ID R7J559_9BACT Unreviewed; 1075 AA.
AC R7J559;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Carbamoyl-phosphate synthase large subunit {ECO:0000313|EMBL:CDE58037.1};
GN ORFNames=BN799_00118 {ECO:0000313|EMBL:CDE58037.1};
OS Prevotella sp. CAG:873.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1262936 {ECO:0000313|EMBL:CDE58037.1, ECO:0000313|Proteomes:UP000018078};
RN [1] {ECO:0000313|EMBL:CDE58037.1, ECO:0000313|Proteomes:UP000018078}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:873 {ECO:0000313|Proteomes:UP000018078};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CDE58037.1}.
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DR EMBL; CBJF010000188; CDE58037.1; -; Genomic_DNA.
DR AlphaFoldDB; R7J559; -.
DR Proteomes; UP000018078; 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:UP000018078};
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; 119427 MW; EBB08FDFA20CDCA2 CRC64;
MTANKTIRKV LLLGSGALKI GEAGEFDYSG SQALKAMKEE GISTVLINPN IATVQTSEGF
ADKIYFLPVT PYFVAKVIEK ERPDGILLAF GGQTALNCGV ELYRDGVFER YGVQVLGTPV
QAIIDTEDRE LFVKRLDEIG VKTIRSSAAD SVAQALDVAS ELGYPVIVRA AYALGGLGSG
FCDNAEELRT LAEKALSFAP QVLIEKSLKG WKEVEYEVVR DRYDNCITVC NMENFDPLGI
HTGESIVVAP SQTLSNDDYH YLRSLAIKII RHVGIVGECN VQYAYDPDSM DYRVIEVNAR
LSRSSALASK ATGYPLAFVA AKLGLGYGLF ELRNSVTHDT SAFFEPALDY VVVKIPRWDL
GKFHGVNREI GSSMKSVGEV MAIGRTFEEA IQKGLRMIGQ GMHGFVENKD IKIDDIDHAL
AEPTDRRIFV IAKAMARGYD VERIHALTKI DRWFLYKLRA IMDTADELGA YNQPEDLPED
LLRMAKQQGF SDFQIARSVY KDDMSHAHES VLEVRRLRKR LGIVPCVKQI DTLAAEYPAS
TNYLYLTYNG TENDVAYRHD RRSIIVLGSG AYRIGSSVEF DWCSVNALRS VKQQGWRSVM
INYNPETVST DYDMCDRLYF DELTFERVMD IIDLEQPHGV ILSVGGQIPN NLATRLDGEG
VKILGTPARD IDNAEDRHKF SAMLDSLGID QPRWRELTDM QSINSFIEEV GFPVLVRPSY
VLSGAAMNVC SNNDELERFL RLAADVSKEH PVVVTQFIQD AKEIEMDAVA RDGEIIVYAI
SEHIEFAGVH SGDATIQFPP QKIYVETVRR IKKVSQQIAR ALHITGPFNI QYLAKNNDIK
VIECNLRASR SFPFVSKVLK INFIDLATKA MLGLDVQRPA KSAFDLDYVG IKASQFSFSR
LQGADPVLGV DMSSTGEVGC LGDDTGEALL TAMISVGQRV PRRSVLLSTG TPRQKADMLD
AAHILHSHGF TIYATGGTHA FLNDNGIPAI RVYWPSQPDM HPQALELLHD HKIDMVVNIP
KNLSTTELSN GYKIRRAAVD LNVPLITNAR LASAYINAFT SIPVDDIEIK SWDEY
//
