ID R6NRT8_9FIRM Unreviewed; 1072 AA.
AC R6NRT8;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Carbamoyl-phosphate synthase large subunit {ECO:0000313|EMBL:CDC11094.1};
GN ORFNames=BN627_00888 {ECO:0000313|EMBL:CDC11094.1};
OS Lachnospiraceae bacterium CAG:364.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1262983 {ECO:0000313|EMBL:CDC11094.1, ECO:0000313|Proteomes:UP000017986};
RN [1] {ECO:0000313|EMBL:CDC11094.1, ECO:0000313|Proteomes:UP000017986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:364 {ECO:0000313|Proteomes:UP000017986};
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 -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl
CC phosphate from bicarbonate: step 1/1. {ECO:0000256|ARBA:ARBA00005077}.
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:CDC11094.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CBER010000155; CDC11094.1; -; Genomic_DNA.
DR AlphaFoldDB; R6NRT8; -.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000017986; 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:UniProtKB-KW.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:UniProt.
DR CDD; cd01424; MGS_CPS_II; 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; IPR033937; MGS_CPS_CarB.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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:UP000017986};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 133..327
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 672..863
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 933..1072
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 1072 AA; 118245 MW; 0920D031EB5FBB0B CRC64;
MPKRNDIHKI LIIGSGPIII GQACEFDYSG TQACKALRNL GYEIVLVNSN PATIMTDPST
ADVTYIEPLN VDRLTEIIAK ERPDALLPNL GGQSGLNLCE ELYHAGVLDK YNVEVIGVQV
DAISRGEDRI EFKNAMDKLG IEMAKSAPAY SVEEALKIAE ELGYPCVIRP AYTMGGTGGG
IVYNEEELKK VAARGIAASM VNQILVEESV IGWEELEVEV VRDKAGKKIS ICFIENIDPM
GVHTGDSFCS APMLTISQDL QDRLEKQAHA IVESIGVIGG TNVQFAHDPK SDRIIIIEIN
PRTSRSSALA SKATGFPIAY VSALLAAGLT LDEIPYWKDG SLANYKPSGD YVVVKFARWA
FEKFKSSQDK LGTQMKAVGE VMSIGKTYKE ALQKAIRSLE RGCYGLGFVK DFHELTLDEL
YAKLEKPTSQ RQFILYEAIR KGASLEKLHD MTHIKLWFLQ QMKELVDLEE EILTYKGKSL
PDELLIQAKK DGFSDKYLAM LLDIDEWELF KHRESLGMGE RWDAVPVSGV EEPAAYYYST
YNGEDKAPVS NGRKVMVLGG GPNRIGQGIE FDYCCVHAAF TLRELGFETI MVNCNPETVS
TDYDTSDKLY FEPLTVEDVM SIYNKEKPLG IIVQFGGQTP LNIAAELEKR GAHILGTSPA
VIDMAEDRDL FNAMMHKLEI PMPESGMAVN VEEALEIAHR IGYPMMVRPS YVLGGRGMEV
VYDDNMLRDY MAAAIDVTPE RPILMDKFLQ NALECETDAI SDGTHAFVPT VMQHIEQAGI
HSGDSACVIP SVEISEKNKE LIRKYTTAIA CEMGVVGLMN MQYAICEDKV YVLEANPRAS
RTVPLVSKVC NINMANIATK LMTYELTNER PDVTAFKEKA HPYYGVKEAV FPFNMFPEVD
PLLGPEMRST GEVLGLSESF GTAYYKAQEA AGAKLPLSGT ALISVNKNDR AQALEAAKQF
KELGFGIVST EGCAKFFNEN GVECKTLKKL QEGSPNVYDA LVSGEIDLVI NTPAGKQSKY
DDSYLRKTAI NKKIPYITTM SAALASATGV KAILNKEAQS LKSLQEYHKT LD
//
