ID A0A1M5X469_BUTFI Unreviewed; 1073 AA.
AC A0A1M5X469;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Carbamoyl-phosphate synthase large subunit {ECO:0000313|EMBL:SHH94402.1};
GN ORFNames=SAMN02745229_01268 {ECO:0000313|EMBL:SHH94402.1};
OS Butyrivibrio fibrisolvens DSM 3071.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Butyrivibrio.
OX NCBI_TaxID=1121131 {ECO:0000313|EMBL:SHH94402.1, ECO:0000313|Proteomes:UP000184278};
RN [1] {ECO:0000313|EMBL:SHH94402.1, ECO:0000313|Proteomes:UP000184278}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3071 {ECO:0000313|EMBL:SHH94402.1,
RC ECO:0000313|Proteomes:UP000184278};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; FQXK01000009; SHH94402.1; -; Genomic_DNA.
DR RefSeq; WP_073386391.1; NZ_FQXK01000009.1.
DR AlphaFoldDB; A0A1M5X469; -.
DR STRING; 1121131.SAMN02745229_01268; -.
DR GeneID; 40456873; -.
DR OrthoDB; 9804197at2; -.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000184278; 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; -; 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; 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; 2.
DR PROSITE; PS50975; ATP_GRASP; 2.
DR PROSITE; PS00866; CPSASE_1; 2.
DR PROSITE; PS00867; CPSASE_2; 2.
DR PROSITE; PS51855; MGS; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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}; Ligase {ECO:0000256|ARBA:ARBA00022598};
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 132..326
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 672..863
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 933..1073
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 1073 AA; 118495 MW; 59ABBB23672E07B6 CRC64;
MKREDIHRIL IIGSGPIIIG QACEFDYSGT QACKALRKLG YEIILVNSNP ATIMTDPETA
DVTYIEPLNV KRLTQIIEKE RPDALLPNLG GQSGLNLASE LAEAGVLEKY GVKVIGVQID
AIERGEDRIE FKKTMDELGI EMARSQVAYS VDEAVEIAAR LGYPVVLRPA YTMGGSGGGL
VYNVEELKTV CARGLQASMV HQVLVEESVI GWEELELEVV RDSKGQMITV CFIENIDPMG
VHTGDSFCSA PMLTISQEVQ DRLQEQAYKI VDKVQVIGGC NCQFAHDPKT DRIIVIEINP
RTSRSSALAS KATGFPIALV SAMLACGLDL DDIECGKYGT LDKYVPGGDY IVIKFARWAF
EKFKGVEDHL GTQMRAVGEV MSIGKTYKEA FQKAIRSLEK SRYGLGFVKD FNEKSLDELY
AMLVTPTSER QFIMYEALRK GADIDRLYEL TKIKRYFIEQ MKELVEEEEE IIKSSNGKVP
EIAVLEKAKK DGFSDKYLSQ ICHVSEDEIR NARENAGITE CWEGIHVSGT KDSAYYFSSY
NIKDNNPVKE DKPKVMILGG GPNRIGQGIE FDYCCVHAAF ALKKLGFETV IVNCNPETVS
TDYDTSDKLY FEPLTLEDVL SIYKKEKPVG VIAQFGGQTP LNLASDLKKN GVNILGTSPE
TIDMAEDRDL FRDMMDRLGI PMAESGMASN VEEAKEIAGR IGYPVMVRPS YVLGGRGMEV
VHSDEQMNIY MAQAVGVTPD RPILIDRFLN HAIECEADAI SDGENVFVPA VMEHIELAGI
HSGDSACVLP SKHLSDNIVA TIKDYTKRIA KEMHVVGLMN MQYAIENNVV YVLEANPRAS
RTVPLVSKVC DINMVKEATN IMTLPITGGK SPVGDLRDRK IPYYGVKEAV FPFNMFPEVD
PVLGPEMRST GEALGLSEDW GRAFFKAQEG TKTELPTEGT VLISVNDRDK PELVEIAQKY
YNDGFNILAT GRTYEMIIEA GIPAKRINKI FEGRPDIVDA ITNGEIDLIV DTPTDKKGDV
SDAYIRKNAI KHHIPYITTM AAARASAEGI GAEKLGEGTP VRSLQEYHAS IVG
//
