ID D1W538_9BACT Unreviewed; 1076 AA.
AC D1W538;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Carbamoyl-phosphate synthase, large subunit {ECO:0000313|EMBL:EFA92351.1};
DE EC=6.3.5.5 {ECO:0000313|EMBL:EFA92351.1};
GN Name=carB {ECO:0000313|EMBL:EFA92351.1};
GN ORFNames=HMPREF0650_0815 {ECO:0000313|EMBL:EFA92351.1};
OS Hoylesella buccalis ATCC 35310.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Hoylesella.
OX NCBI_TaxID=679190 {ECO:0000313|EMBL:EFA92351.1, ECO:0000313|Proteomes:UP000005283};
RN [1] {ECO:0000313|EMBL:EFA92351.1, ECO:0000313|Proteomes:UP000005283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35310 {ECO:0000313|EMBL:EFA92351.1,
RC ECO:0000313|Proteomes:UP000005283};
RA Durkin A.S., Madupu R., Torralba M., Methe B., Sutton G., Strausberg R.L.,
RA Nelson K.E.;
RT "Genome Sequence of Prevotella buccalis ATCC 35310.";
RL Submitted (DEC-2009) 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:EFA92351.1}.
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DR EMBL; ADEG01000045; EFA92351.1; -; Genomic_DNA.
DR RefSeq; WP_004348949.1; NZ_ADEG01000045.1.
DR AlphaFoldDB; D1W538; -.
DR STRING; 679190.HMPREF0650_0815; -.
DR eggNOG; COG0458; Bacteria.
DR Proteomes; UP000005283; 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};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EFA92351.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 132..324
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..1076
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 1076 AA; 120268 MW; 08A0A8D0FAF3D251 CRC64;
MKDENIKKVL LLGSGALKIG EAGEFDYSGS QALKALRQEG VSTVLINPNI ATVQTSEGVA
DKIYFLPVQP YFVERVIQKE KPDGILLSFG GQTALNCGVE LYKSGILEKY HVRVLGTPVQ
AIIDTEDREL FVEKLREIDV KTIKSEACEN IEQARKAAKS LGYPVIIRAA YALGGLGSGF
CDNEEELNKL AEKSFSFSPQ VLVEKSLKGW KEIEYEVVRD RYDNCVTVCN MENFDPLGIH
TGESIVIAPS QTLSNSEYHK LRELSIRIIR HIGIIGECNV QYAFDPESEE YRVIEVNARL
SRSSALASKA TGYPLAFVAA KLGMGYGLFD LKNSVTKTTS AFFEPALDYV VCKIPRWDLS
KFRGVDKELG SSMKSVGEVM AIGRNFEEAI QKGLRMIGQG MHGFVENKEL EIENIDGALR
EPTDKRVFII SKAMHKGYTI DQIHELTKID KWFLQKLKHI IDIDEALKRC TSINVLDKEL
LRTAKVYGFT DFQIARAVGL EAEMANMHQA MLVVRKLRKT YGILPVVKQI DTLAAEYPAQ
TNYLYMTYAG VAHDVAFEKD KQSIIVLGSG AYRIGSSVEF DWCGVQALNT IRREGYRSVM
INYNPETVST DYDMCDRLYF DELTFERVMD IVELEMPHGV IVSTGGQIPN NLAMKLDEQH
VPILGTAAKD IDHAEDRAKF SSLLSQHGIN QPEWSALTSM DDINEFVDRV GFPVLVRPSY
VLSGAAMNVC SNKEELERFL KLAANVSEDH PVVVSKFIEN AKEIEMDAVA MKGEIMAYAI
SEHIEFAGVH SGDATIQFPP QKLYVETVRR IKRVSRQIVS ALHINGPFNI QFMARDNDIL
VIECNLRASR SFPFVSKVLK LNLIDLATKI MLGVPVEKPR KNLFDLDYVG IKASQFSFNR
LQKADPVLGV DMSSTGEVGC LGDDTNQALL KSMLSVGHRI PKHTVLLSTG GAKQKAEMLD
AAKMLKQHGY ELYATAGTSQ YLHENGIDNT MVYWPSDEAK EPQALTLLHE HKIDMVVNIP
KDLTPRELTN GYKIRRAAID LNVPLITNSR LASAFISAFC TLKMDDIDIK AWDEFK
//
