CARB_THET2
ID CARB_THET2 Reviewed; 1028 AA.
AC P96495;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Carbamoyl-phosphate synthase large chain {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=TT_C0247;
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Baetens M., Van de Casteele M., Legrain C., Glansdorff N.;
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(2004).
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 4 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250};
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.
CC {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; Y11467; CAA72256.1; -; Genomic_DNA.
DR EMBL; AE017221; AAS80595.1; -; Genomic_DNA.
DR RefSeq; WP_011172699.1; NC_005835.1.
DR AlphaFoldDB; P96495; -.
DR SMR; P96495; -.
DR STRING; 262724.TT_C0247; -.
DR EnsemblBacteria; AAS80595; AAS80595; TT_C0247.
DR KEGG; tth:TT_C0247; -.
DR eggNOG; COG0458; Bacteria.
DR HOGENOM; CLU_000513_1_0_0; -.
DR OMA; IEPAGIH; -.
DR OrthoDB; 48855at2; -.
DR UniPathway; UPA00068; UER00171.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000000592; 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 Gene3D; 1.10.1030.10; -; 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; IPR016185; PreATP-grasp_dom_sf.
DR Pfam; PF02786; CPSase_L_D2; 2.
DR Pfam; PF02787; CPSase_L_D3; 1.
DR PRINTS; PR00098; CPSASE.
DR SMART; SM01096; CPSase_L_D3; 1.
DR SUPFAM; SSF48108; SSF48108; 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; Arginine biosynthesis; ATP-binding; Ligase;
KW Magnesium; Manganese; Metal-binding; Nucleotide-binding;
KW Pyrimidine biosynthesis; Repeat.
FT CHAIN 1..1028
FT /note="Carbamoyl-phosphate synthase large chain"
FT /id="PRO_0000145059"
FT DOMAIN 133..328
FT /note="ATP-grasp 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT DOMAIN 674..866
FT /note="ATP-grasp 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT DOMAIN 934..1028
FT /note="MGS-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
FT REGION 1..409
FT /note="Carboxyphosphate synthetic domain"
FT REGION 410..549
FT /note="Oligomerization domain"
FT REGION 550..933
FT /note="Carbamoyl phosphate synthetic domain"
FT REGION 934..1028
FT /note="Allosteric domain"
FT BINDING 159..216
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 285
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 299
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 299
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 301
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 700..758
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 825
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 837
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 837
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 839
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT CONFLICT 329
FT /note="G -> P (in Ref. 1; CAA72256)"
FT /evidence="ECO:0000305"
FT CONFLICT 489
FT /note="K -> Q (in Ref. 1; CAA72256)"
FT /evidence="ECO:0000305"
FT CONFLICT 536
FT /note="T -> P (in Ref. 1; CAA72256)"
FT /evidence="ECO:0000305"
FT CONFLICT 576
FT /note="A -> P (in Ref. 1; CAA72256)"
FT /evidence="ECO:0000305"
FT CONFLICT 613
FT /note="F -> V (in Ref. 1; CAA72256)"
FT /evidence="ECO:0000305"
FT CONFLICT 628
FT /note="E -> Q (in Ref. 1; CAA72256)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1028 AA; 113609 MW; DD032A40E389B4CE CRC64;
MPPRRDLKKI LIIGSGPITI GQAAEFDYSG TQAVKALRGA GYRVVLVNSN PATIMTDPEL
AERTYIEPLD LEHLEGILAR EAPDALLPTL GGQTGLNLAM ALYEEGILQK YGVELIGAKA
EAIRKGEDRE AFQEAMRRID LEVPRGQLVG SVEEGLHFAR EVGFPVVVRP SFTLGGTGGG
IAHDEAELVE VLSRGLTLSP VHTALVEESV LGWKEFELEV MRDHADTVVI ITSIENVDPM
GVHTGDSITV APAQTLSDVE YQRMRDAAKA IIREIGVETG GSNIQFAVDP KTGRQVVIEM
NPRVSRSSAL ASKATGFPIA KIAALLAVGY RLDELPNDIT RKTPASFEPT IDYVVVKIPR
FAFEKFRPLR NTLGELKDEL TTQMKSVGEV MAIGRTFKEA LMKALRGLER DVRALAGVRT
EELEKKLYPN PDRVYAVMEL LRRGMPVEEL YQATRIDPWF LHQMKEIVEA EEWLKTHPPK
DREDWRFYKG LGLTDRRIGE LLGKGEKEVR AERKALGVVP VYKTVDTCAA EFEAYTPYHY
STYELEDEVW PSQKPKVVIL GSGPIRIGQG VEFDYATVHA VWALKEAGFE TIMVNSNPET
VSTDYDTADR LYFEPLTLED VLNIVEHEKP IGVIATLGGQ TPLKLAKGLE EAGVRLLGTP
FSAIHQAEDR EAFHALCQRL GIPQPEGRVA QSPEEALRLA PEVGFPLLVR PSYVLGGRAM
QVVRDEGELK RYLEEVYAPL EERPSILLDR FLEGAIELDV DALSDGQEVM VAGIMEHVER
AGVHSGDSAT LLPPVHVPEE ALKKVRDYTR RLALTLGVRG LLNVQYAVVG EEVYVLEANP
RASRTVPFVS KAIGVPLAKL AALIAVGKTL KELGVRDLDP VPPYYAAKEV VIPWIKFPGV
IPELGPEMRS TGESMGIDQD PYLAYYKAEL GAGQRLPLSG QVRFIGEGLE DLKALYQEAG
FALTEGQDYD LLISLVPDPE LRRAVERGLP FITTREGAWW SLKAILRARE SGLRVQSLQD
WHQKAPRG
