ID A0A1F5JV80_9BACT Unreviewed; 1059 AA.
AC A0A1F5JV80;
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:OGE32529.1};
GN ORFNames=A3C59_01510 {ECO:0000313|EMBL:OGE32529.1};
OS Candidatus Daviesbacteria bacterium RIFCSPHIGHO2_02_FULL_36_13.
OC Bacteria; Candidatus Daviesbacteria.
OX NCBI_TaxID=1797768 {ECO:0000313|EMBL:OGE32529.1, ECO:0000313|Proteomes:UP000176902};
RN [1] {ECO:0000313|EMBL:OGE32529.1, ECO:0000313|Proteomes:UP000176902}
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:OGE32529.1}.
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DR EMBL; MFCV01000025; OGE32529.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5JV80; -.
DR STRING; 1797768.A3C59_01510; -.
DR Proteomes; UP000176902; 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 127..319
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 660..851
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 916..1059
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 1059 AA; 117312 MW; 84D58EE4EF037401 CRC64;
MKKILVLGSG ALKIGEAGEF DYSGSQALKA LKEEGIETVL INPNIATIQT SKDLASKIYF
LPVTPYFVEK VIQKEKIDGI FLSFGGQTAL NCGLALEKSG IFKKYGVKVL GTPVKSIQIT
EDREIFAKEL ASVDVKVPKG GFAKTVEQAL KIGEKLGYPL LIRSGFSLGG LGSGVCENKE
ELTKMAGNAL KHTSQIAVEE YLRHWKEIEY EIVRDKMGNK ITVCNMENFD PLGIHTGESI
VVAPSQTLNN FQYHMLRRLS LKVIEHLGIV GECNIQFALD PKTNDYRVIE VNARLSRSSA
LASKATGYPL AYIAAKIGLG YNLPELKNSV THSTSAFFEP ALDYLVVKIP RWDLQKFVGA
KESIGSEMKS VGEVMAIGRS FPEALQKAVR MLDTGQDGLL GNHIDDTKLL PTAERLFAIA
QSFNKGENVE NIYKQTGIDP WFLHQLKQIV NFEKGMKSLK EIPKAKKLGF SDKVIAKTLG
KSEDEIRKFR KSHGIVPKVK HIDTLAAEYP AKTNYLYLTY HGEESEVRDS LFVNSSTKNE
VRKAIVLGSG PYRIGSSVEF DWCSVTAAQA LRKKGLETII INCNPETVST DYDIADKLYF
EELTFERVSD IYDLEGGSLV LSFGGQVPNN LAMQAFKAGY KILGTSPESI DRAEDRNKFS
NILDKLKIEQ PKWQSVKAID EALKFAKLIG YPVLVRPSYV LSGSAMNVAY SQGELKKYLE
QAAAVSSEHP VVLSKFVEGA KEIEIDGVGS RGELLIYAIS EHVENAGVHS GDATIVLPPQ
RLFLETVRKI KTATKRIVKE LNITGPFNIQ FLAKNNQIMV IELNLRASRS FPFVSKVTGY
NFVEMATRVM LGEEITGDFK TIDLDYVAVK APQFSFNRIK GADPRLRVEM SSTGEVACFG
DDLHEAYLKS LMSTGFKMPK KSVFLSIGGQ KNKLDMLLTA KKLINLGLKI YATENTHKFL
KESGIKNQRV YKISEEKHPS LLDLLRDGEI DLAINISEGS ATEKGETDGF IIRRNCIDLG
IPLITNLQSA ELLISALTSK KMDDLQIKSW DEYVAGNVR
//
