ID A0A1J4WW94_9BACT Unreviewed; 1074 AA.
AC A0A1J4WW94;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Carbamoyl phosphate synthase large subunit {ECO:0000313|EMBL:OIO53328.1};
GN ORFNames=AUJ46_05510 {ECO:0000313|EMBL:OIO53328.1};
OS Candidatus Peregrinibacteria bacterium CG1_02_54_53.
OC Bacteria; Candidatus Peregrinibacteria.
OX NCBI_TaxID=1805323 {ECO:0000313|EMBL:OIO53328.1, ECO:0000313|Proteomes:UP000183121};
RN [1] {ECO:0000313|EMBL:OIO53328.1, ECO:0000313|Proteomes:UP000183121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG1_02_54_53 {ECO:0000313|EMBL:OIO53328.1};
RX PubMed=27112493;
RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 0:0-0(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:OIO53328.1}.
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DR EMBL; MNWP01000033; OIO53328.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J4WW94; -.
DR STRING; 1805323.AUJ46_05510; -.
DR Proteomes; UP000183121; 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; 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 137..329
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 676..867
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 933..1074
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 1074 AA; 118316 MW; BB20F3C53D4F66AA CRC64;
MPSLDPRRLK DKTILLLGSG ALKIGEAGEF DYSGSQAIKA FKEEGAHVVL VNPNIATNQT
SWNLADRVYF VPVTPQFVER IIAQEHPQAI ALSFGGQTAL NCGLALADSG VLKKHNVAVL
GAPVESIRKT EDRALFNAEL ASINVDVPRS QACESLDAAL RAAKEIGFPV IIRGAFALGG
KGSGRAMNEK ELHEICKVAF VESPQVLIEE DLTGWKEIEY EVVRDCADNC ITVCNMENVD
PLGIHTGESI VIAPSQTLDN EDYQMLRSIA LRVIRHLGIV GECNIQYALD PRSRRYRVIE
VNARLSRSSA LASKATGYPL AFIAAKLALG YTLPDLRNAI TQVTCADFEP SLDYVAVKMP
RWDLQKFRHV SDTVTSEMKS VGEVMALGRT FEEALQKAIR MLNIGEEGLV PCSMKFSDHG
KEIKRPTPRR LFAVAAALAG EWSVEEVSIA TGIDRWFLER IRTCVTIAAD LQRTRAKSPL
TSSLLRQAKR TGFSDQAIGL LTDLSSNEVR ALRLEHGVTP VIKQIDTLAG EFPAQTNYLY
LTYHGTEHDM TFAGNAPRAI VLGGGPYSIG SSVEFDWCCV QAAHELQQQH YEVLMINSNP
ETVSTDYDEC DALFFDELTE ERVRDIADLT APAGIVVSMG GQIPNSLSPK LAAAGLPILG
TSPKDIDRAE DRHKFSLLLD ELKIDQPEWK EFSELSGASS FAQSVGYPVI VRPSYVLSGA
SMAVVHSHDD LTDYVQRSAF VNKEAPIVIS KFEIGAKEID FDGVAQDGQL LLYAISEHVE
NAGVHSGDAT LVLPPQRVNL ETLRRVKHIA KGIARGLHIS GPFNIQFLAK ENRLKVIECN
LRASRSFPFA SKVTGVNFII LATQALLKKA PKDKRYQTID LDHVGVKAAQ FSFSRLRGAD
PRLGVEMAST GEVACFGTNA EQALLLALIA VGFRLPKKNI LITVGHIEDK LDLFPSIKRL
ADRGFSFFAT QRTHEFLESR GIPSVLLHKI SEPRSPNIRE YLEQKRVDLV INVPTHSSSV
EQTDGYFIRR LATDHGIPLI TNVQLVKRVE EALQRETPES LPLLAWPQLL REER
//
