ID A0A1F6LJJ0_9BACT Unreviewed; 1067 AA.
AC A0A1F6LJJ0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Carbamoyl phosphate synthase large subunit {ECO:0000313|EMBL:OGH59495.1};
GN ORFNames=A2725_01580 {ECO:0000313|EMBL:OGH59495.1};
OS Candidatus Magasanikbacteria bacterium RIFCSPHIGHO2_01_FULL_33_34.
OC Bacteria; Candidatus Magasanikbacteria.
OX NCBI_TaxID=1798671 {ECO:0000313|EMBL:OGH59495.1, ECO:0000313|Proteomes:UP000177067};
RN [1] {ECO:0000313|EMBL:OGH59495.1, ECO:0000313|Proteomes:UP000177067}
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:OGH59495.1}.
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DR EMBL; MFPS01000007; OGH59495.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6LJJ0; -.
DR Proteomes; UP000177067; 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 139..331
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 673..864
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 927..1067
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 1067 AA; 119187 MW; 4C54966AF2161DF3 CRC64;
MNKLNIKKVL LLGSGGLRIG QAGEFDYSGS QAIKALKEEG IHTVLINPNI ATIQTDGQGF
SKSKKAADTV YLQPLNVQTV TKIIEKEKPD AIFLSFGGQT ALNLGLELDE IGIFKKYNVK
VLGTPIKTIR LTEDRELFKQ ALKEIDVKTA RSIATDNITE AISAAKKIGY PIMMRSGYSL
GGLGSGLIKT EEELKIRANE ALHQAPQILI EEYLGGWKEV EYEIVRDSAD NVVTVCNMEN
MDPMGIHTGE SIVVAPSQTL NNHEYHLLRE IAIKTASHIG IIGECNIQYA LNPENGDYRV
IEINARLSRS SALASKATGY PLAFIAAKLG INIRLDEIKN SVTQKTSAFF EPALDYLVIK
IPKWDINKFK NAEQHIGSEM KSVGEVMAIG RSFPETLQKA VRMLNIGTQG LNDYPYKIEN
LKDEIENPTF RRLFAIYQYF KKGATVNEIF KLSKINPWFL HHIYSIAQME KNITKNNLDK
TTLQQAKQFG FSDKTIAKLK NTTEKEIRAK RINLNIKPII KQIDTLAGEF PAKTNYLYTT
YNGQYHDILR SKKKPIIVIG SGPYCIGSSV EFDWCAVNTA RTLKKLKEST IIINSNPETV
STDYDESDRL YFEELTAERI ADIADFENTK GIIVSVGGQI PNNIALPLSK AGYPILGTNA
TSIDQAEDRQ KFSSLLNKLN IDQPTWEEVS TLSKARSFAE RIGYPVLVRP SYVLSGAAMN
VIYDESELKN YLANSATVSP DHPAVLSKFI QNAKELEVDG VAKQGQIIIE AITEHVENAG
VHSGDATIIL PPQRLYLETI RRAKKLTAKI VKALNITGPF NIQFIAKDNW LKIIECNVRA
SRSFPFVSKV TNNNFIEIMT EVILNKHKSK TYQTLELDYV GVKTPQFSYS RLKGSDPVAH
VEMASTGEVA CIGDNYLEAF FTSWLSTEQS ISGKRILLSI GDEKKNKLIN LIQALDEQNW
EIFATEGTHK YLAEYGIAST FLHKASVDAS PNITDTIENK KIDLILNIPR SNGTSNKTDG
FKIRRLAIDH QIPLITNLQI AQLFLRSITE LKLENVPVKS WQEFIKN
//
