ID   A0A4D6XVC8_9GAMM        Unreviewed;      1079 AA.
AC   A0A4D6XVC8;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   25-MAY-2022, entry version 10.
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, ECO:0000313|Proteomes:UP000298660};
RN   [1] {ECO:0000313|EMBL:QCI17551.1, ECO:0000313|Proteomes:UP000298660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ala {ECO:0000313|EMBL:QCI17551.1,
RC   ECO:0000313|Proteomes:UP000298660};
RA   Chong R.A.;
RL   Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:QCI17551.1, ECO:0000313|Proteomes:UP000298660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ala {ECO:0000313|EMBL:QCI17551.1,
RC   ECO:0000313|Proteomes:UP000298660};
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;
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|HAMAP-Rule:MF_01210};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01210};
CC       Note=Binds 4 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01210};
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}.
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DR   EMBL; CP034891; QCI17551.1; -; Genomic_DNA.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000298660; Chromosome.
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.
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   Magnesium {ECO:0000256|ARBA:ARBA00022842};
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          679..870
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          937..1079
FT                   /note="MGS-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51855"
FT   REGION          1..403
FT                   /note="Carboxyphosphate synthetic domain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT   REGION          404..553
FT                   /note="Oligomerization domain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT   REGION          554..936
FT                   /note="Carbamoyl phosphate synthetic domain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT   REGION          937..1079
FT                   /note="Allosteric domain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT   METAL           285
FT                   /note="Magnesium 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT   METAL           299
FT                   /note="Magnesium 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT   METAL           299
FT                   /note="Magnesium 2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT   METAL           301
FT                   /note="Magnesium 2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT   METAL           829
FT                   /note="Magnesium 3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT   METAL           841
FT                   /note="Magnesium 3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT   METAL           841
FT                   /note="Magnesium 4"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT   METAL           843
FT                   /note="Magnesium 4"
FT                   /evidence="ECO:0000256|HAMAP-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
//