ID A0A161LG92_9BACT Unreviewed; 1084 AA.
AC A0A161LG92;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Carbamoyl-phosphate synthase large subunit {ECO:0000313|EMBL:GAT63857.1};
GN ORFNames=PJIAN_4399 {ECO:0000313|EMBL:GAT63857.1};
OS Paludibacter jiangxiensis.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Paludibacteraceae;
OC Paludibacter.
OX NCBI_TaxID=681398 {ECO:0000313|EMBL:GAT63857.1, ECO:0000313|Proteomes:UP000076586};
RN [1] {ECO:0000313|Proteomes:UP000076586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NM7 {ECO:0000313|Proteomes:UP000076586};
RA Qiu Y., Matsuura N., Ohashi A., Tourlousse M.D., Sekiguchi Y.;
RT "Draft genome sequence of Paludibacter jiangxiensis strain NM7.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000076586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NM7 {ECO:0000313|Proteomes:UP000076586};
RA Qiu Y.-L., Tourlousse D.M., Matsuura N., Ohashi A., Sekiguchi Y.;
RT "Draft genome sequence of Paludibacter jiangxiensis NM7(T), a propionate-
RT producing fermentative bacterium.";
RL Genome Announc. 0:0-0(2017).
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:GAT63857.1}.
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DR EMBL; BDCR01000004; GAT63857.1; -; Genomic_DNA.
DR RefSeq; WP_068705431.1; NZ_BDCR01000004.1.
DR AlphaFoldDB; A0A161LG92; -.
DR STRING; 681398.PJIAN_4399; -.
DR OrthoDB; 9804197at2; -.
DR Proteomes; UP000076586; 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:UP000076586};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 143..335
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 690..881
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 947..1084
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 1084 AA; 120708 MW; E237C5D38A21692F CRC64;
MNIKDDFLST DNTRLSIKKV LILGSGALKI GEAGEFDYSG SQALKALKEE GIETVLINPN
IATVQTSEGV ADKIYFLPIT PFFVEKVIKK EQPDGLLLAF GGQTALNCGV KLFESGILEK
YNLRVLGTPV QAIIDTEDRE LFVKKLDQID VKTIKSFAVE NMADAKTAAK DLGYPIIVRA
AYALGGLGSG FCNNEQELEA LAEKAFNYSS QLLVEKSLKG WKEIEYEVVR DRYDNCITVC
NMENFDPLGI HTGESIVVAP SQTLTNSEYH KLREIAIRIV RHIGIVGECN VQYAFDPDSE
DYRVIEVNAR LSRSSALASK ATGYPLAFVA AKLALGYGLF ELKNSVTKTT TAFFEPALDY
VVCKIPRWDL AKFHGVSREI GSSMKSVGEV MAIGRTFEEA LQKGLRMIQQ GMHGFVANKT
LSISDMNKAL SEPTDRRIFY LSQALQSGYT IEQIHNLTKI DNWFLQKLQN IVDVAKDLKL
TESFNDLSDD LLLRAKQMGF SDFQIARLMF DIHENKARIG DEVRAERKRR GILPVVKQID
TLAAEYPAQT NYLYITYNGS ANDVKYLGDH RSVVVLGSGA YRIGSSVEFD WCSVNALNTI
RKQGLRSVMI NYNPETVSTD YDMCDRLYFD ELTYERVMDI LELENPMGTI VSVGGQIPNN
LAVRMSDSGV NILGTKAPSI DNAEDRHKFS SMLDDLKIDQ PRWQELRSLN DITEFVKNVG
FPVLVRPSYV LSGAAMNVCS NQEELEEFLE LATEVSQEHP VVVSEFIENA KEIEIDAVAN
NGDIVIYAIS EHVEFAGVHS GDATIQFPPQ KIYVETVRRI KQIARQIAKS LNISGPFNIQ
FLAKDNDIKV IECNLRASRS FPFVSKVLKI NFIDLATQVM LGLNPAKPEK SAFDLDYVGI
KASQFSFTRL QKADPVLGVD MASTGEVGCI GHQFDDALLT AMLSVGYRIP EKTVMVSSGE
SKSKVAMLDA CLLLSKNGYT IYATHGTQQF LQQNGVDAID VNWPDEDGEH NVMQMIADKK
FDLVINIPKN LTKRELSNGY KIRRGAIDFN IPLITNARLA SAFIKAFCKI TADDIDIRDW
AGYK
//
