ID V6SEK1_9FLAO Unreviewed; 950 AA.
AC V6SEK1;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Carbamoyl phosphate synthase large subunit {ECO:0000313|EMBL:KGO93973.1};
GN ORFNames=Q767_13585 {ECO:0000313|EMBL:KGO93973.1};
OS Flavobacterium enshiense DK69.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1107311 {ECO:0000313|EMBL:KGO93973.1, ECO:0000313|Proteomes:UP000030149};
RN [1] {ECO:0000313|Proteomes:UP000030149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DK69 {ECO:0000313|Proteomes:UP000030149};
RA Zeng Z., Chen C.;
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KGO93973.1, ECO:0000313|Proteomes:UP000030149}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DK69 {ECO:0000313|EMBL:KGO93973.1,
RC ECO:0000313|Proteomes:UP000030149};
RX PubMed=26561515; DOI=10.1186/s40793-015-0084-z;
RA Zeng Z., Chen C., Du H., Wang G., Li M.;
RT "High quality draft genomic sequence of Flavobacterium enshiense DK69(T)
RT and comparison among Flavobacterium genomes.";
RL Stand. Genomic Sci. 10:92-92(2015).
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:KGO93973.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JRLZ01000017; KGO93973.1; -; Genomic_DNA.
DR RefSeq; WP_023573726.1; NZ_JRLZ01000017.1.
DR AlphaFoldDB; V6SEK1; -.
DR STRING; 1107311.Q767_13585; -.
DR PATRIC; fig|1107311.3.peg.1704; -.
DR eggNOG; COG0458; Bacteria.
DR OrthoDB; 9804197at2; -.
DR Proteomes; UP000030149; 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:UP000030149};
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; 105991 MW; D43225A797A810E5 CRC64;
MPKDTSIKSV LIIGSGPIVI GQACEFDYSG SQSARSLREE GIEVILINSN PATIMTDPSM
ADHIYLKPLT TKSIIEILKA HPQIDAVLPT MGGQTALNLC LEADEKGIWT DFGVRLIGVD
VNAINITEDR EQFKQLLEKI EIPVAPAKTA NSFLKGKEIA QEFGFPLVIR PSFTLGGTGA
AFVHKKEDFD DLLTRGLEAS PIHEVLIDKA LLGWKEYELE LLRDKNDNVV IICTIENMDP
MGIHTGDSIT VAPAMTLSDR TFQRMRDMAI LMMRSIGNFA GGCNVQFAVS PDEKEDIVAI
EINPRVSRSS ALASKATGYP IAKIATKLAL GYSLDELQNQ ITKSTSALFE PTLDYVIVKI
PRWNFDKFEG ADRTLGLQMK SVGEVMGIGR SFQEALHKAT QSLEIKRNGL GADGKGYTNF
DQIIDKLTHA SWDRVFVIYD AIAMGIPLSR IHEITKIDMW FLKQYEELYI LEKEVSKYKI
DTLPKELLLE AKQKGFADRQ IAHMMNCLES QVYNLREQMG VNRVYKLVDT CAAEFKAQTP
YYYSTFEAEI EKADGTRYVD NESIVTDKKK VIVLGSGPNR IGQGIEFDYS CVHGVLAAAE
CGYETIMINC NPETVSTDFD TADKLYFEPV FWEHIYDIIR HEKPEGVIVQ LGGQTALKLA
EKLSKYGIKI LGTSYDALDL AEDRGRFSDL LTELHIPFPK YGIAESAEEA SILADKLDFP
LLVRPSYVLG GQGMKIVINK QELEEHVIDL LKSIPGNKLL LDHYLDGAIE AEADAICDGE
NVYIIGIMEH IEPCGVHSGD SNATLPPFNI GEFVMQQIKD HTKKIALALK TVGLINIQFA
IKDDIVYIIE ANPRASRTVP FIAKAYGEPY VNYATKVMLG HNKVTDFNFN PQLKGFAIKQ
PVFSFSKFKN VNKALGPEMK STGESILFID DLKDDQFYEL YSRRKMYLSK
//
