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Database: UniProt
Entry: B1W463
LinkDB: B1W463
Original site: B1W463 
ID   CARB_STRGG              Reviewed;        1102 AA.
AC   B1W463;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   RecName: Full=Carbamoyl phosphate synthase large chain {ECO:0000255|HAMAP-Rule:MF_01210};
DE            EC=6.3.4.16 {ECO:0000255|HAMAP-Rule:MF_01210};
DE            EC=6.3.5.5 {ECO:0000255|HAMAP-Rule:MF_01210};
DE   AltName: Full=Carbamoyl phosphate synthetase ammonia chain {ECO:0000255|HAMAP-Rule:MF_01210};
GN   Name=carB {ECO:0000255|HAMAP-Rule:MF_01210}; OrderedLocusNames=SGR_6051;
OS   Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=455632;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 4626 / NBRC 13350;
RX   PubMed=18375553; DOI=10.1128/jb.00204-08;
RA   Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA   Yamashita A., Hattori M., Horinouchi S.;
RT   "Genome sequence of the streptomycin-producing microorganism Streptomyces
RT   griseus IFO 13350.";
RL   J. Bacteriol. 190:4050-4060(2008).
CC   -!- FUNCTION: Large subunit of the glutamine-dependent carbamoyl phosphate
CC       synthetase (CPSase). CPSase catalyzes the formation of carbamoyl
CC       phosphate from the ammonia moiety of glutamine, carbonate, and
CC       phosphate donated by ATP, constituting the first step of 2 biosynthetic
CC       pathways, one leading to arginine and/or urea and the other to
CC       pyrimidine nucleotides. The large subunit (synthetase) binds the
CC       substrates ammonia (free or transferred from glutamine from the small
CC       subunit), hydrogencarbonate and ATP and carries out an ATP-coupled
CC       ligase reaction, activating hydrogencarbonate by forming carboxy
CC       phosphate which reacts with ammonia to form carbamoyl phosphate.
CC       {ECO:0000255|HAMAP-Rule:MF_01210}.
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:0000255|HAMAP-
CC         Rule:MF_01210};
CC   -!- CATALYTIC ACTIVITY: [Carbamoyl phosphate synthase large chain]:
CC       Reaction=2 ATP + hydrogencarbonate + NH4(+) = 2 ADP + carbamoyl
CC         phosphate + 2 H(+) + phosphate; Xref=Rhea:RHEA:18029,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228,
CC         ChEBI:CHEBI:456216; EC=6.3.4.16; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01210};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01210};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01210};
CC       Note=Binds 4 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01210};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl
CC       phosphate from bicarbonate: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_01210}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       (S)-dihydroorotate from bicarbonate: step 1/3. {ECO:0000255|HAMAP-
CC       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. Tetramer of
CC       heterodimers (alpha,beta)4. {ECO:0000255|HAMAP-Rule:MF_01210}.
CC   -!- DOMAIN: The large subunit is composed of 2 ATP-grasp domains that are
CC       involved in binding the 2 ATP molecules needed for carbamoyl phosphate
CC       synthesis. The N-terminal ATP-grasp domain (referred to as the
CC       carboxyphosphate synthetic component) catalyzes the ATP-dependent
CC       phosphorylation of hydrogencarbonate to carboxyphosphate and the
CC       subsequent nucleophilic attack by ammonia to form a carbamate
CC       intermediate. The C-terminal ATP-grasp domain (referred to as the
CC       carbamoyl phosphate synthetic component) then catalyzes the
CC       phosphorylation of carbamate with the second ATP to form the end
CC       product carbamoyl phosphate. The reactive and unstable enzyme
CC       intermediates are sequentially channeled from one active site to the
CC       next through the interior of the protein over a distance of at least 96
CC       A. {ECO:0000255|HAMAP-Rule:MF_01210}.
CC   -!- SIMILARITY: Belongs to the CarB family. {ECO:0000255|HAMAP-
CC       Rule:MF_01210}.
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DR   EMBL; AP009493; BAG22880.1; -; Genomic_DNA.
DR   RefSeq; WP_003970364.1; NC_010572.1.
DR   AlphaFoldDB; B1W463; -.
DR   SMR; B1W463; -.
DR   GeneID; 6210781; -.
DR   KEGG; sgr:SGR_6051; -.
DR   eggNOG; COG0458; Bacteria.
DR   HOGENOM; CLU_000513_1_0_11; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000001685; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004087; F:carbamoyl-phosphate synthase (ammonia) activity; IEA:RHEA.
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; Arginine biosynthesis; ATP-binding; Ligase;
KW   Magnesium; Manganese; Metal-binding; Nucleotide-binding;
KW   Pyrimidine biosynthesis; Repeat.
FT   CHAIN           1..1102
FT                   /note="Carbamoyl phosphate synthase large chain"
FT                   /id="PRO_1000138898"
FT   DOMAIN          137..334
FT                   /note="ATP-grasp 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   DOMAIN          682..873
FT                   /note="ATP-grasp 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   DOMAIN          955..1100
FT                   /note="MGS-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   REGION          1..408
FT                   /note="Carboxyphosphate synthetic domain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   REGION          409..551
FT                   /note="Oligomerization domain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   REGION          552..954
FT                   /note="Carbamoyl phosphate synthetic domain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   REGION          955..1102
FT                   /note="Allosteric domain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         129
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         175
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         181
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         182
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         214
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         216
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         221
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         247
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         248
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         249
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         291
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         291
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         291
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         305
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         305
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         305
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         305
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         305
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         307
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         307
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         718
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         757
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         759
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         764
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         789
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         790
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         791
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         792
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         832
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         832
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         832
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         844
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         844
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         844
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         844
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         844
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         846
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         846
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
SQ   SEQUENCE   1102 AA;  117431 MW;  30A8D14BC6C3FA04 CRC64;
     MPKRSDIQSV LVIGSGPIVI GQAAEFDYSG TQACRVLKAE GLRVILVNSN PATIMTDPEI
     ADATYVEPIT PEFVEKIIAK ERPDALLPTL GGQTALNTAI SMHDNGVLEK YGVELIGANV
     EAINKGEDRD LFKGVVEAVK EKIGYGESAR SVICHSMDDV IAGVDTLGGY PVVVRPSFTM
     GGAGSGFAHD EEELRRIAGQ GLTLSPTTEV LLEESILGWK EYELELMRDR NDNVVVVCSI
     ENFDPMGVHT GDSITVAPAM TLTDREYQRL RDVGIAIIRE VGVDTGGCNI QFAIDPTDGR
     VIVIEMNPRV SRSSALASKA TGFPIAKIAA KLAVGYTLDE IPNDITEKTP ASFEPTLDYV
     VVKAPRFAFE KFPSADSSLT TTMKSVGEAM AIGRNFTEAL QKALRSLEKK GSQFAFTGPV
     GDKAELLAEA VRPTDGRINT VMQAIRAGAT QEEVFDATKI DPWFVDQLFL IKEIADELAS
     AERLDAGLIA EAKRHGFSDA QIGGIRGLRE DVVREVRHAL GIRPVYKTVD TCAAEFAAKT
     PYFYSSYDEE SEVAPRTKPA VIILGSGPNR IGQGIEFDYS CVHASFALSD AGYETVMVNC
     NPETVSTDYD TSDRLYFEPL TLEDVLEIVH AESLAGPIAG VIVQLGGQTP LGLSQALKDN
     GVPVVGTSPE AIHAAEDRGA FGRVLAEAGL PAPKHGTATT FAEAKAIADE IGYPVLVRPS
     YVLGGRGMEI VYDETRLASY ISESTEISPT RPVLVDRFLD DAIEIDVDAL YDGTELYLGG
     VMEHIEEAGI HSGDSACALP PITLGGFDIK RLRASTEGIA KGVGVLGLIN IQFALSGDIL
     YVLEANPRAS RTVPFTSKAT AVPLAKAAAR ISLGATIAEL RAEGLLPRTG DGGTLPLDAP
     ISVKEAVMPW SRFRDIHGRG VDTVLGPEMR STGEVMGIDS VFGTAYAKSQ AGAYGPLPTA
     GRAFISVANR DKRSMIFPAR ELVAHGFELM ATSGTAEVLK RNGINATVVR KQSEGTGPNG
     EKTIVQHIHD GEVDLIVNTP YGTGGRLDGY EIRTAAVARS VPCLTTVQAL AAAVQGIDAL
     NHGGVGVRSL QEHAEHLTAA RD
//
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