ID A0A1I0PF18_9BACT Unreviewed; 937 AA.
AC A0A1I0PF18;
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:SEW12883.1};
GN ORFNames=SAMN05428988_2320 {ECO:0000313|EMBL:SEW12883.1};
OS Chitinophaga sp. YR573.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=1881040 {ECO:0000313|EMBL:SEW12883.1, ECO:0000313|Proteomes:UP000198758};
RN [1] {ECO:0000313|EMBL:SEW12883.1, ECO:0000313|Proteomes:UP000198758}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YR573 {ECO:0000313|EMBL:SEW12883.1,
RC ECO:0000313|Proteomes:UP000198758};
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; FOJF01000001; SEW12883.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0PF18; -.
DR STRING; 1881040.SAMN05428988_2320; -.
DR OrthoDB; 9804197at2; -.
DR Proteomes; UP000198758; 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 Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 133..328
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 675..866
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 937 AA; 104726 MW; 2537BE0C5179144F CRC64;
MPKDSSIKSV LIIGSGPIII GQACEFDYSG SQAARSLREE GIKVVLINSN PATIMTDPMM
ADKVYLLPLT VESIEQILEE HQIDAVLPTM GGQTALNLCK EVDELGIWQK YNVRLIGVDI
KAIDKAEDRE QFRQWMIQLG VPVAPARTAN SFLEGKEFAQ EIGFPLVIRP SFTLGGTGGG
FVHSKDELDE ALQRGLQASP IHEVLVEKAV LGWKEFELEL LRDSNDNVVI ICTVENLDPM
GIHTGDSITV APAMTLSDTS FQDMRNKAIM MMRDLGNFAG GCNVQFSQNP ANEELIAIEI
NPRVSRSSAL ASKATGYPIA KIAAKLAIGY TLDELENQIT KTTSAFFEPA LDYVIVKMPR
WNFDKFKGAD QTLGLQMKSV GEVMAIGRTF PEALQKACQS LENDALGLGY YGKSLMSSEQ
LLERMKTPTW DRIFRIKDAL MAGVSVKHLH QMTYIDKWFL NQINDIVTLE KQLLEFDLNT
VPNDLLSEAK KMGFSDMQLT HLLDCEEDEV YAKRKALGIT RTFKMVDTCA AEFEAKTPYF
YSTFDTENES KPTDKKKVIV LGSGPNRIGQ GIEFDYCCTH GLQAIQESGY EAIMVNCNPE
TVSTDFDMAD KLYFEPVFWE HLWEIIELEK PEGVIVQLGG QTALKLAKRL EEKGVKIIGT
SFDNMDIAED RGRFSDLLKD LGIPYPNYGT AYNTDDAIEV AKEVGYPVLV RPSYVLGGQR
MRIVINEEEL ETSVLSLLKH LPGNKILIDH FLDRCQEAEI DGIFDGDDFH VMGVMEHIEP
AGIHSGDSNA LLPSFNLTPL EVTTMEFYAE KIARALNIRG LINIQFAIKN GQVFVIEANP
RASRTTPFIA KAYQVPYLNI ATKVMLGAKK LKDFTIEKNL KGFAIKEPVF SFNKFPGVNK
ELGPEMKSTG EAIRFIKDLR DPYFRTLYKE KSMYLSK
//
