ID A0A1F5Q9U3_9BACT Unreviewed; 1085 AA.
AC A0A1F5Q9U3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Carbamoyl phosphate synthase large subunit {ECO:0000313|EMBL:OGE98550.1};
GN ORFNames=A3J05_04210 {ECO:0000313|EMBL:OGE98550.1};
OS Candidatus Doudnabacteria bacterium RIFCSPLOWO2_02_FULL_48_13.
OC Bacteria; Candidatus Doudnabacteria.
OX NCBI_TaxID=1817845 {ECO:0000313|EMBL:OGE98550.1, ECO:0000313|Proteomes:UP000177235};
RN [1] {ECO:0000313|EMBL:OGE98550.1, ECO:0000313|Proteomes:UP000177235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- CATALYTIC ACTIVITY:
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;
CC Evidence={ECO:0000256|ARBA:ARBA00043687};
CC -!- SIMILARITY: Belongs to the CarB family.
CC {ECO:0000256|ARBA:ARBA00009799}.
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:OGE98550.1}.
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DR EMBL; MFFF01000030; OGE98550.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5Q9U3; -.
DR Proteomes; UP000177235; 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-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:UniProt.
DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:UniProtKB-KW.
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 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; 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; 1.
DR PROSITE; PS00867; CPSASE_2; 2.
DR PROSITE; PS51855; MGS; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 131..337
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 684..875
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 935..1085
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 1085 AA; 121116 MW; A47E6CFDC0D18B5B CRC64;
MIVNPKKILV LGSGALKIGE AGEFDYSGSQ AMKALKEEKI KIILINPNIA TIQTSPLLAD
EIYFLPVTPY FVEKVIARER PDGILLSFGG QTALNCGLAL HRKGILKKYR VRVLGTPVEA
IVLTEDRQKF ADHLTKLGIS VPKSKAATTL PAAVNIAKSI GYPVMVRAAY ALGGQKSGMA
RNRPELEALA RGALAIAPQI LVEKYLHHYK ELEYEVVRDA YDNCITVCNM ENMDPLGIHT
GDSIVVAPSQ TLTNDEYHLL REASQKIVRS LGIVGECNVQ YAVNPRPTSP RRSSVGQANP
RFEFEVIEVN ARLSRSSALA SKATGYPLAY VAAKLALGKS LLDVQNQVTK VTRSFFEPSL
DYVVVKIPRW DLEKFRGAEE KIGSAMKSVG EVMAIGRTFE EAIQKGVRML GGRVQGVADN
RFPDDKKTIL RYLSIPTPKR LFALAESMRR GVSIKEIYKL TGIDPWFLHR IKNIVDHEQV
LAKIKKKGLS KLFFLKLKQL GFSDRRIARI LDIPDEDVTE LRRKMKIRPS VFQIDTLAGE
IPAKTNYLYL TYNGSHHDVK PLGPRSVIVL GSGPYHIGSS VEFDWSAVAT ALALPEYGRQ
SIIINCNPET VSTDYDMSER LYFDELSFET VSEIYDFENP EGLVVSVGGQ RPNNLAPRLA
AIGAKILGTS AENIDRAEDR NKFSALLDRL SIPQPRWNSF TDMQEAKQFA STVRYPVLVR
PSYVLSGSAM SVCYNERELE LFIEKATTLN KTHPVTISKF FTGAREIEFD AVAQKGRIQI
YAISEHIENA GVHSGDATIV YPTQRVYAST ERRIQKIAKD LARELEITGP INIQFLVKDN
KVYVIEANLR ASRTFPFLSK ATRFNFAEVI VASFYGKARR IEIPYPDYAV VKSPQFSFAR
LAGADPLLHV EMSSTGEVAC FGDTAEEALL KSIYASVPLS DKKAVLLSLG GAVNKKKFLE
HAQMLYRAGY KIYATDTTCD FLNENNISSR KVYKVQENRK LNVLEFINQK KVAFVVNLTE
RDPEEQQALS PKITDGQLIR RAAVDNNIPL FTDLQLARSF VKALTTYKLD DLKIKSWNEY
QGQNL
//
