ID   M7MZ23_9FLAO            Unreviewed;       950 AA.
AC   M7MZ23;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Carbamoyl-phosphate synthase large chain {ECO:0000313|EMBL:EMQ94749.1};
GN   ORFNames=D778_00389 {ECO:0000313|EMBL:EMQ94749.1};
OS   Xanthomarina gelatinilytica.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Xanthomarina.
OX   NCBI_TaxID=1137281 {ECO:0000313|EMBL:EMQ94749.1, ECO:0000313|Proteomes:UP000012024};
RN   [1] {ECO:0000313|EMBL:EMQ94749.1, ECO:0000313|Proteomes:UP000012024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AK20 {ECO:0000313|EMBL:EMQ94749.1,
RC   ECO:0000313|Proteomes:UP000012024};
RA   Kumar R., Khatri I., Vaidya B., Subramanian S., Pinnaka A.;
RT   "Genome assembly of Formosa sp. AK20.";
RL   Submitted (DEC-2012) 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:EMQ94749.1}.
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DR   EMBL; ANLA01000014; EMQ94749.1; -; Genomic_DNA.
DR   RefSeq; WP_007649875.1; NZ_ANLA01000014.1.
DR   AlphaFoldDB; M7MZ23; -.
DR   PATRIC; fig|1137281.3.peg.1821; -.
DR   eggNOG; COG0458; Bacteria.
DR   OrthoDB; 9804197at2; -.
DR   Proteomes; UP000012024; 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; 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   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   SMART; SM01209; GARS_A; 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   Reference proteome {ECO:0000313|Proteomes:UP000012024};
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;  106521 MW;  44F280A085E40C88 CRC64;
     MPKNSKLKSI LIIGSGPIVI GQACEFDYSG TQALRSLRED GIETILINSN PATIMTDPSM
     ADHVYLLPLT TKSIIQILKE HPQIDAVLPT MGGQTALNLC IEADEKGIWK DFNVDIIGVD
     IDAINITEDR EKFRELMLKI GIPMAPQATA TSYLQGKEIA QEFGFPLVIR ASFTLGGAGA
     SFVYKEEEFD ELLTRGLEIS PIHEVMIDKA LIGWKEYELE LLRDANDNVV IICSIENMDP
     MGIHTGDSIT VAPAMTLSDR TYQKMRDMAI HMMRSIGDFA GGCNVQFAVS PDDEENIIAI
     EINPRVSRSS ALASKATGYP IAKVAAKLAI GYHLDELDNQ ITKSTSALFE PTLDYVIVKI
     PRWNFDKFEG SDRTLGLQMK SVGEVMGIGR SFQEALHKAT QSLEIKRNGL GADGKGYKNY
     DQIISKLTYA SWDRVFVIYD AIQMGIPLSR IHEITKIDMW FLKQYEELYH LEKEISNYSI
     ETLNRELLLE AKQKGYGDRQ IAHMLNCLES QVYKKREELG IKRVYKLVDT CAAEFKAQTP
     YYYSTFENEM ETADGTLYPH NESIVSDKKK IVVLGSGPNR IGQGIEFDYC CVHGVLAAAE
     CGYETIMINC NPETVSTDFD TADKLYFEPV FWEHIYDIIK HEKPEGVIVQ LGGQTALKLA
     EKLDRYGIKI IGTTYQSLDL AEDRGSFSKL LKENDIPYPK FDVATTAEEA LAVADKLDFP
     ILVRPSYVLG GQGMKIVINK KELEEHVVDL LRSIPNNKLL LDHYLDGAIE AEADAICDGE
     NVYIIGIMEH IEPCGIHSGD SNATLPPFNL GEFVMQQIKD HTKKIALALN TVGLINIQFA
     IKDDIVFIIE ANPRASRTVP FISKAYGEPY VNYATKVMLG EKKVTDFNFN PQLKGYAIKQ
     PVFSFNKFHN VNKKLGPEMK STGESILFIE SLKDDEFYNL YSRRKMYLSK
//