ID A0A0G0VSS3_9BACT Unreviewed; 1064 AA.
AC A0A0G0VSS3;
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:KKS03959.1};
GN ORFNames=UU56_C0012G0033 {ECO:0000313|EMBL:KKS03959.1};
OS Candidatus Curtissbacteria bacterium GW2011_GWA2_41_24.
OC Bacteria; Candidatus Curtissbacteria.
OX NCBI_TaxID=1618411 {ECO:0000313|EMBL:KKS03959.1, ECO:0000313|Proteomes:UP000034493};
RN [1] {ECO:0000313|EMBL:KKS03959.1, ECO:0000313|Proteomes:UP000034493}
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:KKS03959.1}.
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DR EMBL; LCBC01000012; KKS03959.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0VSS3; -.
DR PATRIC; fig|1618411.3.peg.765; -.
DR Proteomes; UP000034493; 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 130..336
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 690..881
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 944..1064
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 1064 AA; 118118 MW; BBCBD39870B190DB CRC64;
MKKIKKVLLL GSGALKIGQA GEFDYSGSQA IKALKEESIK VILVNPNIAT IQTSQGFANT
VYFLPIEPYF VKKIIQKEKP DGIILSFGGQ TALNCGLLLA KDRIFQKYQV EVLGTSIETI
EKTEDRQLFV NTLDQINLKC PQSQAVKTVK QALAVATTIG YPIMIRGGFS LGGQDSGMAQ
NRKQLVEIAT RALAKVGQIL IEEYLDKWKE VEYEVVRDKF DNCITVCNME NIDPMGIHTG
ESIVVAPSQT LNNFEYHKLR EISIKVIRHL GIVGECNIQF ALNPNPKWDP ASHFSSLTSS
LDYRIIEVNA RLSRSSALAS KATGYPLAYI AAKLALGYSL TDLQNSVTKK TIACFEPALD
YLVVKFPRWD LAKFLKSQTE IGSSMQSVGE VMAVGRKFEE AIQKAVRMLD IGFEGILDEK
APKVSWAKPT PWRIFAIARA IRQKTAVEKI AQATGIDPFF LYKLKNICDF EKSIKVSKQK
THGTPDTFNS RDALLLAKQL GFSDKRLTTL TGSTKDKIRQ LRHKFDIHPS VKQIDTLAAE
YPAETNYLYL TYNGESDDVV SQRSNVKGQM SKVIVLGSGP YRIGSSVEFD WCSVTCAQTA
ESCNFSTIII NCNPETVSTD FDMAQKLYFE ELTEETITEI YHKEKPSGLI VSMGGQTPNN
LATKLTQRGL AILGTKVTSI DRAEDRSKFS KLCDELDIAQ PVWAKLKNVG EAIVFAQKIG
YPVLVRPSYV LSGAAMNVAF NPQDLEAYLL AASQVSAEYP VVISQFHQNS KEIEIDAVAK
NGKVLCQAII EHVENAGVHS GDSSMVLPAQ KLYTQTIEQI KKIAQKIARE LNITGPFNIQ
FLAENNRVMV IECNLRASRS LPFVSKVTGI NFAKLATEAI LGIDQRPETR DQRPDYVAVK
APQFSFARIK GADPILRVEM ASTGEVACFG DDIYEAYLKS QIATGVSLPK KSVFISLAGE
ENKIKFQEAA KTLFKMGLKI YATAGTAQFF KNHGIDVTKL YKIHEHQKPN VLDFLLAKKI
DLVINIFDPY FKKEFDDDYL IRRASIDFGI PLLANMQAAI LGII
//
