ID A0A1Z5JGP6_FISSO Unreviewed; 1517 AA.
AC A0A1Z5JGP6;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Carbamoyl-phosphate synthase {ECO:0000313|EMBL:GAX13177.1};
DE EC=6.3.4.16 {ECO:0000313|EMBL:GAX13177.1};
GN ORFNames=FisN_17Hh107 {ECO:0000313|EMBL:GAX13177.1};
OS Fistulifera solaris (Oleaginous diatom).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Bacillariophyceae; Bacillariophycidae; Naviculales; Naviculaceae;
OC Fistulifera.
OX NCBI_TaxID=1519565 {ECO:0000313|EMBL:GAX13177.1, ECO:0000313|Proteomes:UP000198406};
RN [1] {ECO:0000313|EMBL:GAX13177.1, ECO:0000313|Proteomes:UP000198406}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JPCC DA0580 {ECO:0000313|EMBL:GAX13177.1,
RC ECO:0000313|Proteomes:UP000198406};
RX PubMed=25634988; DOI=10.1105/tpc.114.135194;
RA Tanaka T., Maeda Y., Veluchamy A., Tanaka M., Abida H., Marechal E.,
RA Bowler C., Muto M., Sunaga Y., Tanaka M., Yoshino T., Taniguchi T.,
RA Fukuda Y., Nemoto M., Matsumoto M., Wong P.S., Aburatani S., Fujibuchi W.;
RT "Oil accumulation by the oleaginous diatom Fistulifera solaris as revealed
RT by the genome and transcriptome.";
RL Plant Cell 27:162-176(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 -!- 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:GAX13177.1}.
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DR EMBL; BDSP01000061; GAX13177.1; -; Genomic_DNA.
DR InParanoid; A0A1Z5JGP6; -.
DR OrthoDB; 309at2759; -.
DR Proteomes; UP000198406; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004087; F:carbamoyl-phosphate synthase (ammonia) activity; IEA:UniProtKB-EC.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01744; GATase1_CPSase; 1.
DR CDD; cd01423; MGS_CPS_I_III; 1.
DR Gene3D; 3.40.50.20; -; 2.
DR Gene3D; 3.40.50.880; -; 1.
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; 3.50.30.20; Carbamoyl-phosphate synthase small subunit, N-terminal domain; 1.
DR Gene3D; 1.10.1030.10; Carbamoyl-phosphate synthetase, large subunit oligomerisation domain; 1.
DR Gene3D; 3.40.50.1380; Methylglyoxal synthase-like domain; 1.
DR HAMAP; MF_01209; CPSase_S_chain; 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; IPR006274; CarbamoylP_synth_ssu.
DR InterPro; IPR002474; CarbamoylP_synth_ssu_N.
DR InterPro; IPR036480; CarbP_synth_ssu_N_sf.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR035686; CPSase_GATase1.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR011607; MGS-like_dom.
DR InterPro; IPR036914; MGS-like_dom_sf.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR NCBIfam; TIGR01369; CPSaseII_lrg; 1.
DR NCBIfam; TIGR01368; CPSaseIIsmall; 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 Pfam; PF00988; CPSase_sm_chain; 1.
DR Pfam; PF00117; GATase; 1.
DR Pfam; PF02142; MGS; 1.
DR PRINTS; PR00098; CPSASE.
DR PRINTS; PR00099; CPSGATASE.
DR PRINTS; PR00096; GATASE.
DR SMART; SM01096; CPSase_L_D3; 1.
DR SMART; SM01097; CPSase_sm_chain; 1.
DR SMART; SM00851; MGS; 1.
DR SUPFAM; SSF48108; Carbamoyl phosphate synthetase, large subunit connection domain; 1.
DR SUPFAM; SSF52021; Carbamoyl phosphate synthetase, small subunit N-terminal domain; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 2.
DR SUPFAM; SSF52335; Methylglyoxal synthase-like; 1.
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; PS51273; GATASE_TYPE_1; 1.
DR PROSITE; PS51855; MGS; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:GAX13177.1};
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:UP000198406};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 559..751
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1100..1291
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1362..1517
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT ACT_SITE 300
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 384
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 386
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1517 AA; 167388 MW; 9CCA8EA24608735F CRC64;
MNLAILRSAR NAIHFRKPNL RTGRAAFMST HSGDDAKRPE AVAMLHLEDG TTLVGKSFGC
HTSVEGEVVF TTGMVGYPES LTDPSYEGQI LTLTQPMVGN YGVPDRKKLD EYGLPADFES
NRIHATGLIV QNYSHHYSHW KAASSLGDWL KEEGVPGLCD IDTRMLTKKI REKGAMLGRI
EVDLNAPVPD FSKMVDPNKR HLVGEVSVKE PTVYGKGNPT KVIAVDCGMK YSIIRQLVKR
GVELTVVPWN YPFAADMHKY DGLFLSNGPG DPNMCMETVK ELEKVITCPE DQIKPIYGIC
MGNQLIGLAA GGKAVKLPFG NRGQNQPVLN HQTGECYITP QNHGYHIDTS TLKPGWKTLF
TNANDGSNEG IGHETRPYFT AQFHPEASSG PTDTEFMFDT FLDACRSKLK DGKIKFPDRK
PAPTPPKVKK VLLLGSGGTS IGQAGEFDYS GGQAIKALKE EGCEVVLMNP NIASVQTNTD
DKSTSKADHV FFLPVTPDFV EEVIKKEKPD GVVVSMGGQT ALNCAVEMYL AGTFQKYGVH
VLGTPIESVI NTEDRQLFSD RLNEINEKIA ESYTADTIDQ AVEHARKVGY PCMIRSAFAL
GGLGSGICQD EPHLKDMARK ALSVSPQILV EKSMKGWKEV EYEVVRDVYD NCVTVCNMEN
FDPLGIHTGD SIVMAPSQTL SDEEYHMLRE TAIKVVRHLG IVGECNIQYA LHPESLEYAI
IEVNARLSRS SALASKATGY PLAFVAAKLC LGIPLTEVIN SVTKKTQAAF EPSLDYIVTK
IPRWDMSKFE GVNQEIGSAM KSVGEVMGIG RTMEESIQKA LRMVDPSNPG FSMKNRYETL
SELKRELAVP TDKRIWAIAQ ALHEKSLTVS EIHDITKIDF WFLRRLEDIV KAWDEMETVT
IDELSDDLML HAKKMGYSDQ QIANCLKGAT TEMQVRQKRE AAGIVPFTKQ IDTLAAEYPA
ETNYLYMTYH GSENDVESQN GGIAVLGSGC YRIGSSIEFD WCGVSAIRTL RKMGYKSTMI
NYNPETVSTD YDECDRLYFE ELSVERVMDI YKRDKTEGVV VSVGGQIPNG IALNLDKNGV
KILGTPAAMI DNAEDRFKFS DMIDEIGVQQ PAWRELTSTQ SAIDFASKVG YPVLVRPSYV
LSGAAMNVAY SDEQLRSCLN EAAEVSQEHP VVISDFIQGA TEIEMDGVGK DGELIAAAIH
EHIENAGVHS GDATLVLPPH TLSAYTKERV RDAARKIVKR LNITGPVNIQ FVAKGTDVMC
IECNVRASRS FPFVSKTMGV DFIEAATKAI VGVDTSDMNL PTLDTRDRPN GYVGVKAPMF
SFARLRGSDP VLGVEMASTG EVACFGANKE EAFLKALLST GFKLPKKNIL VSVQEDLQDE
FTHCAWQLHE LGYNLYATRS TAAVLEKNRV PCTAVPYPTE ESDEANAAEL IKNGTINLVI
NVPSQNSKRL EDNFLMRRTA MDFGAPLLTN MNLVKMFTDS MYKYRKEGMA GLEPKTLFEH
YQAESDADAW TSPSEFH
//
