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Database: UniProt
Entry: I1HFW7_BRADI
LinkDB: I1HFW7_BRADI
Original site: I1HFW7_BRADI 
ID   I1HFW7_BRADI            Unreviewed;       605 AA.
AC   I1HFW7;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   RecName: Full=CTP synthase {ECO:0000256|RuleBase:RU810713};
DE            EC=6.3.4.2 {ECO:0000256|RuleBase:RU810713};
DE   AltName: Full=UTP--ammonia ligase {ECO:0000256|RuleBase:RU810713};
GN   Name=100845896 {ECO:0000313|EnsemblPlants:KQK04626};
GN   ORFNames=BRADI_2g14730v3 {ECO:0000313|EMBL:KQK04626.1};
OS   Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX   NCBI_TaxID=15368 {ECO:0000313|EMBL:KQK04626.1};
RN   [1] {ECO:0000313|EMBL:KQK04626.1, ECO:0000313|EnsemblPlants:KQK04626}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bd21 {ECO:0000313|EMBL:KQK04626.1,
RC   ECO:0000313|EnsemblPlants:KQK04626};
RX   PubMed=20148030; DOI=10.1038/nature08747;
RG   International Brachypodium Initiative;
RT   "Genome sequencing and analysis of the model grass Brachypodium
RT   distachyon.";
RL   Nature 463:763-768(2010).
RN   [2] {ECO:0000313|EMBL:KQK04626.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Bd21 {ECO:0000313|EMBL:KQK04626.1};
RG   The International Brachypodium Initiative;
RA   Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D.,
RA   Barry K., Shu S., Lindquist E., Wang M., Pitluck S., Vogel J.P.,
RA   Garvin D.F., Mockler T.C., Schmutz J., Rokhsar D., Bevan M.W.;
RT   "WGS assembly of Brachypodium distachyon.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblPlants:KQK04626}
RP   IDENTIFICATION.
RC   STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQK04626};
RG   EnsemblPlants;
RL   Submitted (AUG-2018) to UniProtKB.
CC   -!- FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with
CC       either L-glutamine or ammonia as the source of nitrogen.
CC       {ECO:0000256|RuleBase:RU810713}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + L-glutamine + UTP = ADP + CTP + 2 H(+) + L-
CC         glutamate + phosphate; Xref=Rhea:RHEA:26426, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:37563, ChEBI:CHEBI:43474, ChEBI:CHEBI:46398,
CC         ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.4.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00000314,
CC         ECO:0000256|RuleBase:RU810713};
CC   -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway;
CC       CTP from UDP: step 2/2. {ECO:0000256|ARBA:ARBA00005171,
CC       ECO:0000256|RuleBase:RU810713}.
CC   -!- SIMILARITY: Belongs to the CTP synthase family.
CC       {ECO:0000256|ARBA:ARBA00007533, ECO:0000256|RuleBase:RU810713}.
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DR   EMBL; CM000881; KQK04626.1; -; Genomic_DNA.
DR   RefSeq; XP_003567802.1; XM_003567754.3.
DR   AlphaFoldDB; I1HFW7; -.
DR   STRING; 15368.I1HFW7; -.
DR   MEROPS; C26.964; -.
DR   EnsemblPlants; KQK04626; KQK04626; BRADI_2g14730v3.
DR   GeneID; 100845896; -.
DR   Gramene; KQK04626; KQK04626; BRADI_2g14730v3.
DR   KEGG; bdi:100845896; -.
DR   eggNOG; KOG2387; Eukaryota.
DR   HOGENOM; CLU_011675_5_0_1; -.
DR   InParanoid; I1HFW7; -.
DR   OMA; MTEWSAR; -.
DR   OrthoDB; 166427at2759; -.
DR   UniPathway; UPA00159; UER00277.
DR   Proteomes; UP000008810; Chromosome 2.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003883; F:CTP synthase activity; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR   GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006241; P:CTP biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0019856; P:pyrimidine nucleobase biosynthetic process; IBA:GO_Central.
DR   CDD; cd03113; CTPS_N; 1.
DR   CDD; cd01746; GATase1_CTP_Synthase; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_01227; PyrG; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR004468; CTP_synthase.
DR   InterPro; IPR017456; CTP_synthase_N.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR033828; GATase1_CTP_Synthase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR00337; PyrG; 1.
DR   PANTHER; PTHR11550; CTP SYNTHASE; 1.
DR   PANTHER; PTHR11550:SF21; CTP SYNTHASE; 1.
DR   Pfam; PF06418; CTP_synth_N; 1.
DR   Pfam; PF00117; GATase; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU810713};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW   ECO:0000256|PROSITE-ProRule:PRU00605};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU810713};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU810713};
KW   Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975,
KW   ECO:0000256|RuleBase:RU810713};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008810}.
FT   DOMAIN          2..272
FT                   /note="CTP synthase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06418"
FT   DOMAIN          310..543
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   REGION          560..605
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        564..596
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        398
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        525
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        527
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   605 AA;  66154 MW;  045E00168B995860 CRC64;
     MKYVLVTGGV VSGLGKGVTA SSIGVVLKAC GLRITSIKID PYLNTDAGTM SPFEHGEVFV
     LDDGGEVDLD LGNYERFLDI KLTRDNNITT GKIYQSVLEK ERKGEYLGKT VQVVPHITNA
     IQDWIERVAA VPVDGKEGPA DVCVIELGGT IGDIESMPFI EALGQFSYRV GAGNFCLVHV
     SLVPVLNVVG EQKTKPTQHS VRGLRGLGLT PNILACRSTK ELEENVKDKL SQFCHVPAAN
     IFTLYDVSNI WRIPLLLRDQ NAHNAILNVL NLGSAVREPK LEEWVARATL YDTLQDKVRI
     AMVGKYTGLS DSYLSVLKAL LHASVFCHRK LVVDWVASAD LEDSTATEAP DAYNTAWSLL
     RGADGVLVPG GFGDRGVKGK ILAAQYAREN NVPYLGICLG MQLAVVEFAR HVMNFPDADS
     TEFDPNTKTP CVIFMPEGSK THMGGTMRLG SRRTFFKVTD CKSAKLYGNV NYVDERHRHR
     YEVNPDMVPI FENAGLKFVG KDETGRRMEI IEMPDHRFFI GVQFHPEFKS TPSKPSAPFV
     GLIAASSGQL DQVLEDSCNG HTAADKHRPS NGSLTPQEHQ NGHTKKQANG VANGTCHANG
     NGMHH
//
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