ID   A0A1I6YL40_9GAMM        Unreviewed;      1081 AA.
AC   A0A1I6YL40;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   11-DEC-2019, 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=SAMN04487956_10620 {ECO:0000313|EMBL:SFT51196.1};
OS   Halomonas saccharevitans.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=416872 {ECO:0000313|EMBL:SFT51196.1, ECO:0000313|Proteomes:UP000199594};
RN   [1] {ECO:0000313|EMBL:SFT51196.1, ECO:0000313|Proteomes:UP000199594}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.6493 {ECO:0000313|EMBL:SFT51196.1,
RC   ECO:0000313|Proteomes:UP000199594};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; carbamoyl
CC       phosphate from bicarbonate: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01210,
CC       ECO:0000256|SAAS:SAAS00981844}.
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, 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 the
CC       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 of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01210}.
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DR   EMBL; FPAQ01000006; SFT51196.1; -; Genomic_DNA.
DR   BioCyc; GCF_900116405:BM388_RS04280-MONOMER; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000199594; 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: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_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; 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; 1.
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, 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, ECO:0000256|PROSITE-
KW   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, ECO:0000256|SAAS:SAAS00981845}.
FT   DOMAIN          133..328
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          683..874
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   REGION          1..403
FT                   /note="Carboxyphosphate synthetic domain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT   REGION          941..1081
FT                   /note="Allosteric domain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
SQ   SEQUENCE   1081 AA;  118392 MW;  22A020A2B5B38DD6 CRC64;
     MPKRTDIKSI LIIGAGPIVI GQACEFDYSG AQACKALREE GYRVILVNSN PATIMTDPAM
     ADATYIEPIT WQTVEKIIEA ERPDVILPTM GGQTALNCAL ELDKHGVLAK YGVEMIGANA
     DAINKAEDRD LFDKAMKNIG LECPKAKVAH SMQEAWEIQA ELGFPTIIRP SYTMGGSGGG
     VAYNKEEFDE ICQRGFELSN NHELLIDESL LGWKEYEMEV VRDKHDNCII VCAIENFDPM
     GVHTGDSITV APAQTLTDKE YQIMRDASLA VLREIGVETG GSNVQFGMDP QTGRMVVIEM
     NPRVSRSSAL ASKATGFPIA KIAAKLAVGY TLDELQNDIT GGRTPASFEP AIDYVVTKIP
     RFTFEKFPQA NDRLTTQMKS VGEVMAIGRT FQESLHKALR GMETGNDGLD PVFPEQKPGA
     FTAEAMAHIK GELQAAGAER IFFVADAMRA GMSLEEVFAL TNIDRWFLVQ IEELIRIEAE
     VATRPLSEFT PRELYRLKRK GFSDARLARL LGVAEKEFRR TRQRAGIRPV YKRVDTCAAE
     FASDTAYMYS TYEEECEAEV SDKKKIMVLG GGPNRIGQGI EFDYCCVHAA FAMHDDGYET
     IMVNCNPETV STDYDTSDRL YFEPVTLEDV LEIADKEQPV GVIVQFGGQT PLKLARELEA
     AGVPIIGTTP DAIDRAEDRE RFQQMIDKLG LKQPPNATAR SFDEAFAKAE AIGYPLVVRP
     SYVLGGRAME IVYDASELEN YMTHAVKVSN DSPVLLDHFL NAAIEIDIDA VSDGSQVVIG
     GIMQHIEQAG VHSGDSACAL PPYSLPAEVQ DAMREQVKQM AVELGVKGLM NVQLAWQDDE
     IYVIEVNPRA SRTVPFVSKC IGTSLAQVAA RCMAGQTLTE QGFEAEIVPH FYSVKEAVFP
     FNKFPGVDPI LSPEMKSTGE VMGSGDTFAE AFYKAQLGAG EAIPRLEGKR KAFLSVRDPD
     KAGIIEVARS LVTLGFTLCA TRGTAKALEG TELSVQIVNK VYEGRPHIVD LLKNDEVAYI
     VNTTEGRQAI NDSSVIRRTA LARKVPYATT LAGANAVCMA LEYGNAITVR RLQELHAGAT
     Q
//