ID   A0A1N6JIK3_9BACT        Unreviewed;       938 AA.
AC   A0A1N6JIK3;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Carbamoyl-phosphate synthase large subunit {ECO:0000313|EMBL:SIO44063.1};
GN   ORFNames=SAMN04488055_4049 {ECO:0000313|EMBL:SIO44063.1};
OS   Chitinophaga niabensis.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Chitinophaga.
OX   NCBI_TaxID=536979 {ECO:0000313|EMBL:SIO44063.1, ECO:0000313|Proteomes:UP000185003};
RN   [1] {ECO:0000313|EMBL:SIO44063.1, ECO:0000313|Proteomes:UP000185003}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 24787 {ECO:0000313|EMBL:SIO44063.1,
RC   ECO:0000313|Proteomes:UP000185003};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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; FSRA01000002; SIO44063.1; -; Genomic_DNA.
DR   RefSeq; WP_074241418.1; NZ_FSRA01000002.1.
DR   AlphaFoldDB; A0A1N6JIK3; -.
DR   STRING; 536979.SAMN04488055_4049; -.
DR   OrthoDB; 9804197at2; -.
DR   Proteomes; UP000185003; 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   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; 1.
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:UP000185003};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          133..328
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          676..867
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   938 AA;  104945 MW;  2A5960D5DAFC71C6 CRC64;
     MPKDTSIKSV LIIGSGPIII GQACEFDYSG SQAARSIREE GIKVILINSN PATIMTDPMM
     ADRVYLLPLT VESIEQILEE NQIDAVLPTM GGQTALNLCK EVDELGIWEK FNVRLIGVDI
     KAIDKAEDRE QFRQWMIQLG IPVAPARTAN SLLEGKEFAQ EIGFPLVIRP SFTLGGTGGG
     FVHGKEDLDE ALDRGLKASP MHEVLVEKAV LGWKEYELEL LRDKNDNVVI ICTVENLDPM
     GIHTGDSITV APAMTLSDTA FQDMRNKAMM MMRQLGNFAG GCNVQFAMNP ENEELIAIEI
     NPRVSRSSAL ASKATGYPIA KIAAKLAIGY TLDELENQIT RTTSAFFEPA LDYVIVKMPR
     WNFDKFKGAD DTLGLQMKSV GEVMSIGRTF TEALQKACQS LENDAVGLGY YGKSLLKSEQ
     LIEKLKRPTW DRIFRIKDAL MEGMSVKSIH QATLIDRWFL HQINDIVTVE KQLLEHDLES
     VPMDLLKEAK QMGFSDKQLA IIFGNCEEDE VYEKRKAAGI VRTYKMVDTC AAEFEAKTPY
     FYSTFDTENE SIPSDKKKVI VLGSGPNRIG QGIEFDYCCT HGLQAIQECG YDAIMVNCNP
     ETVSTDFDMA NKLYFEPVYW EHLWEIIELE KPEGVIVQLG GQTALKLAKK LTEKGVKIIG
     TSFDSMDIAE DRGRFSDRLK ELGIPFPKYG TAYNTDDAIE VAKEVGYPVL VRPSYVLGGQ
     RMRIVINEEE LEKSVLSLLK HLPGNKILID HFLDRCQEAE IDAIFDGENF HVMGVMEHIE
     PAGIHSGDSN AVLPAFNLSQ MIVTTMEYYS EKIARALNIK GLINIQFAIK DGQVFVIEAN
     PRASRTTPFI AKAYQVPYLN IATKVMLGAN KLTDFKIEKN LKGFAIKEPV FSFNKFPGVN
     KELGPEMKST GEAIRFIKDL RDPYFRTLYK ERSMHLSK
//