ID A0A0G1G7W7_9BACT Unreviewed; 741 AA.
AC A0A0G1G7W7;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Carbamoyl-phosphate synthase large subunit, carbamoyl-phosphate synthase large subunit {ECO:0000313|EMBL:KKS95048.1};
DE EC=6.3.4.16 {ECO:0000313|EMBL:KKS95048.1};
DE EC=6.3.5.5 {ECO:0000313|EMBL:KKS95048.1};
GN ORFNames=UV73_C0024G0005 {ECO:0000313|EMBL:KKS95048.1};
OS Candidatus Gottesmanbacteria bacterium GW2011_GWA2_43_14.
OC Bacteria; Candidatus Gottesmanbacteria.
OX NCBI_TaxID=1618443 {ECO:0000313|EMBL:KKS95048.1, ECO:0000313|Proteomes:UP000034894};
RN [1] {ECO:0000313|EMBL:KKS95048.1, ECO:0000313|Proteomes:UP000034894}
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:KKS95048.1}.
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DR EMBL; LCFP01000024; KKS95048.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1G7W7; -.
DR STRING; 1618443.UV73_C0024G0005; -.
DR PATRIC; fig|1618443.3.peg.1712; -.
DR Proteomes; UP000034894; 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 Gene3D; 3.40.50.20; -; 1.
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 InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
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; IPR016185; PreATP-grasp_dom_sf.
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 PRINTS; PR00098; CPSASE.
DR SMART; SM01096; CPSase_L_D3; 1.
DR SUPFAM; SSF48108; Carbamoyl phosphate synthetase, large subunit connection domain; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 2.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR PROSITE; PS50975; ATP_GRASP; 2.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KKS95048.1};
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 31..102
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 452..643
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 741 AA; 82963 MW; D97547C20BF949DB CRC64;
MENMDPLGVH TGESIVVAPS QTLTNFEYHY LRELSIKIVR SLGIVGECNV QFALNPSPTM
GPVSSQIDYY VIEVNARLSR SSALASKATG YPLAYVAAKL ILGKSLMEIK NQVTQITQSF
FEPALDYIVV KIPRWDMDKF KGTTEKINSS MKSVGEIMAI GRTFEETIQK GVRMLDIGVQ
GVTDNNFDLT EEEVLANIKQ ANSKRIFFIA KALKLGVSVE KIYQLSGIDP WFLYRLLEII
KAERELASVG NAYIRSLQPK QLLKYKQLGF SDKKIGQITG NSEFEIRNLR IKNKITPSVF
QIDTLAGEFP AKTNYLYTTY NGSHHDVKPI GDNGVMVLGS GPYRIGSSVE FDWTCVNSSL
FLKKYGKKSI IVNCNPETVS TDYDISDRLY FEELSFERVA DIYEFEKSSS VVVSVGGQTP
NNIAKKIDQY GIKILGTTAS NIDRAEDRKK FSQLLDDLKI KQPVWNSFTD MEVALKFSKE
VGYPILVRPS YVLSGAAMNL CYNPIELKHF IEKATNINKK HPVTISKYMV NAREIEFDGV
AEKGKVKVYA ISNHIEHAGV HSGDATIVYP AERVRFFSGE RMIEIANQLS KSLNISGPFN
IQFMVKDNEV YVIEMNLRAS RTFPFISKVT GVNFAEVIVD SFFGKSKEYK IKYPNYVAVK
APQFSFARME GADPALGVEM GSTGEVACFG DTAEEAYLKS LFSTGLSLTL PKKPIFFSKP
KAFGQNWSIN FLKKPVRPSL I
//
