ID   A0A1G7EPG0_9FLAO        Unreviewed;       951 AA.
AC   A0A1G7EPG0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Carbamoyl-phosphate synthase large subunit {ECO:0000313|EMBL:SDE65477.1};
GN   ORFNames=SAMN05421636_106269 {ECO:0000313|EMBL:SDE65477.1};
OS   Pricia antarctica.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Pricia.
OX   NCBI_TaxID=641691 {ECO:0000313|EMBL:SDE65477.1, ECO:0000313|Proteomes:UP000199109};
RN   [1] {ECO:0000313|EMBL:SDE65477.1, ECO:0000313|Proteomes:UP000199109}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23421 {ECO:0000313|EMBL:SDE65477.1,
RC   ECO:0000313|Proteomes:UP000199109};
RA   de Groot N.N.;
RL   Submitted (OCT-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; FNAO01000006; SDE65477.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G7EPG0; -.
DR   STRING; 641691.SAMN05421636_106269; -.
DR   OrthoDB; 9804197at2; -.
DR   Proteomes; UP000199109; 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   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:UP000199109};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          134..330
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          689..880
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   951 AA;  106349 MW;  167753F2D39E3C02 CRC64;
     MPKREDLKSI LIIGSGPIII GQACEFDYAG SQSLRSLRED GVETILINSN PATIMTDPTM
     ADHVYLKPLT TKSIVEILKA HPQIDAVLPT MGGQTALNLC IQADEKGIWE DFGVEIIGVD
     IDAINITEDR EKFRELMLKI GIGMAPQATA TSFLKGKEIA QEFGFPLVIR ASYTLGGDGA
     SIVYKPEEFD EMLSRGLEIS PIHEVMIDKA LIGWKEYELE LLRDRNDNVV IICAIENMDP
     MGIHTGDSIT VAPAMTLSDR TYQKMRDMAI HMMRSIGDFA GGCNVQFAVS PDENEDIIAI
     EINPRVSRSS ALASKATGYP IAKIASKLAI GYHLDELDNQ ITKSTSALFE PALDYVIVKI
     PRWNFDKFEG SDRTLGLQMK SVGEVMGIGR SFQEALHKAT QSLEIKRNGL GADGKGYKDY
     DQIISKLTIP SWDRVFVIYD AIQLGIPLSR IHEITKIDMW FLKQYEELHY LEKEISTYTI
     ATITRELMLE AKQKGFADRQ IAHMLDCYES EVHKKRTLEM DINRVYKLVD TCAAEFKAMT
     PYYYSTFEAE IEKPDGTRYV ENDSIVTDKK KVVVLGSGPN RIGQGIEFDY CCVHGVLAAA
     ECGYETIMIN CNPETVSTDF DTADKLYFEP VFWEHIYDII LHEKPEGVIV QLGGQTALKL
     AEKLDKYGIK IIGTSFQSLD LAEDRGSFSE LLKANDIPFP EFGVAETADE ALALADKLDF
     PLLVRPSYVL GGQGMKIVIN KTELEEHVVD LLRKIPNNKL LLDHYLDGAI EAEADAICDG
     KDVYIIGIME HIEPCGIHSG DSNATLPPFN LGEFVLQQIK DHTNKIALAL NTVGLINIQF
     AIKDDIVYII EANPRASRTV PFIAKAYGEP YVNYATKVML GEKKVKDFDF NPQLEGFAIK
     QPVFSFNKFP NVNKNLGPEM KSTGESILFI DNLKDDQFYD LYGRRKMYLS K
//