ID A0A0S8IXT7_9BACT Unreviewed; 722 AA.
AC A0A0S8IXT7;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Carbamoyl phosphate synthase large subunit {ECO:0000313|EMBL:KPL01954.1};
DE EC=6.3.5.5 {ECO:0000313|EMBL:KPL01954.1};
DE Flags: Fragment;
GN Name=carB {ECO:0000313|EMBL:KPL01954.1};
GN ORFNames=AMK75_03375 {ECO:0000313|EMBL:KPL01954.1};
OS Planctomycetes bacterium SM23_65.
OC Bacteria; Planctomycetota.
OX NCBI_TaxID=1704030 {ECO:0000313|EMBL:KPL01954.1, ECO:0000313|Proteomes:UP000052185};
RN [1] {ECO:0000313|EMBL:KPL01954.1, ECO:0000313|Proteomes:UP000052185}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_65 {ECO:0000313|EMBL:KPL01954.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(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:KPL01954.1}.
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DR EMBL; LJUT01000059; KPL01954.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8IXT7; -.
DR Proteomes; UP000052185; 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; -; 2.
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; 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; 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 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; 2.
DR PROSITE; PS50975; ATP_GRASP; 2.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
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:KPL01954.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975}.
FT DOMAIN 133..328
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 684..722
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT NON_TER 722
FT /evidence="ECO:0000313|EMBL:KPL01954.1"
SQ SEQUENCE 722 AA; 79137 MW; 2D5C510074D68EAC CRC64;
MPKRTDLKKI LIIGSGPIII GQACEFDYSG SQACKALKEE GYEVVLVNSN PATIMTDPRM
ADRTYVEPIT AEVIEKIIAR ERPDAILPTL GGQTGLNVAV FLSRAGVYDR YGVEVLGASA
EAISRAEDRD LFKQAMQEIG LGVPDSGIAT SVEEGMAIGE RIGFPLILRP AFTLGGFGGA
TAYNVEELEE YLSKAITISP VGQVLVEQSV LGWKEIEFEV MRDCADNVIM ITSMENIDAM
GVHTGDSMVV APSQTLTAKE YKQYVDLSRR IIRKIDITGG GVNIQFAGNP ENGDIVVIEV
NPRLSRSSAL ASKATGFPIA RVATKLAVGL TLDEIMNDVT GKTSTFFEPT VDYCVFKIAR
FTFKKFPQAD PTVNTSMKSV GEAMSIGRSF QEALQKGVRS LEIGRYGLGF DGRDSRVDVP
KNDAELTHKL VVPNDKRHFY VKYALERGWS VEDVARLTHI DPWFVQNIAG IIELGGRIAA
FRGKRGVEKI PEPLWWEIKG AGFSDVQIAE LTGTDEVTVY GVRNRRGVCP AYKLVDTCAG
EFDPDRPYFY STYERLNENR VSDRKKVIIL GGGPNRIGQG IEFDYCCCHA SYAVKELGYE
AIMINSNPET VSTDYDTSDK LYFEPLTRED VLAIVEQEKP EGVIVQLGGQ TPLNLAVPLE
QAGVRILGTS PDSIDRAEDR ERFKQLLAKL GLVQAPNGTA TSYEQAKVIA ADIGYPVMVR
PS
//
