ID   A0A1M7NMP6_9FLAO        Unreviewed;       950 AA.
AC   A0A1M7NMP6;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Carbamoyl-phosphate synthase large subunit {ECO:0000313|EMBL:SHN05221.1};
GN   ORFNames=SAMN05216269_111121 {ECO:0000313|EMBL:SHN05221.1};
OS   Flavobacterium xinjiangense.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=178356 {ECO:0000313|EMBL:SHN05221.1, ECO:0000313|Proteomes:UP000184092};
RN   [1] {ECO:0000313|EMBL:SHN05221.1, ECO:0000313|Proteomes:UP000184092}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.2749 {ECO:0000313|EMBL:SHN05221.1,
RC   ECO:0000313|Proteomes:UP000184092};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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}.
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DR   EMBL; FRCL01000011; SHN05221.1; -; Genomic_DNA.
DR   RefSeq; WP_073210233.1; NZ_FRCL01000011.1.
DR   AlphaFoldDB; A0A1M7NMP6; -.
DR   STRING; 178356.SAMN05216269_111121; -.
DR   OrthoDB; 9804197at2; -.
DR   Proteomes; UP000184092; 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..879
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   950 AA;  105640 MW;  F34DBA349E597ABC CRC64;
     MPKDTSIKSV LIIGSGPIVI GQACEFDYAG SQSARSIREE GIEVILINSN PATIMTDPSM
     ADHIYLKPLT TKSIIEILKA HPQIDAVLPT MGGQTALNLC LEADEKGIWA DFGVKLIGVD
     VNAINITEDR EQFKQLLKKI GVPSAPAEIC TSYLRGKEIA QEFGFPLVIR PSFTLGGTGA
     AIVYKKEDFD ELLTRGLEAS PIHEVLIDKA LMGWKEYELE LLRDKNDNVV IICSIENMDP
     MGIHTGDSIT VAPAMTLSDT TFQKMRDYAI LMMRSIGNFA GGCNVQFAVS PDDKEDIVAI
     EINPRVSRSS ALASKATGYP IAKIASKLAL GYNLDELQNQ ITKSTSALFE PTLDYVIVKI
     PRWNFDKFEG ADRTLGLQMK SVGEVMGIGR SFQEALHKAT QSLEIKGNGL GADGKGYKNY
     EQIIEKLTFA SWDRVFVIYD AIAMGIPLSR IHEITKIDMW FLKQYEELYT LEKEISNYKV
     ESLPRELLLE AKQKGFADRQ IAHMVGCLES QVHTLRTTMN INRVFKLVDT CAAEFKAKTP
     YYYSTFEAEI EKADGTRYVD NESVVTDKKK IIVLGSGPNR IGQGIEFDYS CVHGVLAAKE
     CGYETIMINC NPETVSTDFD TADKLYFEPV FWEHIYDIIQ HEKPEGVIVQ LGGQTALKLA
     EKLSKYGIKI IGTSFDALDL AEDRGRFSEL LTDLKIPFPQ FGIAETADEA SALADVLDFP
     LLIRPSYVLG GQGMKIVINK QELEEHVINL LKTIPGNKLL LDHYLDGAIE AEADAICDGE
     NVYIIGIMEH IEPCGVHSGD SNATLPPFNL GEFVMQQIKD HTKNIALALR TVGLINIQFA
     IKDDIVYIIE ANPRASRTVP FIAKAYGEAY VNYATKVMLG EKKVTDFVFN PQLKGFAIKQ
     PVFSFSKFHN VNKALGPEMK STGESILFID DLKDDQFYEL YSRRKMYLSK
//