ID A0A0A2G6Y3_9PORP Unreviewed; 1075 AA.
AC A0A0A2G6Y3;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Carbamoyl phosphate synthase large subunit {ECO:0000313|EMBL:KGN98996.1};
GN ORFNames=HQ36_00480 {ECO:0000313|EMBL:KGN98996.1};
OS Porphyromonas gingivicanis.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=266762 {ECO:0000313|EMBL:KGN98996.1, ECO:0000313|Proteomes:UP000030134};
RN [1] {ECO:0000313|EMBL:KGN98996.1, ECO:0000313|Proteomes:UP000030134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COT-022 OH1391 {ECO:0000313|Proteomes:UP000030134};
RA Wallis C., Deusch O., O'Flynn C., Davis I., Jospin G., Darling A.E.,
RA Coil D.A., Alexiev A., Horsfall A., Kirkwood N., Harris S., Eisen J.A.;
RT "Porphyromonas gingivicanis strain:COT-022_OH1391 Genome sequencing.";
RL Submitted (AUG-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:KGN98996.1}.
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DR EMBL; JQZW01000002; KGN98996.1; -; Genomic_DNA.
DR RefSeq; WP_036882622.1; NZ_JQZW01000002.1.
DR AlphaFoldDB; A0A0A2G6Y3; -.
DR STRING; 266762.HQ36_00480; -.
DR eggNOG; COG0458; Bacteria.
DR OrthoDB; 9804197at2; -.
DR Proteomes; UP000030134; 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:UP000030134};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 133..325
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 681..872
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 938..1075
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 1075 AA; 119789 MW; A4A8D9E2B3A120A3 CRC64;
MIDRKEMKKV LVLGSGALKI GEAGEFDYSG SQALKAIREE GIRTILINPN IATVQTSHEV
ADEVYFLPVT PFFVEKVIAK ERPDGILLAF GGQTALNCGV ALYRSGILER YNVAVLGTPV
ETIIATEDRE LFVDKLNEIN VKTIASEAVE SIEAARLAAA RLGYPVIIRA AYALGGLGSG
FCDNEAELNA LCEKAFSFSP QVLVEKSLRG WKEIEYEVVR DAYDNCITVC NMENFDPLGI
HTGESIVVAP SQTLTNGEYH KLRELAIRII RHLGIVGECN VQYALDPVSE DYRVIEVNAR
LSRSSALASK ATGYPLAFVA AKLGLGYGLF EIKNAVTRNT PAFFEPSLDY CVCKIPRWDL
GKFQGVSRQL GSSMKSVGEV MAIGRTFEEA IQKGLRMIGQ GMHGFCENKD LVIKNLDQAL
REPTDTRIFV ISKAFRQGYS VEEIHDLTRI DKWFLHRLRN ILDTAELLEQ HNSADTLSAD
LIRRAKQQGF SDFQIARAVF KYTREDLEDA SLEIRKMRQE MGILPVVKQI DTLAAEYPAQ
TNYLYLTYNG VEHDIAYTNE KPAVVVLGSG AYRIGSSVEF DWCGVNALNT IRREGYHSVM
INYNPETVST DYDESDRLYF DELTFERVMD ILELETPKGV ILSTGGQIPN NLAVRLDQQN
VNILGTTAKS IDNAEDRHKF SAMLDHLGID QPAWRELSSL EDINQFVSEV GFPVLVRPSY
VLSGAAMNVC SNHSELERFL QLAANVSQKH PVVVSQFIEH AKEVEMDAVA RNGEIIAYAI
SEHIEFAGVH SGDATIQFPA QKLYVETVRR IKRISRQIAE ALNISGPFNI QFLAKDNDIK
VIECNLRASR SFPFVSKVLK INFIDLATRI MLGLPVEKPE KNAFDLDYVG IKASQFSFTR
LQKADPVLGV DMTSTGEVGC IADDTDEAIL KSMLSVGHRI PKKNVLLSTG GYKQKVDMMD
SCRLLTQKGY TIYATEGTHK FLQDNGIPSI RVYWPDEEGK PQAVSLLQDH TIDLVVNINK
NLSQGELTNG YKLRRSAIDL NIPLITNARL ASAFIIAFCR LSADDIQIKP WSEYK
//
