ID A0A1Z5IK64_9LACO Unreviewed; 834 AA.
AC A0A1Z5IK64;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Carbamoyl phosphate synthase large subunit {ECO:0000313|EMBL:GAX02018.1};
GN Name=carB_2 {ECO:0000313|EMBL:GAX02018.1};
GN ORFNames=IWT126_02082 {ECO:0000313|EMBL:GAX02018.1};
OS Secundilactobacillus silagei JCM 19001.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Secundilactobacillus.
OX NCBI_TaxID=1302250 {ECO:0000313|EMBL:GAX02018.1, ECO:0000313|Proteomes:UP000198402};
RN [1] {ECO:0000313|EMBL:GAX02018.1, ECO:0000313|Proteomes:UP000198402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IWT126 {ECO:0000313|EMBL:GAX02018.1,
RC ECO:0000313|Proteomes:UP000198402};
RA Tohno M., Tanizawa Y., Arita M.;
RT "Draft genome sequences of new species of the genus Lactobacillus isolated
RT from orchardgrass silage.";
RL Submitted (NOV-2015) 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:GAX02018.1}.
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DR EMBL; BCMG01000011; GAX02018.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z5IK64; -.
DR STRING; 1302250.GCA_001313225_01900; -.
DR OrthoDB; 9804197at2; -.
DR Proteomes; UP000198402; 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:0006520; P:amino acid metabolic process; IEA:UniProt.
DR Gene3D; 3.40.50.20; -; 2.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 1.10.1030.10; Carbamoyl-phosphate synthetase, large subunit oligomerisation domain; 1.
DR InterPro; IPR011761; ATP-grasp.
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; IPR016185; PreATP-grasp_dom_sf.
DR PANTHER; PTHR11405:SF5; CAD PROTEIN; 1.
DR PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR Pfam; PF02787; CPSase_L_D3; 1.
DR PRINTS; PR00098; CPSASE.
DR SMART; SM01096; CPSase_L_D3; 1.
DR SUPFAM; SSF48108; Carbamoyl phosphate synthetase, large subunit connection domain; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 2.
DR PROSITE; PS50975; ATP_GRASP; 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 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}.
FT DOMAIN 131..325
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 834 AA; 92351 MW; 0D1C39E48A8242A5 CRC64;
MDNEIQKVLI IGGGPTEIGH ETELDAACVQ VIQAFKKQGI RSLLIDNNPF SVALEDVQPT
NMFIQAVTAN NVQRIIEREQ PDAILASVGG VTAISVVQEL QENGVLADND VKTLGIPADA
LMDINNPDRL NDVMRHVGVP VIASETVGTL DEAINVAAKI GYPVIVKPIA PRIDTNRMLC
ENEQDMISAV SRGFSWSRFK QCVIEQSIVG YKEIELVSMR DAMGTQVLIA GLENIDPIGI
HSGDSMVVTP TLTLSNEEYE TLRDTAFAIN NQFQFTGVVH THFALGSSED SYYVTKVTPY
NDRGTSLVAC ATGYPIAYVA ANLYLNQKLT DVHLPEIYHF KQTALLEPSL DHVVVRIPLW
PFEDVKNADQ HLSTVMKSVG STIGVGRSTE EAILKALRSS QFSPQDELPS MSDLTDSQLI
SQLIHPLSSR ILVLIEALRR GYQVDELSEL TKIDPFYFVK LRHILEIEEQ IKTHPMAVDA
LHEGRYYGFG DGMIARIWHT DIETVRRLGQ DNHISPTYKG IEPSAGELLN SPTAYYSTFE
LENESQQISA KTVLVLGRGG NQLGPNASAD YFTTEMLKQL RKSGYQTVIM NTNPNAGSLT
ATLTDKQIID PVQLGDIMNV IAIEHPVKIF VPGNRHYLTR ELRQRNYAIS ILPPDQEKRS
ELLNDHANIG LDLFVTEGHI VPILASDLRS DQGIATTLDQ ITLMRTPATL TDQQLTAIIA
HAKDYLGAHK RTGMVQMLYT TNGQQAPQFA GVRPTRLTTI AYLNKVTGIN WVRMLVRQAL
GEIDEDLIAK LAVDIRSDRR SQVRGTFPFK QLQLPDQLGL TTQEVGARIS FETL
//
