ID A0A4D6XVC8_9GAMM Unreviewed; 1079 AA. AC A0A4D6XVC8; DT 31-JUL-2019, integrated into UniProtKB/TrEMBL. DT 31-JUL-2019, sequence version 1. DT 18-SEP-2019, entry version 2. 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=D9V61_00720 {ECO:0000313|EMBL:QCI17551.1}; OS Buchnera aphidicola (Acyrthosiphon lactucae). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Erwiniaceae; Buchnera. OX NCBI_TaxID=1241832 {ECO:0000313|EMBL:QCI17551.1}; RN [1] {ECO:0000313|EMBL:QCI17551.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Ala {ECO:0000313|EMBL:QCI17551.1}; RA Chong R.A.; RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:QCI17551.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Ala {ECO:0000313|EMBL:QCI17551.1}; RA Moran N.A.; RT "Genome evolution of the obligate endosymbiont Buchnera aphidicola."; RL Submitted (MAY-2019) 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; 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 --------------------------------------------------------------------------- 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; CP034891; QCI17551.1; -; Genomic_DNA. DR UniPathway; UPA00068; UER00171. DR UniPathway; UPA00070; UER00115. 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, ECO:0000313|EMBL:QCI17551.1}; 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 133 328 ATP-grasp. {ECO:0000259|PROSITE:PS50975}. FT DOMAIN 679 870 ATP-grasp. {ECO:0000259|PROSITE:PS50975}. FT REGION 1 403 Carboxyphosphate synthetic domain. FT {ECO:0000256|HAMAP-Rule:MF_01210}. FT REGION 404 553 Oligomerization domain. FT {ECO:0000256|HAMAP-Rule:MF_01210}. FT REGION 554 936 Carbamoyl phosphate synthetic domain. FT {ECO:0000256|HAMAP-Rule:MF_01210}. FT REGION 937 1079 Allosteric domain. {ECO:0000256|HAMAP- FT Rule:MF_01210}. SQ SEQUENCE 1079 AA; 120621 MW; AE9B5B2D38E71B29 CRC64; MPKSTDIKSI LILGAGPIVI GQACEFDYSG AQACKALKEE GYKIILVNSN PATIMTDPCM ADSTYIEPIH WKIVEKIIQK EKPDALLPTM GGQTALNCAL KLDQKGVLKT HGVKIIGATV NAIKKAENRK LFEHSMKKLN LETAKCGIAH NIQEAFLVLN DVGFPCIIRP SFTMGGHGGG IAYNHEEFEK ICERGLKLSP NTELLIDESL IGWKEYEMEV VRDRNDNCII VCSIENLDPM GIHTGDSITV APAQTLTDKE YQVMRNASMA ILREIGVETG GSNVQFAINP KNGRMIVIEM NPRVSRSSAL ASKATGFPIA KIAAKLAIGY TLDELTNDIT GMNTTASFEP SIDYIVTKIP RFNFEKFPGC DDRLTTQMKS VGEVMAIGRT FQESIQKAIR GLELGVSGFD SKISHLDPEY LIKIRRELKD AGSERIWYIG DAFRSGMSVN DVFNLTSIDP WFLVQIEEII QLENKIIKNG FLGLKYDFFY LIKRKGFSDQ RIAILTQKNE SQIRELRYKL NLHPVYKRID TCSAEFSTET AYMYSTWEDE CESYPNKNNK KIIILGGGPN RIGQGIEFDY CCVHAAQALR EDGFEAIMIN CNPETVSTDY DISDRLYFEP ITLENVLEIV RIEKPRGIII QYGGQTPLKL AREFEKEGVP IIGTSPDSID KAEDRDRFQK IVTKLKLQQP LNATVLTLDE AYKQAEIIGY PIMVRPSYVL GGRAMEIVYE QYGLKNYFKT VLKENNTTPI LLDQYLNYAT EVDVDAVCDG KTVLIGGIME HIEQAGVHSG DSACSLPVYT LTNKVQNEIR KQVTKLAFEL SVKGLMNVQF AIKRNIIYII EVNPRAARTV PFISKATGLA LAKISARVMY GKTLLEQGFI KEIIPPYFSV KEAVLPFDKF QGVDPILGPE MRSTGEVMGM GKNFSEAFSK AMLGAHTNMK KSGRILLSVR DDDKNNIVNL AVKLKKIGFK IDATKGTSIA LRKSGISSRL VNKVHEGRPH IQDRLKNGEY SYIVNTTSSH QGIKDSKLIC RSALQYKVHY DTTVNGAFAT VMALNENPIK NIKSLQEMHK KIKLFYKKK //