ID A0A150WSB2_BDEBC Unreviewed; 1064 AA.
AC A0A150WSB2;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Carbamoyl phosphate synthase large subunit {ECO:0000313|EMBL:KYG67401.1};
GN Name=carB {ECO:0000313|EMBL:KYG67401.1};
GN ORFNames=AZI86_10440 {ECO:0000313|EMBL:KYG67401.1};
OS Bdellovibrio bacteriovorus.
OC Bacteria; Bdellovibrionota; Bdellovibrionia; Bdellovibrionales;
OC Pseudobdellovibrionaceae; Bdellovibrio.
OX NCBI_TaxID=959 {ECO:0000313|EMBL:KYG67401.1, ECO:0000313|Proteomes:UP000075320};
RN [1] {ECO:0000313|EMBL:KYG67401.1, ECO:0000313|Proteomes:UP000075320}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R0 {ECO:0000313|EMBL:KYG67401.1,
RC ECO:0000313|Proteomes:UP000075320};
RA Ploux O.;
RL Submitted (MAR-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 -!- 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:KYG67401.1}.
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DR EMBL; LUKE01000001; KYG67401.1; -; Genomic_DNA.
DR RefSeq; WP_061834981.1; NZ_LUKE01000001.1.
DR AlphaFoldDB; A0A150WSB2; -.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000075320; 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; 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:UP000075320};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 133..328
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 667..859
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 928..1064
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 1064 AA; 117301 MW; D1E97C2A71CB3D51 CRC64;
MPRKSNIKKV LIIGSGPIVI GQACEFDYSG TQACKALMRE GLEVILVNSN PATIMTDPEV
ATRVYVEPLK VDYLEKIIEK EKPDAVIPTL GGQTALNLAL DLYAKGILQK HKVQLLGATP
QVIKAGEDRE IFRGLLDKIG AKYPKSHMVR TFEHGLQVAE ELGYPIVLRP NYTLGGGGGG
IAYSPEEYQK MLVGGLHESP TSEVLVEESI LGWKEYELEV MRDYQGTFVV VCSIENLDPC
GVHTGDSITV APQQTLSDRE YQAMRDEACK IINEVGIQTG GANIQFAVHP KTGERVVIEM
NPRVSRSSAL ASKATGFPIA KIAALLAIGY SLDELQNDIT KVTPSCYEPA LDYVVTKIPR
FAFEKFQGSK DTLTTQMKSV GEVMGIGRTL QESLMKALAS LEANPQAIPE VELEVGKISY
PNSLRIYQLF QAFREGKTVA EIEELTGIIP YFLEQIEGLI KFENKFKRDF TPEAIDLMLT
AKRKGFTDAR LGALMGKTEK EIREFREKHQ ILPRYQQVDT CAGEFESSTP YFYSSYWPTV
SASVNAPNAV VIIGSGPNRI GQGIEFDYSC VRGVKGFQKN GSKVIMVNSN PETVSTDYDT
SDVLFFEPLT VESLIEVMRF MKPKGFVAQL GGQTPINAAP ELVKAGFHLL GSSLETIDLA
EDRGLFSKIC KELNFAIPNS AMAGSLMDAL NFEENVGYPM ICRPSYVLGG RRMEVIENRD
ELMSYFQRHK DYISKERPCL MDQFLAGALE VDVDLVRGED WTVIGGVVEH IEAAGVHSGD
SMGVLPPQRL KPETCQRIED LSKQLANRIG VIGHLNLQLA VLNDVVYMLE ANPRSSRSVP
FVAKATAIPL IDLGVAAMLG KKAKDLKLDG LQWRKTEHVS VKGVVFPFKK FPEADSLLGP
EMKSTGESMG RGNNYSEALS KAFLSSNIKL PRTGQVFFSL RDKDKESMLT LAKELQRMGY
GVSATTGTAS FFNDRGVNCM SLKKVDEGRP HCVDKIRSGE VAFVINTTSG RRAIEASFDI
RRACTDYNIP CLTESDAAEA FVLALQNQKN ESSNVESLMA MEEF
//
