Waite D.W., Rinke C., Skarshewski A., RA Chaumeil P.A., Hugenholtz P.; RT "A standardized bacterial taxonomy based on genome phylogeny RT substantially revises the tree of life."; RL Nat. Biotechnol. 36:996-1004(2018). 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; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01210, ECO:0000256|SAAS:SAAS01124510}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|SAAS:SAAS00981842}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|SAAS:SAAS00611658}; CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; CC carbamoyl phosphate from bicarbonate: step 1/1. CC {ECO:0000256|HAMAP-Rule:MF_01210, ECO:0000256|SAAS:SAAS00981844}. CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo CC pathway; (S)-dihydroorotate from bicarbonate: step 1/3. CC {ECO:0000256|HAMAP-Rule:MF_01210, ECO:0000256|SAAS:SAAS01000080}. 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. CC {ECO:0000256|HAMAP-Rule:MF_01210, ECO:0000256|SAAS:SAAS00570548}. CC -!- SIMILARITY: Belongs to the CarB family. {ECO:0000256|HAMAP- CC Rule:MF_01210, ECO:0000256|SAAS:SAAS00570556}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01210}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:HAW50636.1}. 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; DNCM01000191; HAW50636.1; -; Genomic_DNA. DR UniPathway; UPA00068; UER00171. DR UniPathway; UPA00070; UER00115. 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_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. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01210, KW ECO:0000256|SAAS:SAAS00981831}; KW Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01210, KW ECO:0000256|SAAS:SAAS00981841}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01210, ECO:0000256|PROSITE- KW ProRule:PRU00409, ECO:0000256|SAAS:SAAS00710217}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_01210, KW ECO:0000256|SAAS:SAAS00710245}; KW Magnesium {ECO:0000256|SAAS:SAAS00981805}; KW Manganese {ECO:0000256|SAAS:SAAS00459951}; KW Metal-binding {ECO:0000256|SAAS:SAAS00086100}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01210, KW ECO:0000256|PROSITE-ProRule:PRU00409, ECO:0000256|SAAS:SAAS00710285}; KW Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01210, KW ECO:0000256|SAAS:SAAS01000143}; KW Repeat {ECO:0000256|HAMAP-Rule:MF_01210, KW ECO:0000256|SAAS:SAAS00981845}. FT DOMAIN 133 327 ATP-grasp. {ECO:0000259|PROSITE:PS50975}. FT DOMAIN 670 861 ATP-grasp. {ECO:0000259|PROSITE:PS50975}. FT REGION 1 400 Carboxyphosphate synthetic domain. FT {ECO:0000256|HAMAP-Rule:MF_01210}. FT REGION 928 1069 Allosteric domain. {ECO:0000256|HAMAP- FT Rule:MF_01210}. SQ SEQUENCE 1069 AA; 119348 MW; 6675D1D9E8E18D6A CRC64; MSKRKDLKKI LIIGSGPIVI GQACEFDYSG TQACKALREE GYEVVLVNSN PATIMTDPGM ADKTYIEPLT VESLEKIIER ERPDGLLSNL GGQTALNLAF SLHKSGVLEK YGVEIIGVKS DTIERGENRV VFKETMAKLG IHVPRSEPCH SVEEAERIAE KLGYPVILRP AYTLGGTGGG CVYNVEELRV IAARGLSASL IHQVLVEESV LGWEELELEV VRDQKGQMIT VCFIENVDPM GVHTGDSFCV APMLTIPKAL QMRMQELSYK IVEAIDVIGG TNIQFAHNPK DDRLVVIEIN PRTSRSSALA SKATGFPIAR ISAKLAVGVT LDEIPYWRKK TLEKYEPWGD YVIVKFARFA FEKFPQARDI LGTQMKAVGE VMSIGKTFKE AFQKSIRSLE IKRYGLCVEK FKALSLSQLK EKLGVPSSER IFLMYEALRR GISVEELYEM TSINMWFINE IKELVEFEEE LLKYTWDNLP DNELIKAKEW GFSDKYLASL FKVDERGVRK KRVSLGKYVR FDAVSVSGVE NTSYYYSTYI GEDKVGISPN RKILILGGGP NRIGQGIEFD YTCVHAAFAL ADEGYESVMI NCNPETVSTD YDTASKLYFE PLTVEDVLNI YEKERPEGVI VQFGGQTPLN IAQELKDNGV NILGTSPESI GFAEDRERFR QKMIELNILQ PDGGTARSLD EAIGIANRIG YPLMVRPSFV LGGRGMEIVY DEEMLRKYAE EAIQVSPEYP MLIDKFLEEA VEAEVDAICD GEETFIVAVM EHIELAGVHS GDSACVIPPR AIKEEHLKTI EEYTVRIARE LKVMGLINIQ YAICEDKVYI LEANPRASRT VPLVSKVMGI PVARIATYLM LGKKLQDFPE LKKKKFSHIG VKETVFSFGM FPDVDPILGP EMKATGEVMG IAETFGLSFY KAQEAAGSKL PLEGNVLLTV ADKDKLALLP VAKRIHKLGF NIYATKGTSK YLKENDIPNT VIKTIHEGRP NIADAIKNRN IHLIINTPIG RTSKYDDSYI RMMAVQNKIP YVTSISAAWA SVEGIEAAKR CKILPKSIQE YHKECGFND //