ID   A0A099Y4T9_9FLAO        Unreviewed;       951 AA.
AC   A0A099Y4T9;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Carbamoyl-phosphate synthase large chain {ECO:0000313|EMBL:KGL63605.1};
DE            EC=6.3.5.5 {ECO:0000313|EMBL:KGL63605.1};
GN   ORFNames=PHEL85_0642 {ECO:0000313|EMBL:KGL63605.1};
OS   Polaribacter sp. Hel1_85.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae.
OX   NCBI_TaxID=1250005 {ECO:0000313|EMBL:KGL63605.1, ECO:0000313|Proteomes:UP000029991};
RN   [1] {ECO:0000313|EMBL:KGL63605.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hel1_85 {ECO:0000313|EMBL:KGL63605.1};
RA   Xing P., Hahnke R.L., Unfried F., Markert S., Huang S., Barbeyron T.,
RA   Harder J., Becher D., Schweder T., Gloenk F.O., Amann R.I., Teeling H.;
RT   "Niches of two polysaccharide-degrading Polaribacter strains isolated from
RT   the North Sea during a spring diatom bloom.";
RL   ISME J. 0:0-0(2014).
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:KGL63605.1}.
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DR   EMBL; JPDS01000001; KGL63605.1; -; Genomic_DNA.
DR   RefSeq; WP_036820924.1; NZ_JPDS01000001.1.
DR   AlphaFoldDB; A0A099Y4T9; -.
DR   STRING; 1250005.PHEL85_0642; -.
DR   eggNOG; COG0458; Bacteria.
DR   OrthoDB; 9804197at2; -.
DR   Proteomes; UP000029991; 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};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KGL63605.1};
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;  106192 MW;  959C5CFD6DF61F31 CRC64;
     MPKRKDLKSV LIIGSGPIVI GQACEFDYSG SQSLRSLRED GIETILINSN PATIMTDPSM
     ADHIYLLPLT TKSIIQILKE HPQIDAVLPT MGGQTALNLC IEADDKGIWE DFNVKLIGVD
     INAINITEDR EQFRELMIKI DVPMAPQATA TSFLKGKEIA QEFGFPLVIR SSYTLGGAGA
     SIVYDPKDFD ELLSRGLEAS PIHEVMIDKA MMGWKEYELE LLRDKNDNVV IICSIENMDP
     MGIHTGDSIT VAPAMTLSDT TFQKMRDMAI HMMRSIGDFE GGCNVQFAVS PDENEDIIAI
     EINPRVSRSS ALASKATGYP IAKVATKLAI GYSLDELENG ITKSTSALFE PTLDYVIVKI
     PRWNFDKFEG SDRTLGLQMK SVGEVMGIGR SFQEALHKAT QSLEIKRNGL GADGKGYTNY
     NQIIDKLTNA SWDRVFAIYD AIAIGIPLSQ IHDITKIDMW YLKQYEELFQ LQKEISTYTI
     DTIQRDLLLE AKQKGYGDRQ IAHMLDCLES QVYTKREELK VQRVFKLVDT CAAEFKAKTP
     YYYSTFENEI ETSDGQITIA NESIVTDKKK IIVLGSGPNR IGQGIEFDYC CVHGVLAAAE
     CGYETIMINC NPETVSTDFD TADKLYFEPV FWEHIYDIIR HEKPEGVIVQ LGGQTALKLA
     EKLTKYGIKI IGTSFEALDI AEDRGRFSAM LKENKIPFPE YGIAETADEA LDLADQLDFP
     ILVRPSYVLG GQGMKIVINK EELVKHVVDL LGRMPGNKLL LDHYLDGAIE AEADAICDAD
     GNVYIIGIME HIEPCGIHSG DSNATLPAFN LGEFVMQQIK DHTSTIATEL KTVGLINIQF
     AIKDDIVYII EANPRASRTV PFIAKAYKEP YVNYATKVML GHNKVTDFNF NPQLEGFAIK
     QPVFSFNKFP NVDKKLGPEM KSTGESILFI DSLKDDDFYD LYSRRKMYLN K
//