ID   W0F2J5_9BACT            Unreviewed;       952 AA.
AC   W0F2J5;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Carbamoyl phosphate synthase large subunit {ECO:0000313|EMBL:AHF16033.1};
GN   ORFNames=NIASO_14470 {ECO:0000313|EMBL:AHF16033.1};
OS   Niabella soli DSM 19437.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Niabella.
OX   NCBI_TaxID=929713 {ECO:0000313|EMBL:AHF16033.1, ECO:0000313|Proteomes:UP000003586};
RN   [1] {ECO:0000313|EMBL:AHF16033.1, ECO:0000313|Proteomes:UP000003586}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19437 {ECO:0000313|Proteomes:UP000003586};
RG   DOE Joint Genome Institute;
RA   Eisen J., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA   Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA   Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL   Submitted (DEC-2013) 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; CP007035; AHF16033.1; -; Genomic_DNA.
DR   RefSeq; WP_008586614.1; NZ_CP007035.1.
DR   AlphaFoldDB; W0F2J5; -.
DR   STRING; 929713.NIASO_14470; -.
DR   KEGG; nso:NIASO_14470; -.
DR   eggNOG; COG0458; Bacteria.
DR   HOGENOM; CLU_000513_1_0_10; -.
DR   OrthoDB; 9804197at2; -.
DR   Proteomes; UP000003586; Chromosome.
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:UP000003586};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          133..328
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          690..881
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   952 AA;  105678 MW;  345036EC991111A9 CRC64;
     MPKDTSIKSV LIIGSGPIII GQACEFDYSG TQAARSLREE GIKVILINSN PATIMTDPMM
     ADRVYLLPLT TESIEQILQE NDIDAVLPTM GGQTALNLCK EAEELGIWKQ YNVRLIGVDI
     KAIDKAEDRE LFRQWMIQLG IQVATAKTAN SFLEGKEYAQ EIGFPLVIRP SFTLGGTGGG
     FVHDKDELDE ALNRGLQASP IHEVLVEQAV LGWKEFELEL LRDAADNVCI ICTVENFDPM
     GVHTGDSITV APAMTLSDTG MQLMRNTAIR MMRDLGNFSG GCNVQFAMNP ATEEIIAIEI
     NPRVSRSSAL ASKATGYPIA KIAAKLAIGY NLDELENQIT KTTSAYFEPA LDYVIVKIPR
     WNFDKFKGAN DTLGLQMKSV GEVMAIGRTF NEAIQKACQS LENNAIGLGY YGKSLMRGEE
     LLEYIKTPKW DRIFRIKDAL MAGISVGTIS KATNGIDRWF LSEIQKLCTI EKQIAAYTLE
     TLPAELLRDA KVNGFSDAQI AEIMGHGNTE DAVYSKRKEL GISRVYKMVD TCSAEFEAKT
     PYFYSTFDAP VNAAVTTDGL VHNESKVTDR KKIIVLGSGP NRIGQGIEFD YCCVHGLLAI
     KEAGYEAIMM NCNPETVSTD FDMADKLYFE PVYWEHVREL IEYEKPEGVI VQLGGQTALK
     LAEKITAMGV KIMGTSFDNM DIAEDRGRFS DMLKELGIPY PEYGSAWNVD EAVAIANRVG
     YPVLVRPSYV LGGQRMRIVI NDDELERAVI SLLKHIPGNK ILIDHFLDRC QEAEVDAIYD
     GTNFHVMGVM EHIEPAGIHS GDSNAVLPAF NLSPMEVTTM EHYSEKIARA LNIQGLINIQ
     FAIKDGTVYV IEANPRASRT TPFIAKAYQI PYLNVATKVM IGANKLTDFK FEKKLKGYAI
     KEPVFSFNKF PGVNKELGPE MKSTGEAIRF IKDLRDPYFR ALYKDRSMYL SK
//