ID   A0A0A2MB51_9FLAO        Unreviewed;       951 AA.
AC   A0A0A2MB51;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Carbamoyl phosphate synthase large subunit {ECO:0000313|EMBL:KGO89494.1};
GN   ORFNames=Q764_06885 {ECO:0000313|EMBL:KGO89494.1};
OS   Flavobacterium suncheonense GH29-5 = DSM 17707.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1121899 {ECO:0000313|EMBL:KGO89494.1, ECO:0000313|Proteomes:UP000030121};
RN   [1] {ECO:0000313|EMBL:KGO89494.1, ECO:0000313|Proteomes:UP000030121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GH29-5 {ECO:0000313|EMBL:KGO89494.1,
RC   ECO:0000313|Proteomes:UP000030121};
RA   Zeng Z., Chen C.;
RL   Submitted (SEP-2013) 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:KGO89494.1}.
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DR   EMBL; JRLW01000008; KGO89494.1; -; Genomic_DNA.
DR   RefSeq; WP_026979291.1; NZ_JRLW01000008.1.
DR   AlphaFoldDB; A0A0A2MB51; -.
DR   STRING; 1121899.GCA_000430025_00499; -.
DR   eggNOG; COG0458; Bacteria.
DR   OrthoDB; 9804197at2; -.
DR   Proteomes; UP000030121; 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;  106090 MW;  41D608D2E4946641 CRC64;
     MPKDTSIKSV LIIGSGPIVI GQACEFDYSG SQSARSLREE GIEVILINSN PATIMTDPSM
     ADHVYLKPLT TKSIIEILKA HPQIDAVLPT MGGQTALNLC LEADEKGIWQ DFGVRLIGVD
     VNAINVTEDR EQFKQLLAKI DVPVAPAKTA NSFLKGKEIA QEFGFPLVIR PSFTLGGTGA
     AFVHKKEDFD DLLTRGLEAS PIHEVLIDKA LLGWKEYELE LLRDKNDNVV IICTIENMDP
     MGIHTGDSIT VAPAMTLSDR TFQRMRDMAI LMMRSIGNFA GGCNVQFAVS PDEKEDIVAI
     EINPRVSRSS ALASKATGYP IAKIATKLAL GYTLDELQNQ ITKSTSALFE PTLDYVIVKI
     PRWNFDKFEG ADRTLGLQMK SVGEVMGIGR SFQEALHKAT QSLEIKRNGL GADGKGYKNY
     DQIIEKLTYA SWDRVFVIYD AIAMGIPLSR IHEITKIDMW FLKQYEELYA LEKEISNYKI
     DTLPKDLLLE AKQKGYGDRQ IAHMLGCLES QVHKLRDEMG VKRVYKLVDT CAAEFKAQTP
     YYYSTFEAEI ERPDGTRYVD NESIVTDRKK VVVLGSGPNR IGQGIEFDYS CVHGVLAASE
     CGYETIMINC NPETVSTDFD TADKLYFEPV FWEHIYDIIQ HEKPEGVIVQ LGGQTALKLA
     EKLNKYGIKI LGTSFDALDL AEDRGRFSEL LTELNIPFPR FGVAENAEEA SVLADSLDFP
     LLVRPSYVLG GQGMKIVINK QELEEHVIEI LKHIPGNKLL LDHYLDGAIE AEADAICDAD
     GNVYIIGIME HIEPCGIHSG DSNATLPPFN LGEFVMQQIK DHTHKIAKAL KTVGLINIQF
     AIKDDIVYII EANPRASRTV PFIAKAYGEP YVNYATKVML GHNKVTDFNF NPQLKGFAIK
     QPVFSFSKFK NVNKALGPEM KSTGESILFI EDLKDDQFYE LYSRRKMYLS R
//