ID A0A255ZAZ4_9FLAO Unreviewed; 950 AA.
AC A0A255ZAZ4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Carbamoyl phosphate synthase large subunit {ECO:0000313|EMBL:OYQ38035.1};
GN ORFNames=CHU92_06960 {ECO:0000313|EMBL:OYQ38035.1};
OS Flavobacterium cyanobacteriorum.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=2022802 {ECO:0000313|EMBL:OYQ38035.1, ECO:0000313|Proteomes:UP000216605};
RN [1] {ECO:0000313|EMBL:OYQ38035.1, ECO:0000313|Proteomes:UP000216605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TH021 {ECO:0000313|EMBL:OYQ38035.1,
RC ECO:0000313|Proteomes:UP000216605};
RA Cai H.;
RT "Flavobacterium cyanobacteriorum sp. nov., isolated from cyanobacterial
RT aggregates in a eutrophic lake.";
RL Submitted (JUL-2017) 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}.
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:OYQ38035.1}.
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DR EMBL; NOXV01000241; OYQ38035.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A255ZAZ4; -.
DR OrthoDB; 9804197at2; -.
DR Proteomes; UP000216605; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000216605};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 134..330
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 688..879
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 950 AA; 106343 MW; 49E5F2888CDDCE25 CRC64;
MPKDTSIKCV LIIGSGPIVI GQACEFDYAG SQSARSLREE GITVILINSN PATIMTDPSM
ADHVYLKPLT TKSIIEILKA HPEIDAVLPT MGGQTALNLC LEADEKGIWS DFNVRLIGVD
INAINITEDR EQFKQLLQRI DIPAAPAKTA NSFLKGKEIA QEFGFPLVIR PSFTLGGTGA
AFVHRKEDFD ELLTRGLEAS PIHEVLIDKA LFGWKEYELE LLRDKNDNVV IICSIENMDP
MGIHTGDSIT VAPAMTLSDR TYQRMRDMAI KMMRSIGNFA GGCNVQFAVS PDEKEDIVAI
EINPRVSRSS ALASKATGYP IAKIASKLAL GYNLDELQNQ ITKSTSALFE PTLDYVIVKI
PRWNFDKFEG ADRTLGLQMK SVGEVMGIGR SFQEALHKAT QSLEIKRNGL GADGKGYKNY
EQIIDKLANP SWDRVFVIYD AIQMGIPLSR IHEITKIDMW FLKQYEELYA LEKEISTYTI
DTLPKELLRE AKQKGFADRQ IAHMMQCLES QVYNKREEMG IKRVYKLVDT CAAEFEAKTP
YYYSTFEAEI EKADGTRYVH NESIVTDKKK VVVLGSGPNR IGQGIEFDYS CVHGVLAASE
CGYETIMINC NPETVSTDFD TADKLYFEPV FWEHIYDIIR HEKPEGVIVQ LGGQTALKLA
EKLDRYGIKI LGTSFDALDL AEDRGRFSEL LSELHIPFPK FGVAESAEEA VKLADELDFP
LLVRPSYVLG GQGMKIVINK QELEEHVIDL LKNIPGNKLL LDHYLDGAIE AEADAICDGE
NVYIIGIMEH IEPCGVHSGD SNATLPPFNL GEFVMQQIKD HTKKIALALK TVGLINIQFA
IKDDTVYVIE ANPRASRTVP FIAKAYGEPY VNYATKIMLG EKKVTDFEFN PKLKGYAIKQ
PVFSFNKFPG VNKKLGPEMK STGESILFID DLKDDQFYEL YSRRKMYLSR
//
