ID   A0A9X1VAN6_9BACL        Unreviewed;      1064 AA.
AC   A0A9X1VAN6;
DT   08-NOV-2023, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2023, sequence version 1.
DT   24-JAN-2024, 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   ECO:0000313|EMBL:MCI0184187.1};
GN   ORFNames=MM817_02482 {ECO:0000313|EMBL:MCI0184187.1};
OS   Sulfoacidibacillus ferrooxidans.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC   Sulfoacidibacillus.
OX   NCBI_TaxID=2005001 {ECO:0000313|EMBL:MCI0184187.1, ECO:0000313|Proteomes:UP001139263};
RN   [1] {ECO:0000313|EMBL:MCI0184187.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=S0AB {ECO:0000313|EMBL:MCI0184187.1};
RA   Vergara E., Pakostova E., Johnson D.B., Holmes D.S.;
RT   "Draft Genome Sequence of Firmicute Strain S0AB, a Heterotrophic
RT   Iron/Sulfur-Oxidizing Extreme Acidophile.";
RL   Submitted (MAR-2022) 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}.
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:MCI0184187.1}.
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DR   EMBL; JALBUF010000009; MCI0184187.1; -; Genomic_DNA.
DR   Proteomes; UP001139263; Unassembled WGS sequence.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   CDD; cd01424; MGS_CPS_II; 1.
DR   Gene3D; 3.40.50.20; -; 2.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
DR   Gene3D; 1.10.1030.10; Carbamoyl-phosphate synthetase, large subunit oligomerisation domain; 1.
DR   Gene3D; 3.40.50.1380; Methylglyoxal synthase-like domain; 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; IPR013815; ATP_grasp_subdomain_1.
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   NCBIfam; TIGR01369; CPSaseII_lrg; 1.
DR   PANTHER; PTHR11405:SF5; CAD PROTEIN; 1.
DR   PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
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; SM01209; GARS_A; 1.
DR   SMART; SM00851; MGS; 1.
DR   SUPFAM; SSF48108; Carbamoyl phosphate synthetase, large subunit connection domain; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 2.
DR   SUPFAM; SSF52335; Methylglyoxal synthase-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 2.
DR   PROSITE; PS50975; ATP_GRASP; 2.
DR   PROSITE; PS00866; CPSASE_1; 1.
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..327
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          671..861
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          930..1064
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          547..929
FT                   /note="Carbamoyl phosphate synthetic domain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT   REGION          930..1064
FT                   /note="Allosteric domain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT   BINDING         284
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT   BINDING         298
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT   BINDING         298
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT   BINDING         300
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT   BINDING         820
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT   BINDING         832
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT   BINDING         832
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT   BINDING         834
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
SQ   SEQUENCE   1064 AA;  117377 MW;  B1799B6DA9E9F859 CRC64;
     MSKRRDIKSI LVIGSGPIVI GQAAEFDYAG TQACHALREE GIRVVLVNSN PATIMTDPET
     ADRVYIEPLT KEFLAQIIRQ ERPDGILATL GGQTALNLAV ELSEDGVLER EGVQLLGTSL
     SSIRMAEDRE EFRELMNRLG EPIPESKIVT SLQEAELFLK EIGLPVIIRP AYTLGGTGGG
     IATTNEEFVK IAALGLSLSP IGQVLIEQSI AGYKEIEYEV MRDGADNCIV ICNMENFDPV
     GVHTGDSIVV APSQTLSDQD YQMLRSASLR IIRALGIEGG CNVQLALDPV SKQYYVIEVN
     PRVSRSSALA SKATGYPIAK VAAKVALGYT LDEILNPITG QTYACFEPAL DYVVTKIPRW
     PFDKFASAER NLGTQMKATG EVMALGRTME ESLMKAVRSL EIGLYSLELP ALKNLSDEEL
     WQRAIHPDDE RIFILYELLR RNVGIEQLYD ATKVDSFFLR KLQNILRLAN DLEAHGLTDQ
     LLYLAKRSGF VDAYIAKLTG LTLQEVEQRR LSKHLVPVYK MVDTCAAEFE AQTPYYYSTY
     ETEDEVESSD AKKVVVLGSG PIRIGQGIEF DYCSVHASLA LRKEGYESIV INNNPETVST
     DFNMSSRLYF EPLYVEDVMN VIARERPEGV IVQFGGQTAI HLAKPLADLG IKILGTHVED
     IDRAENREKF DDLLSKLDIL RPAGRAVTKL SQAMDAAKEL QFPVLVRPSY VLGGRAMQIV
     YTDVELSQYM QEAALVSPEH PVLIDRYLLG VEVEVDAISD GETVIIPGVM EHIERAGVHS
     GDSIAVYPAQ SLTHEWKEKI ISDTVRIARE LHVVGLLNIQ FVIHDHNVYV LEVNPRSSRT
     VPFLSKVTGI PMVDLAMHAV LGQKLADLGW QTGLVPEKQL ISVKVPVFSF AKLREVDVTL
     GPEMKSTGEV MGTDETLGKA LYKGMLAAGF RFPAHGAIIA TIADKDKEEA LPILRGLSAL
     GFHLYATEGT ASFLMRYGIA STLVNKISLE GPSLLDMIRK GQAMMVINTL TRGKKPERDG
     FRIRREAVEH AIPCLTSLDT AKAVFDVLSS LHFSTRPLQA VEER
//