ID A0A099BYX4_9BACT Unreviewed; 1074 AA.
AC A0A099BYX4;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Carbamoyl phosphate synthase large subunit {ECO:0000313|EMBL:KGI61471.1};
GN ORFNames=HMPREF0671_00370 {ECO:0000313|EMBL:KGI61471.1};
OS Prevotella sp. S7 MS 2.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1287488 {ECO:0000313|EMBL:KGI61471.1, ECO:0000313|Proteomes:UP000029732};
RN [1] {ECO:0000313|EMBL:KGI61471.1, ECO:0000313|Proteomes:UP000029732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S7 MS 2 {ECO:0000313|EMBL:KGI61471.1,
RC ECO:0000313|Proteomes:UP000029732};
RA McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (JUL-2014) 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 -!- 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:KGI61471.1}.
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DR EMBL; JRPT01000001; KGI61471.1; -; Genomic_DNA.
DR RefSeq; WP_036895889.1; NZ_JRPT01000001.1.
DR AlphaFoldDB; A0A099BYX4; -.
DR eggNOG; COG0458; Bacteria.
DR Proteomes; UP000029732; 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 CDD; cd01423; MGS_CPS_I_III; 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; 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.
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 Reference proteome {ECO:0000313|Proteomes:UP000029732};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 132..324
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 680..871
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 937..1074
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 1074 AA; 119621 MW; 8EC86B68DB1E5BEE CRC64;
MKDEKIKKVL LLGSGALKIG EAGEFDYSGS QALKAMREEG IYTVLINPNI ATVQTSEGVA
DQIYFLPVQP YFVERVIEKE RPDGILLSFG GQTALNCGVE LYKSGILEKY NVQVLGTPVQ
AIMDTEDREL FVEKLDEIDV KTIKSEACDN IEKTRKAARE LGYPVIIRAA YALGGLGSGF
ADNEEELDKL AEKAFSFSPQ VLVEKSLKGW KEIEYEVVRD RFDNCITVCN MENFDPLGIH
TGESIVIAPS QTLTNSEYHK LRALAIRIIR HIGIVGECNV QYAFDPKSED YRVIEVNARL
SRSSALASKA TGYPLAFVAA KLGLGYGLFD LKNSVTKTTS AFFEPALDYV VCKIPRWDLS
KFRGVDKELG SSMKSVGEVM AIGRNFEEAI QKGLRMIGQG MHGFVENKEL EIEDIDAALK
EPTDKRIFVI SKAMHKAYTV DQIHELTKID KWFLQKLKNI IDIDEQLKTC NINTLDKELL
QKAKVYGFTD FQIARAVGLE GELHNMFKAQ LLVRNLRKNY GILPVVKQID TLAAEYPAQT
NYLYLTYAGV QNDIDFEKDK RSIIVLGSGA YRIGSSVEFD WCGVQALNTI RKEGYRSVMI
NYNPETVSTD YDMCDRLYFD ELTFERVMDI IELETPHGVI VSTGGQIPNN LAMKLDEQNV
PILGTAAQDI DGAEDRAKFS AMLTRNGINQ PEWSALTSMD DIGKFVERVG FPVLVRPSYV
LSGAAMNVCS NEEELVKFLQ LAANVSEDHP VVVSKFIEHA KEIEMDAVAR NGEILAYAIS
EHVEFAGVHS GDATIAFPPQ KLYVETVRRV KHVSRQIAKE LHISGPFNIQ FMARDNDILV
IECNLRASRS FPFVSKVLKI NLIELATKVM LGLPVEKPNK NLFDLDYVGI KASQFSFSRL
QKADPVLGVD MSSTGEVGCL GDDTNDALLK SMLSVGHRIP AKTVLLSTGG AKEKAGMLDA
ARELVEHGYK LYATGGTSKY LAENGVANER VFWPSEEGQE PQALTMLHEH KIDMVVNIPK
NLTVHELTNG YKIRRAAIDL NVPLITNSRL ASAFIHAFCS VPLDEIEIKS WSEY
//
