ID A0A0G1WXC8_9BACT Unreviewed; 1075 AA.
AC A0A0G1WXC8;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Carbamoyl-phosphate synthase, large subunit {ECO:0000313|EMBL:KKW23396.1};
GN ORFNames=UY65_C0004G0022 {ECO:0000313|EMBL:KKW23396.1};
OS Parcubacteria group bacterium GW2011_GWA2_51_12.
OC Bacteria.
OX NCBI_TaxID=1618856 {ECO:0000313|EMBL:KKW23396.1, ECO:0000313|Proteomes:UP000034905};
RN [1] {ECO:0000313|EMBL:KKW23396.1, ECO:0000313|Proteomes:UP000034905}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKW23396.1}.
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DR EMBL; LCQU01000004; KKW23396.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1WXC8; -.
DR PATRIC; fig|1618856.3.peg.128; -.
DR Proteomes; UP000034905; 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..327
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 672..863
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 925..1075
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 1075 AA; 118638 MW; 465C67CCE992FA67 CRC64;
MNYKNQKILV LGSGALKIGE AGEFDYSGSQ AMKALREEGV KIVLVNPNIA TIQTSPLLAD
EIYFLPVTPE FVVRVIAKER PDAILLSFGG QTALNCGVAL HKSGILKKYR VAVLGTPVGS
IILTEDRQKF ADHLKKIKIP IPESGATASA VSAESIAKKI GYPVMVRAAF TLGGQKSGVA
RDLAELREIA AGALAVAPQI LVEKYLEHYK EIEYEVVRDR AGNCVTVCNM ENFDPMGIHT
GDSIVVAPSQ TLTNEEYHGL RRAAIDIVQS LAIVGECNVQ FALNPKPKGE KLEYYVIEVN
ARLSRSSALA SKATGYPLAY VAAKLALGQI LSEVKNQVTK VTQSFFEPAL DYVVVKIPRW
DIEKFKGAEE RIGSAMKSVG EVMAIGRTFE EALQKAVRML HSGAEGVTEN GFGPDKKSLE
RFLHIPTPKR LFAVAEALKR GIKAERIHEL SGIDLWFIWR INNIVQWEKK LLKHKKLGHD
LLLKLKQLGF SDRRIALLRK TDAAEIRKLR HSYGLRPSVF QIDTLAGEAP AKTNYLYLTY
NGAHHDVSPL GKRAVVVLGS GPYHIGSSVE FDWSCVHTAL SLRKYGKQSI IVNCNPETVS
TDYDMSRRLY FEELTFETIS EIYEFEKPSG VVVSVGGQTP NNLARDFSAA GFHILGTTAA
NIDRAEDRNK FSALLDSLGI PQPLWKSFVS MSEALRFARE VGYPVLVRPS YVLSGSAMSV
CFDNEELRLL VEKAAVINRA HPVTISKFIT GAKELELDAV AQRGKILAAF LSEHVENAGV
HSGDATIVYP AQKVYTATEQ RILQIAESLA RDLQITGPFN IQFLVKENKA FVIEINLRAS
RTFPLLSKAT NVNLADLLVA AFFGRGRAPK IKYPDYVVVK SPQFSFSRLQ GADPVLRVEM
ASTGEVACFG DTFEEALLKS IYSSITFSPR KSALLALGGA VNKKRFLDAA RRLVAKGYKL
YATGTTHRFL QENAVPSKLV SKVYEGKKPD VVDLINSKRV GFVVNLSEQD EGPERHHKEH
VSDGYLIRRA AVDNNTPLFT NSLLARAFVR AVTSFGPKDL KIKSWREYTE SNLHE
//
