GenomeNet

Database: UniProt
Entry: A9E774_9FLAO
LinkDB: A9E774_9FLAO
Original site: A9E774_9FLAO 
ID   A9E774_9FLAO            Unreviewed;       951 AA.
AC   A9E774;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   24-JAN-2024, entry version 75.
DE   RecName: Full=carbamoyl-phosphate synthase (glutamine-hydrolyzing) {ECO:0000256|ARBA:ARBA00012738};
DE            EC=6.3.5.5 {ECO:0000256|ARBA:ARBA00012738};
DE   AltName: Full=Carbamoyl-phosphate synthetase ammonia chain {ECO:0000256|ARBA:ARBA00030577};
GN   ORFNames=KAOT1_08694 {ECO:0000313|EMBL:EDP94878.1};
OS   Kordia algicida OT-1.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Kordia.
OX   NCBI_TaxID=391587 {ECO:0000313|EMBL:EDP94878.1, ECO:0000313|Proteomes:UP000002945};
RN   [1] {ECO:0000313|EMBL:EDP94878.1, ECO:0000313|Proteomes:UP000002945}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OT-1 {ECO:0000313|EMBL:EDP94878.1,
RC   ECO:0000313|Proteomes:UP000002945};
RX   PubMed=21622754; DOI=10.1128/JB.05241-11;
RA   Lee H.S., Kang S.G., Kwon K.K., Lee J.H., Kim S.J.;
RT   "Genome sequence of the algicidal bacterium Kordia algicida OT-1.";
RL   J. Bacteriol. 193:4031-4032(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP +
CC         carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate;
CC         Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359,
CC         ChEBI:CHEBI:456216; EC=6.3.5.5;
CC         Evidence={ECO:0000256|ARBA:ARBA00001777};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
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:EDP94878.1}.
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; ABIB01000012; EDP94878.1; -; Genomic_DNA.
DR   RefSeq; WP_007094301.1; NZ_DS544873.1.
DR   AlphaFoldDB; A9E774; -.
DR   STRING; 391587.KAOT1_08694; -.
DR   eggNOG; COG0458; Bacteria.
DR   HOGENOM; CLU_000513_1_0_10; -.
DR   OrthoDB; 9804197at2; -.
DR   Proteomes; UP000002945; 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:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
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}; Reference proteome {ECO:0000313|Proteomes:UP000002945};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          134..330
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          689..880
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   951 AA;  106628 MW;  86802235843A12A4 CRC64;
     MPKREDLKSI LIIGSGPIVI GQACEFDYSG SQALRSLRED GIETILINSN PATIMTDPSM
     ADHVYLKPLT TKSIIEVLKK HPNIDAVLPT MGGQTALNLC IEADEKGIWE DFGVKLIGVD
     IEAINITEDR EKFRELMGQI GVGMAPQATA TSFLKGKEIA QEFGFPLVIR ASYTLGGAGA
     SIVYDPEDFD ELLRRGLEAS PIHEVMIDKA MMGWKEYELE LLRDKNDNVV IICSIENMDP
     MGIHTGDSIT VAPAMTLSDR TYQKMRDMAI KMMRSIGDFE GGCNVQFAVS PDEKEEIIAI
     EINPRVSRSS ALASKATGYP IAKIAAKLAI GYSLDELDNQ ITKSTSALFE PTLDYVIVKI
     PRWNFDKFEG SDRELGLQMK AVGEVMGIGR SFQEALHKAT QSLEIKRNGL GADGKGYKNY
     DQILNKLRHA SWDRVFVIYD AIQMGIPLSR IYEITKIDMW FLKQYEELYN LEKEISSHNK
     IDSISRDLLL EAKQKGFADR QIAHMLGCWE SEVYKKREEL GIKRVYKLVD TCAAEFTAKT
     PYYYSTFEAE IETADGNRYV HNESIVTDKK KIVVLGSGPN RIGQGIEFDY CCVHGVLASA
     ECGYETIMIN CNPETVSTDF DTADKLYFEP VFWEHIYDII RHEKPEGVIV QLGGQTALKL
     AEKLDRHGIK IIGTTYQSLD LAEDRGSFST LLKENNIPYP EFGVAENADE ALALADELDF
     PILVRPSYVL GGQGMKIVIN KQELEETVVD LLRKIPNNKL LLDHYLDGAI EAEADAICDG
     ENVYIIGIME HIEPCGIHSG DSNATLPPFN LGEFVMQQIK DHTKKIALAL NTVGLINIQF
     AIKDDMVYII EANPRASRTV PFIAKAYKEP YVNYATKVML GEKKITDFDF NPQLEGYAIK
     QPVFSFNKFP NVNKRLGPEM KSTGESILFI DSLKDDDFYN LYSRRKMYLS K
//
DBGET integrated database retrieval system