ID   A0A7W2CZU3_9ACTN        Unreviewed;      1102 AA.
AC   A0A7W2CZU3;
DT   02-JUN-2021, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 1.
DT   13-SEP-2023, 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   ECO:0000313|EMBL:MBA4862116.1};
GN   ORFNames=H1V43_12095 {ECO:0000313|EMBL:MBA4862116.1};
OS   Streptomyces himalayensis subsp. aureolus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces himalayensis.
OX   NCBI_TaxID=2758039 {ECO:0000313|EMBL:MBA4862116.1, ECO:0000313|Proteomes:UP000586976};
RN   [1] {ECO:0000313|EMBL:MBA4862116.1, ECO:0000313|Proteomes:UP000586976}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PSKA54 {ECO:0000313|EMBL:MBA4862116.1,
RC   ECO:0000313|Proteomes:UP000586976};
RA   Mandal S., Maiti P.K.;
RT   "Streptomyces isolated from Indian soil.";
RL   Submitted (JUL-2020) 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:MBA4862116.1}.
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DR   EMBL; JACEQY010000010; MBA4862116.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A7W2CZU3; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000586976; 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; 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_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; 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; 2.
DR   PROSITE; PS00867; CPSASE_2; 2.
DR   PROSITE; PS51855; MGS; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_01210};
KW   Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571, ECO:0000256|HAMAP-
KW   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..334
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          682..873
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          955..1100
FT                   /note="MGS-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51855"
FT   REGION          1..408
FT                   /note="Carboxyphosphate synthetic domain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT   REGION          955..1102
FT                   /note="Allosteric domain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT   BINDING         291
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT   BINDING         305
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT   BINDING         305
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT   BINDING         307
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
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         844
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT   BINDING         844
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
FT   BINDING         846
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01210"
SQ   SEQUENCE   1102 AA;  117729 MW;  C7229F022C569BB3 CRC64;
     MPKRTDIQSV LVIGSGPIVI GQAAEFDYSG TQACRVLKAE GLRVILVNSN PATIMTDPEI
     ADATYVEPIT PEFVEKIIAK ERPDALLPTL GGQTALNTAI SLHEAGTLEK YGVELIGANV
     EAINKGEDRD LFKEVVEAVR AKIGHGESAR SVICHSMDDV LKGVETLGGY PVVVRPSFTM
     GGAGSGFAHD EEELRRIAGQ GLTLSPTTEV LLEESILGWK EYELELMRDK HDNVVVVCSI
     ENFDPMGVHT GDSITVAPAM TLTDREYQIL RDIGIAVIRE VGVDTGGCNI QFAVNPEDGR
     VIVIEMNPRV SRSSALASKA TGFPIAKIAA KLAVGYTLDE IPNDITEQTP ASFEPTLDYV
     VVKAPRFAFE KFPSADSTLT TTMKSVGEAM AIGRNFTEAL QKALRSLEKK GSQFTFVGEP
     GDKAELLREA VRPTDGRINC VMQAIRAGAT PEEVFEATKI DPWFVDQLFL IKEIADELAA
     AERLDPELLA DAKRHGFSDV QIAEIRGLRE DVVREVRHAL GVRPVYKTVD TCAAEFAAKT
     PYFYSSYDEE SEVAPRTKPA VIILGSGPNR IGQGIEFDYS CVHASFALSD AGYETVMVNC
     NPETVSTDYD TSDRLYFEPL TLEDVLEIVH AESLAGPVAG VVVQLGGQTP LGLSQALKDN
     GVPIVGTSPE AIHAAEDRGA FGRVLAEAGL PAPKHGTATT FAGAKAIADE IGYPVLVRPS
     YVLGGRGMEI VYDEARLEAY IAESTEISPT RPVLVDRFLD DAIEIDVDAL YDGEELYLGG
     VMEHIEEAGI HSGDSACALP PITLGGFDIK RLRASTEAIA KGVGVRGLIN IQFALAGDIL
     YVLEANPRAS RTVPFTSKAT AVPLAKAAAR ISLGATIAEL RAEGLLPANG DGGELPLDAP
     ISVKEAVMPW SRFRDIHGRG VDTVLGPEMR STGEVMGIDS VFGTAYAKSQ AGAYGPLPTK
     GRAFVSVANR DKRAMIFPAR ELVAHGFELL ATSGTAEVLK RNGINATIVR KQSEGEGPNG
     EKTIVQMIHD GEVDLIVNTP YGTGGRLDGY DIRTAAVARS VPCLTTVQAL AAAVQGIDAL
     NHGGVGVRSL QEHAEHLTAA RD
//