ID   A0A1B8TP82_9FLAO        Unreviewed;       951 AA.
AC   A0A1B8TP82;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Carbamoyl phosphate synthase large subunit {ECO:0000313|EMBL:OBY61374.1};
GN   ORFNames=LPB3_16315 {ECO:0000313|EMBL:OBY61374.1};
OS   Polaribacter vadi.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae.
OX   NCBI_TaxID=1774273 {ECO:0000313|EMBL:OBY61374.1, ECO:0000313|Proteomes:UP000092584};
RN   [1] {ECO:0000313|Proteomes:UP000092584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LPB0003 {ECO:0000313|Proteomes:UP000092584};
RA   Shin S.-K., Yi H., Kim E.;
RL   Submitted (FEB-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}.
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:OBY61374.1}.
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DR   EMBL; LSFM01000027; OBY61374.1; -; Genomic_DNA.
DR   RefSeq; WP_065320704.1; NZ_LSFM01000027.1.
DR   AlphaFoldDB; A0A1B8TP82; -.
DR   STRING; 1774273.LPB03_16375; -.
DR   KEGG; pob:LPB03_16375; -.
DR   OrthoDB; 9804197at2; -.
DR   Proteomes; UP000092584; 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   Gene3D; 3.40.50.20; -; 2.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 2.
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   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; 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   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; 2.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 2.
DR   PROSITE; PS50975; ATP_GRASP; 2.
DR   PROSITE; PS00866; CPSASE_1; 2.
DR   PROSITE; PS00867; CPSASE_2; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          134..330
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          688..880
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   951 AA;  106300 MW;  DE48E10DA46F8727 CRC64;
     MPKRKDLKSI LIIGSGPIVI GQACEFDYSG SQSLRSLRED GIETILINSN PATIMTDPSM
     ADHIYLLPLT TKSIIQILKE HPQIDAVLPT MGGQTALNLC IEADDKGIWK DFNVKLIGVD
     IDAINVTEDR EQFRELMLKI GVPMAPQATA TSFLKGKEIA QEFGFPLVIR SSYTLGGAGA
     SIVYKPEDFD ELLSRGLEAS PIHEVMIDKA MMGWKEYELE LLRDKNDNVV IICSIENMDP
     MGIHTGDSIT VAPAMTLSDK TYQKMRDMAI HMMRSIGDFE GGCNVQFAVS PDEKEDIIAI
     EINPRVSRSS ALASKATGYP IAKVATKLAI GYTLDELENG ITKSTSALFE PTLDYVIVKI
     PRWNFDKFEG SDRTLGLQMK AVGEVMGIGR SFQEALHKAT QSLEIKRNGL GADGKGYTNY
     NQIIEKLTNA SWDRVFAIYD AIAMGIPLSQ IYEITKIDMW YLKQYEELFQ LQKEISTFTI
     DTLQRDLLLE AKQKGYGDRQ IAHMLGCLES EVYNKREELK VQRVFKLVDT CAAEFKAKTP
     YYYSTFENEI ETADGEITIA NESIVTDKKK IIVLGSGPNR IGQGIEFDYC CVHGVLAAAE
     CGYETIMINC NPETVSTDFD TADKLYFEPV FWEHIYDIIR HEKPEGVIVQ LGGQTALKLA
     EKLTKYGIKI IGTSFEALDI AEDRGRFSSM LKENNIPYPE FGIAETADEA LQLADELDFP
     ILVRPSYVLG GQGMKIVINK EELVEHVVDL LGRMPGNKLL LDHYLDGAIE AEADAICDAD
     GNVYIIGIME HIEPCGIHSG DSNATLPAFN LGDLVMQQIK DHTHTIAREL KTIGLINVQF
     AIKDDIVYII EANPRASRTV PFIAKAYKEP YVNYATKVML GHNKVTDFKF NPQLEGYAIK
     QPVFSFNKFP NVNKKLGPEM KSTGESILFI DSLKDDQFYD LYARRKMYLN K
//