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}.
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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
//