ID   A0A1H7BQA4_9BACT        Unreviewed;       939 AA.
AC   A0A1H7BQA4;
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:SEJ75605.1};
GN   ORFNames=SAMN05192553_11175 {ECO:0000313|EMBL:SEJ75605.1};
OS   Cyclobacterium xiamenense.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC   Cyclobacterium.
OX   NCBI_TaxID=1297121 {ECO:0000313|EMBL:SEJ75605.1, ECO:0000313|Proteomes:UP000199403};
RN   [1] {ECO:0000313|Proteomes:UP000199403}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBRC-M 10761 {ECO:0000313|Proteomes:UP000199403};
RA   Varghese N., Submissions S.;
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; FNZH01000011; SEJ75605.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H7BQA4; -.
DR   STRING; 1416801.SAMN05192553_11175; -.
DR   Proteomes; UP000199403; 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   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          134..329
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          677..868
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   939 AA;  104326 MW;  F078C3DBC8789960 CRC64;
     MPKDSSIKHV LIIGSGPIII GQACEFDYAG SQAARSLREE GIKVTLINSN PATIMTDPVT
     ADNVYLLPLE KKSIVQILKE HPDIDCVLPT MGGQTALNLA IDCDKAGIWQ KFGTKMIGVD
     IDAIETAENR EKFKALMEKL NVDVCLGRTA RSFLQGKEIA QEIGFPLVIR PSYTLGGTGG
     GFVDGPDNFE KALSAGLQAS PTHEVLIEQS ILGWKEYELE VLRDNIGNMV VICSIENFDP
     MGVHTGDSIT VAPAMTLPDT VYQEMRNKAI RMMEGIGNFA GGCNVQFAVS PDNQTIIGVE
     INPRVSRSSA LASKATGYPI AKVAAKLSIG YNLDELKNSI TGNTSAFFEP AIDYVIVKIP
     RWNFDKFKGS DRKLGLSMKA VGEVMGIGRN FQEALQKACQ SLEIKRNGLG ADGKELKNQD
     EILYSLANPS WNRLFHIYDA FKLGISFRTI QDLTKIDKWF LKQIDELVQL DGVLGKETLE
     TISPDLMKKA KHKGYADRQI AHLLGCLESE VFQKRREEMG IRRVFKLVDT CAAEFEAQTP
     YFYSSFGEEN ESHVSDKKKV VVLGSGPNRV GQGIEFDYSC VHGVLAAKEC GYETIMINCN
     PETVSTDFDI ADKLYFEPVF WEHIYEIILH ENPIGVIVQL GGQTALKLAE KLDKYNIPIL
     GTSFRALDLA EDRGRFSNLL KENGVPYPEF GTIHSTDEAL ELCKTLGFPL LVRPSYVLGG
     QGMKIVINEK ELEQHVVNVL RDIPNNEILL DHFLEGAIEA EADAICDGEN VYIIGIMQHI
     EPAGIHSGDS YAVLPPYNLG DLVVRQIETF TEKIALALET KGLINIQFAI KNDKVYVIEA
     NPRASRTVPF ICKAYQEPYV NYATKVMLGE NKVTDFNFSP VKKGYAIKEP VFSFHKFPNV
     NKELGPEMKS TGEAIYFIDD LMDDYFLKIY AERNLYLSR
//