ID Q8AAA8_BACTN Unreviewed; 1075 AA.
AC Q8AAA8;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 162.
DE SubName: Full=Carbamyl phosphate synthetase {ECO:0000313|EMBL:AAO75664.1};
GN OrderedLocusNames=BT_0557 {ECO:0000313|EMBL:AAO75664.1};
OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=226186 {ECO:0000313|EMBL:AAO75664.1, ECO:0000313|Proteomes:UP000001414};
RN [1] {ECO:0000313|EMBL:AAO75664.1, ECO:0000313|Proteomes:UP000001414}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50 {ECO:0000313|Proteomes:UP000001414};
RX PubMed=12663928; DOI=10.1126/science.1080029;
RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA Hooper L.V., Gordon J.I.;
RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL Science 299:2074-2076(2003).
RN [2] {ECO:0000313|EMBL:AAO75664.1, ECO:0000313|Proteomes:UP000001414}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50 {ECO:0000313|Proteomes:UP000001414};
RX PubMed=19321416; DOI=10.1073/pnas.0901529106;
RA Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S.,
RA Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L.,
RA Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C.,
RA Hettich R.L., Gordon J.I.;
RT "Characterizing a model human gut microbiota composed of members of its two
RT dominant bacterial phyla.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009).
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}.
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DR EMBL; AE015928; AAO75664.1; -; Genomic_DNA.
DR RefSeq; NP_809470.1; NC_004663.1.
DR RefSeq; WP_011107320.1; NZ_UYXG01000009.1.
DR AlphaFoldDB; Q8AAA8; -.
DR STRING; 226186.BT_0557; -.
DR PaxDb; 226186-BT_0557; -.
DR EnsemblBacteria; AAO75664; AAO75664; BT_0557.
DR GeneID; 60926514; -.
DR KEGG; bth:BT_0557; -.
DR PATRIC; fig|226186.12.peg.557; -.
DR eggNOG; COG0458; Bacteria.
DR HOGENOM; CLU_000513_1_3_10; -.
DR InParanoid; Q8AAA8; -.
DR OrthoDB; 9804197at2; -.
DR Proteomes; UP000001414; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0006541; P:glutamine metabolic process; IBA:GO_Central.
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:UP000001414};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 131..323
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; 119808 MW; E108B4D0044CF3EF CRC64;
MKENIKKVLL LGSGALKIGE AGEFDYSGSQ ALKALKEEGI ETILINPNIA TVQTSEGVAD
QIYFLPVTPY FVEKVIQKEK PEGIMLAFGG QTALNCGVAL YKEGILEKYN VKVLGTPVQA
IMDTEDRELF VQKLNEINVK TIKSEAVENA EDARRAAKEL GYPVIVRAAY ALGGLGSGFC
DNEEQLDVLV EKAFSFSPQV LVEKSLRGWK EVEYEVVRDR FDNCITVCNM ENFDPLGIHT
GESIVIAPSQ TLTNSEYHKL RELAIRIIRH IGIVGECNVQ YAFDPESEDY RVIEVNARLS
RSSALASKAT GYPLAFVAAK LGLGYGLFDL KNSVTKTTSA FFEPALDYVV CKIPRWDLGK
FHGVDKELGS SMKSVGEVMA IGRTFEEAIQ KGLRMIGQGM HGFVENKELV IPDIDKALRE
PTDKRIFVIS KAFRAGYTID QVHELTKIDK WFLQKLMNIM KTSEEMHEWG NNHKQIADLP
VELLRKAKVQ GFSDFQIARA IGYEGDMENG SLYVRKYRKA AGILPVVKQI DTLAAEYPAQ
TNYLYLTYSG VANDVHYLGD HKSIVVLGSG AYRIGSSVEF DWCGVQALNT IRKEGWRSVM
INYNPETVST DYDMCDRLYF DELTFERVMD ILELENPHGV IVSTGGQIPN NLALRLDAQN
IHILGTSAQS IDNAEDREKF SAMLDRIGVD QPRWRELTSL EDINEFVDEV GFPVLVRPSY
VLSGAAMNVC SNQEELERFL KLAANVSKKH PVVVSQFIEH AKEVEMDAVA QNGEIIAYAI
SEHIEFAGVH SGDATIQFPP QKLYVETVRR IKRISREIAK ALNISGPFNI QYLAKDNDIK
VIECNLRASR SFPFVSKVLK INFIELATKV MLGLPVEKPE KNLFELDYVG IKASQFSFNR
LQKADPVLGV DMASTGEVGC IGSDTSCAVL KAMLSVGYRI PKKNILLSTG TMKQKADMMD
AARMLVNKGY KLFATGGTHK TFAENGIEST LVYWPSEEGH PQALEMLHNK EIDMVVNIPK
NLTAGELDNG YKIRRAAIDL NVPLITNARL ASAFINAFCT MTVDDIAIKS WEEYK
//
