ID A0A1H8A1T0_9BACT Unreviewed; 1086 AA.
AC A0A1H8A1T0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Carbamoyl-phosphate synthase large subunit {ECO:0000313|EMBL:SEM63864.1};
GN ORFNames=SAMN04487902_102104 {ECO:0000313|EMBL:SEM63864.1};
OS Prevotella sp. ne3005.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1761887 {ECO:0000313|EMBL:SEM63864.1, ECO:0000313|Proteomes:UP000199132};
RN [1] {ECO:0000313|Proteomes:UP000199132}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NE3005 {ECO:0000313|Proteomes:UP000199132};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOCK01000002; SEM63864.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8A1T0; -.
DR STRING; 1761887.SAMN04487902_102104; -.
DR OrthoDB; 9804197at2; -.
DR Proteomes; UP000199132; 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:UP000199132};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 131..323
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 691..882
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 948..1086
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 1086 AA; 120702 MW; 985E3DB8FB1633F0 CRC64;
MKKELKKVLV LGSGALKIGQ AGEFDYSGSQ ALKALREEGI KSVLVNPNIA TIQTSEGIAD
KVYFQPVNTH FVTEIIKKER PDGILLAFGG QTALNCGTEL YLNGTLKEYG VEVLGTSVEA
IMNTEDRDLF VKKLAEVQLK VPVSHAVESM EDALKAAHEI GFPIMIRSAY ALGGLGSGIC
PDEKKFIELA ESAFTFAPQI LVEESLKGWK EIEFECIRDA NDRCFTVASM ENFDPLGIHT
GESIVVAPTC SLKEEQVKML QEITIKCVKH LGIVGECNIQ FAFNAETNDY RIIEINARLS
RSSALASKAT GYPLAFVAAK IALGYTLDQI GEMGTTSSAY VAPSLDYMIC KIPRWDLTKF
AGVSRQIGSS MKSVGEIMSI GRSFEEMIQK GLRMIGQGMH GFVGNDHTKF DNLDEELANP
TDLRIFAIAQ ALEEGYTIER IEQLTKIDVW FLERLKHIVD LKHELLKYNT LEELPDELLL
EVKRCGFSDF QIARFVLKSK GSNMEKENLE VRKYRKQKGI LPSVKRIPTV ASENPELTNY
LYFTYTHTPA FGNPEGEKYE AAHDVNYYSH EKSVVVLGSG AYRIGSSVEF DWCSVNAINT
ARKLGYKSIM INYNPETVST DYDMCDRLYF DELSLERVLD VIDLESPRGV IVSVGGQIPN
NLAMKLYRQG VPVLGTSPVN IDRAENRDKF SAMLDKLCID QPAWQALTSF DDVKEFVAKV
GYPVLVRPSY VLSGAAMNVC YDEEELHRFL NMATEVSKEF PVVVSKFMTE TKEIEFDAVA
DKGEVIEYAI SEHVEYAGVH SGDATMVFPA QHIYFSTIRQ IKKIARKIAA ELNISGPFNI
QFLAKNREVK VIECNLRASR SFPFVSKILK RNFIETATKI MLDAPYQKPE RSEFDIDRIG
VKASQFSFAR LQNADPVLGV DMSSTGEVGC LGDDLNEAML NALIATGYSI PKDAVLISSG
GAKGKVSLLE PAQQLAKKGY TIYATAGTAK FFNDNGVKAV TVAWPDEDGD NNVMDLISQH
KVGLVINVPK NHSSRELTNG YKIRRGAIDH NIPLMTNVRL AKAFIEAFTA MNLEDVKIKS
WQEYNS
//
