ID G2FM70_9FIRM Unreviewed; 956 AA.
AC G2FM70;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Carbamoyl-phosphate synthase, large subunit {ECO:0000313|EMBL:EGW41293.1};
DE EC=6.3.5.5 {ECO:0000313|EMBL:EGW41293.1};
DE Flags: Fragment;
GN ORFNames=DOT_0778 {ECO:0000313|EMBL:EGW41293.1};
OS Desulfosporosinus sp. OT.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfosporosinus.
OX NCBI_TaxID=913865 {ECO:0000313|EMBL:EGW41293.1, ECO:0000313|Proteomes:UP000004928};
RN [1] {ECO:0000313|EMBL:EGW41293.1, ECO:0000313|Proteomes:UP000004928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OT {ECO:0000313|EMBL:EGW41293.1,
RC ECO:0000313|Proteomes:UP000004928};
RX PubMed=21994931; DOI=10.1128/JB.06018-11;
RA Abicht H.K., Mancini S., Karnachuk O.V., Solioz M.;
RT "Genome Sequence of Desulfosporosinus sp. OT, an Acidophilic Sulfate-
RT Reducing Bacterium from Copper Mining Waste in Norilsk, Northern Siberia.";
RL J. Bacteriol. 193:6104-6105(2011).
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 -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl
CC phosphate from bicarbonate: step 1/1. {ECO:0000256|ARBA:ARBA00005077}.
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:EGW41293.1}.
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DR EMBL; AGAF01000041; EGW41293.1; -; Genomic_DNA.
DR RefSeq; WP_009614186.1; NZ_AGAF01000041.1.
DR AlphaFoldDB; G2FM70; -.
DR PATRIC; fig|913865.3.peg.720; -.
DR eggNOG; COG0458; Bacteria.
DR OrthoDB; 9804197at2; -.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000004928; 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:UniProtKB-KW.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:UniProt.
DR CDD; cd01424; MGS_CPS_II; 1.
DR Gene3D; 3.40.50.20; -; 1.
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; IPR033937; MGS_CPS_CarB.
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; 1.
DR PROSITE; PS50975; ATP_GRASP; 2.
DR PROSITE; PS00866; CPSASE_1; 2.
DR PROSITE; PS00867; CPSASE_2; 2.
DR PROSITE; PS51855; MGS; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EGW41293.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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 31..225
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 569..759
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 826..956
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EGW41293.1"
SQ SEQUENCE 956 AA; 105397 MW; 624708232B5BC8B7 CRC64;
AKRGVLERCE VTLMGTSLKS IDQAEDRESF RALMQELGEP IPESKIVAHV EEALEFAAKT
GYPLIVRPAF TLGGTGGGIV QNAEELEQIA ASGLQASLIG QILVERSVAG WKEVEFEVLR
DGAGNCITIC HMENMDPVGV HTGDSIVVAP CQTLTDREVQ ALRSASRRIV NGLGIEGGCN
VQFALHPARN EYVVIEVNPR LSRSSALASK ATGYPIAKVA AKIALGYALT EIKNAVTEKT
SACFEPALDY VVVKIPRWPF DKFTEADRRL GTQMKATGEV MGIGRNLETA LLKAIRSLDI
KAYGLRLPEL EVLSDAELKT ECLQPDDRQL FVFAEALRRG WTVDWLVEET GWNLFYLNFL
RRLVDNTVLL EQAAWDKASL LRAKRLGYAD LEIAALWKSS EDEVYRFRIE HGIRPVFKMV
DTCSGEFEAT TPYFYSSYDV EDEGEVHKRP KVVVLGSGPI RIGQGIEFDY CSVHAVLALR
KAGFESIIIN NNPETVSTDF DTADRLYFEP LTLEDVSAIL DKEQPDGVVV QFGGQTAIGL
ASGLARRGYP ILGTAVEDID RAEERGTFDR VLQELAAKRP RGGGATSMEQ VQTVAQEIGF
PLVVRPSYVL GGRAMDIVYE AKELETVVRR ALSASSDQEI WMDQYLLGKE VEVDAISDGE
NVFIPGIMEH LERAGVHSGD SIAVYPPQTL DVSMQERIIT LTESLARSLK IKGLLNIQYV
IYQNELFVLE VNPRSSRTVP FLSKVTGVPI VDWATQVILG RKWEEIKIPH GLYPTGDRVA
VKAPVFSFSK LQRVEPSLGP EMKSTGEVMG MDRTYEKALY KALLGAGLSF TTYGSVFVTL
ADRDKAEGVA LARRFAELGF RLLATEGTTR YLKNEGLRVE QLAKLHDGSN EIIDGIRKQQ
IQYVVNTTTH GRIQESDGFA IRRAAVEHGI PCFTSLDTAA ALLQVLESIS PGLMPL
//
