ID   A0A1G7XS18_9FLAO        Unreviewed;       950 AA.
AC   A0A1G7XS18;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Carbamoyl-phosphate synthase large subunit {ECO:0000313|EMBL:SDG86987.1};
GN   ORFNames=SAMN04488027_10994 {ECO:0000313|EMBL:SDG86987.1};
OS   Psychroflexus sediminis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Psychroflexus.
OX   NCBI_TaxID=470826 {ECO:0000313|EMBL:SDG86987.1, ECO:0000313|Proteomes:UP000199296};
RN   [1] {ECO:0000313|EMBL:SDG86987.1, ECO:0000313|Proteomes:UP000199296}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19803 {ECO:0000313|EMBL:SDG86987.1,
RC   ECO:0000313|Proteomes:UP000199296};
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; FNCW01000009; SDG86987.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G7XS18; -.
DR   STRING; 470826.SAMN04488027_10994; -.
DR   OrthoDB; 9804197at2; -.
DR   Proteomes; UP000199296; 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:UP000199296};
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;  106269 MW;  DBFD559BA5659EF4 CRC64;
     MPKNNSIKTI LIIGSGPIVI GQACEFDYAG SQSLRSLREE GIKTILINSN PATIMTDPSM
     ADHVYLKPLT TKSIVEILTD HPEIDAVLPT MGGQTALNLC IEADDKGIWE DFKVNIIGVD
     IDAINITEDR EKFRKLMQDI GVGVAPSKTV TSFLQGKEVA QVFGFPLVIR ASFTLGGSGA
     SIVYAEDQFE ELLTRGLEAS PIHEVIIDKA LLGWKEFELE LLRDRNDNVT IICSIENMDP
     MGIHTGDSIT VAPAMTLSDR TYQKMRDMAI KMMRSIGDFA GGCNVQFAVS PDEKEDIIAI
     EINPRVSRSS ALASKATGYP IAKIASKLAI GYHLDELQNQ ITQTTSAFFE PTLDYVIVKI
     PRWNFDKFEG SDRTLGLQMK SVGEVMGIGR SFQEALHKAT QSLEIKRNGL GADGKSYTDY
     NQILSKLEFA SWDRVFVIYD AIQLGIPLSR IHEITKIDMW FLKQYEELFN LEKEISKYSI
     QNISKDLMLE AKQKGFADRQ IAHMLKCLES EVYAKREELN VNRIYKLVDT CAAEFEAHTP
     YYYSTFEADV ENKDGEIINT NESIVTSKKK VIVLGSGPNR IGQGIEFDYC CVHGVLAAAE
     CGYETIMINC NPETVSTDFD TADKLYFEPV FWEHIYDIIK HEKPEGVIVQ LGGQTALKLA
     EKLNRYGIKI LGTSYESLDL AEDRGSFSKL LQDNNIPYPE FGVAETADEA LALAEKLDFP
     LLVRPSYVLG GQGMKIVINK KDLETHVVDL LRKIPNNKLL LDHYLDGAIE AEADAICDGE
     DVYIVGIMEH IEPCGVHSGD SNAMLPPFNL GDLVLEQIKD HTRKIALALN TVGLLNVQFA
     IKDDHVYIIE ANPRASRTVP FIAKAYKEPY VNYATKIMLG ENKLNDFTFN PQLEGYAIKQ
     PVFSFDKFHN VNKQLGPEMK STGESILFID SLRDDTFYEL YGRRKMYLSK
//