ID C9MKP4_9BACT Unreviewed; 1074 AA.
AC C9MKP4;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Carbamoyl-phosphate synthase, large subunit {ECO:0000313|EMBL:EEX19849.1};
DE EC=6.3.5.5 {ECO:0000313|EMBL:EEX19849.1};
GN Name=carB {ECO:0000313|EMBL:EEX19849.1};
GN ORFNames=HMPREF0973_00168 {ECO:0000313|EMBL:EEX19849.1};
OS Prevotella veroralis F0319.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=649761 {ECO:0000313|EMBL:EEX19849.1, ECO:0000313|Proteomes:UP000003327};
RN [1] {ECO:0000313|EMBL:EEX19849.1, ECO:0000313|Proteomes:UP000003327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0319 {ECO:0000313|EMBL:EEX19849.1,
RC ECO:0000313|Proteomes:UP000003327};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2009) 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:EEX19849.1}.
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DR EMBL; ACVA01000007; EEX19849.1; -; Genomic_DNA.
DR RefSeq; WP_004381765.1; NZ_GG698712.1.
DR AlphaFoldDB; C9MKP4; -.
DR STRING; 649761.HMPREF0973_00168; -.
DR eggNOG; COG0458; Bacteria.
DR HOGENOM; CLU_000513_1_0_10; -.
DR OrthoDB; 9804197at2; -.
DR Proteomes; UP000003327; 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};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EEX19849.1};
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:UP000003327};
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; 119654 MW; 71C3F17C59E87A91 CRC64;
MKDDSIKKVL LLGSGALKIG EAGEFDYSGS QALKALREEG VSTVLINPNI ATVQTSEGVA
DQIYFLPVQP YFVERVIEKE RPDGILLSFG GQTALNCGVE LERTGVLKKY NVRVLGTPVA
AIMNTEDREL FVERLDEIDV KTIKSEACED IVQARKAAKT LGYPVIVRAA YALGGLGSGF
ADNEEELNTL CEKAFSFSPQ VLVEKSLKGW KEIEYEVVRD QYDNCITVCN MENFDPLGIH
TGESIVIAPS QTLTNSEYHK LRALSIKIVR HIGIIGECNV QYAFDPQSED YRVIEVNARL
SRSSALASKA TGYPLAFVAA KLGMGYGLFE LKNSVTKTTS AFFEPALDYV VCKIPRWDLS
KFRGVDKELG SSMKSVGEVM AIGRNFEEAI QKGLRMIGQG MHGFVENKEL QIEDIDAALR
EPTDKRVFII SKAMHKGYTV DQIHDLTKID KWFLNKLKHI IDIDEELKRK NINTLDKQLL
REAKVYGFTD FQIARAVGLE EECPNMHKAM MLVRRLRKGF GILPVVKQID TLAAEYPAQT
NYLYVTYAGV ASDVTFSNDR KSVIVLGSGA YRIGSSVEFD WCGVQALNTI RRHGYRSVMI
NYNPETVSTD YDMCDRLYFD ELTFERVMDI IDAETPHGVI VSTGGQIPNN LAMYLDEENV
PILGTAAKDI DNAEDRAKFS SMLTENGINQ PEWSALTSME DIDRFVDRVG FPVLVRPSYV
LSGAAMNVCS NKDELTRFLQ LAANVSEDHP VVVSKFIENA KEIEMDAVAK DGEIMAYAIS
EHIEFAGVHS GDATIQFPPQ KLYVETVRRI KRISRQIAKK LHINGPFNIQ YMARENDILV
IECNLRASRS FPFVSKVLKL NFIDLATKIM LGVPVEKPNK NLFDLDYVGI KASQFSFNRL
QKADPVLGVD MSSTGEVGCL GDDSATALLK SMLSVGQRIP KKTILLSTGG AKQKAEMLDA
AKTLKQHGYE LFATVGTSKY LTENGIENTL VYMPSDKEHS PQALDLLHEK KIDMVVNMPK
DLTPRELTNG YKIRRAAIDL NIPLITNSRL ASAFINAFCN VSLNDIDIKA WGEY
//
