ID A0A0A2ES02_PORCN Unreviewed; 1073 AA.
AC A0A0A2ES02;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Carbamoyl phosphate synthase large subunit {ECO:0000313|EMBL:KGN81698.1};
GN ORFNames=HQ35_03965 {ECO:0000313|EMBL:KGN81698.1};
OS Porphyromonas cangingivalis.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=36874 {ECO:0000313|EMBL:KGN81698.1, ECO:0000313|Proteomes:UP000030125};
RN [1] {ECO:0000313|EMBL:KGN81698.1, ECO:0000313|Proteomes:UP000030125}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COT-109 OH1386 {ECO:0000313|Proteomes:UP000030125};
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 cangingivalis strain:COT-109_OH1386 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:KGN81698.1}.
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DR EMBL; JQJD01000024; KGN81698.1; -; Genomic_DNA.
DR RefSeq; WP_036851236.1; NZ_JQJD01000024.1.
DR AlphaFoldDB; A0A0A2ES02; -.
DR STRING; 36874.HQ34_03580; -.
DR eggNOG; COG0458; Bacteria.
DR OrthoDB; 9804197at2; -.
DR Proteomes; UP000030125; 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:UP000030125};
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..1073
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 1073 AA; 119076 MW; DFF565D6DB2D4649 CRC64;
MAIKKYNKVL VLGSGALKIG EAGEFDYSGS QALKALKEEG ISTVLVNPNI ATVQTSEGVA
DVVYFLPVTP YFLERVIEKE RPDGILLAFG GQTALNCGVA LHRAGVLEKY NIEVLGTPVQ
AIIDTEDREL FVQKLDEIDV KTISSEACEN IEAARAAAKR LGYPVIIRAA YALGGLGSGF
CDNEEELDVL CEKAFAFSPQ VLVEKSLKGW KEIEYEVVRD KYNNCITVCN MENFDPLGIH
TGESIVIAPS QTLTNSEHQK LREIAIKIVR HIGIVGECNV QYALDTESED YRVIEVNARL
SRSSALASKA TGYPLAFVAA KLGMGYGLFD LKNSVTKHTS ACFEPALDYV VCKIPRWDLS
KFHGVSRELG SSMKSVGEIM AIGRTFEESI QKGLRMIGQG MHGFVENKEL VLDDIDGALR
QPTDNRIFVI SKAFRKGYTI EDIHQLTKID LFFLRKLRKI VDTAEELEQL TDITQVSKDL
MKRAKKEGFS DFQIARAIYK HTIDDIEGVQ DKVRTYRKSM GIVPVIKQID TLAAEYPALT
NYLYLTYGGD VHDVQPEHDN RSVIVLGSGA YRIGSSVEFD WCGVSALKTI RKAGLRSIMI
NYNPETVSTD YDLSDRLYFD ELSFERVQDI IELEQPRGTI LSTGGQIPNN LAVKLAAKGV
TILGTQAKDI DNAEDRHKFS AMLDRLGIDQ PAWKELTSLE DVTAFVEQVG YPVLVRPSYV
LSGAAMNVCS NDDELRRFLE LAANVSQKHP VVVSSFIEHA KEVEMDAVAD HGELIAYAIS
EHIEFAGVHS GDATIQFPAQ KIYIETIRRI KRITRQIAKE LHISGPFNIQ FLAKGNEIKV
IECNLRASRS FPFVSKVLKI DLIDLATKIM LREPYERPQK NAFDLDYVGI KASQFSFSRL
QKADPVLGVD MTSTGEVGCI ASDSNEAILK AMLSVGQRIP EKAILMSTGG ARQKVDMLEA
AKALHRKGYK IYATQGTHAF LDENGIPSKV CYWPSEHGQP QALDLLQSRE VDLVVNINKN
LSAGELTNGY KLRRAATDLN IPLITNARLA SAFITAFCKL SLEDIQIKSW QEY
//
