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Database: UniProt
Entry: T1K7X0_TETUR
LinkDB: T1K7X0_TETUR
Original site: T1K7X0_TETUR 
ID   T1K7X0_TETUR            Unreviewed;       593 AA.
AC   T1K7X0;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   RecName: Full=Bifunctional purine biosynthesis protein ATIC {ECO:0000256|ARBA:ARBA00017905};
DE            EC=2.1.2.3 {ECO:0000256|ARBA:ARBA00012253};
DE            EC=3.5.4.10 {ECO:0000256|ARBA:ARBA00012712};
DE   AltName: Full=AICAR transformylase/inosine monophosphate cyclohydrolase {ECO:0000256|ARBA:ARBA00032307};
GN   Name=107361202 {ECO:0000313|EnsemblMetazoa:tetur06g05840.1};
OS   Tetranychus urticae (Two-spotted spider mite).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Acariformes; Trombidiformes; Prostigmata; Eleutherengona; Raphignathae;
OC   Tetranychoidea; Tetranychidae; Tetranychus.
OX   NCBI_TaxID=32264 {ECO:0000313|EnsemblMetazoa:tetur06g05840.1, ECO:0000313|Proteomes:UP000015104};
RN   [1] {ECO:0000313|Proteomes:UP000015104}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=London {ECO:0000313|Proteomes:UP000015104};
RA   Rombauts S.;
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:tetur06g05840.1}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JUN-2015) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D-
CC         ribosyl)imidazole-4-carboxamide = (6S)-5,6,7,8-tetrahydrofolate + 5-
CC         formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide;
CC         Xref=Rhea:RHEA:22192, ChEBI:CHEBI:57453, ChEBI:CHEBI:58467,
CC         ChEBI:CHEBI:58475, ChEBI:CHEBI:195366; EC=2.1.2.3;
CC         Evidence={ECO:0000256|ARBA:ARBA00035778};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22193;
CC         Evidence={ECO:0000256|ARBA:ARBA00035778};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=10-formyldihydrofolate + 5-amino-1-(5-phospho-beta-D-
CC         ribosyl)imidazole-4-carboxamide = 5-formamido-1-(5-phospho-D-
CC         ribosyl)imidazole-4-carboxamide + 7,8-dihydrofolate;
CC         Xref=Rhea:RHEA:59144, ChEBI:CHEBI:57451, ChEBI:CHEBI:57452,
CC         ChEBI:CHEBI:58467, ChEBI:CHEBI:58475;
CC         Evidence={ECO:0000256|ARBA:ARBA00000945};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59145;
CC         Evidence={ECO:0000256|ARBA:ARBA00000945};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + IMP = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-
CC         carboxamide; Xref=Rhea:RHEA:18445, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:58053, ChEBI:CHEBI:58467; EC=3.5.4.10;
CC         Evidence={ECO:0000256|ARBA:ARBA00001252};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18447;
CC         Evidence={ECO:0000256|ARBA:ARBA00001252};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC       formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-
CC       1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route):
CC       step 1/1. {ECO:0000256|ARBA:ARBA00004954}.
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; IMP
CC       from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide: step
CC       1/1. {ECO:0000256|ARBA:ARBA00004844}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000256|ARBA:ARBA00004514}.
CC   -!- SIMILARITY: Belongs to the PurH family.
CC       {ECO:0000256|ARBA:ARBA00007667}.
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DR   EMBL; CAEY01001813; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_015783455.1; XM_015927969.1.
DR   RefSeq; XP_015783456.1; XM_015927970.1.
DR   AlphaFoldDB; T1K7X0; -.
DR   STRING; 32264.T1K7X0; -.
DR   EnsemblMetazoa; tetur06g05840.1; tetur06g05840.1; tetur06g05840.
DR   GeneID; 107361202; -.
DR   eggNOG; KOG2555; Eukaryota.
DR   HOGENOM; CLU_016316_3_2_1; -.
DR   OMA; WRVAKFV; -.
DR   OrthoDB; 275312at2759; -.
DR   UniPathway; UPA00074; UER00133.
DR   Proteomes; UP000015104; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0003937; F:IMP cyclohydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004643; F:phosphoribosylaminoimidazolecarboxamide formyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd01421; IMPCH; 1.
DR   Gene3D; 1.10.287.440; -; 1.
DR   Gene3D; 3.40.140.20; -; 2.
DR   Gene3D; 3.40.50.1380; Methylglyoxal synthase-like domain; 1.
DR   HAMAP; MF_00139; PurH; 1.
DR   InterPro; IPR024051; AICAR_Tfase_dup_dom_sf.
DR   InterPro; IPR024050; AICAR_Tfase_insert_dom_sf.
DR   InterPro; IPR016193; Cytidine_deaminase-like.
DR   InterPro; IPR011607; MGS-like_dom.
DR   InterPro; IPR036914; MGS-like_dom_sf.
DR   InterPro; IPR002695; PurH-like.
DR   NCBIfam; TIGR00355; purH; 1.
DR   PANTHER; PTHR11692:SF0; BIFUNCTIONAL PURINE BIOSYNTHESIS PROTEIN ATIC; 1.
DR   PANTHER; PTHR11692; BIFUNCTIONAL PURINE BIOSYNTHESIS PROTEIN PURH; 1.
DR   Pfam; PF01808; AICARFT_IMPCHas; 1.
DR   Pfam; PF02142; MGS; 1.
DR   PIRSF; PIRSF000414; AICARFT_IMPCHas; 1.
DR   SMART; SM00798; AICARFT_IMPCHas; 1.
DR   SMART; SM00851; MGS; 1.
DR   SUPFAM; SSF53927; Cytidine deaminase-like; 1.
DR   SUPFAM; SSF52335; Methylglyoxal synthase-like; 1.
DR   PROSITE; PS51855; MGS; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015104};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..147
FT                   /note="MGS-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51855"
SQ   SEQUENCE   593 AA;  65097 MW;  B1834D8F47AE5A3C CRC64;
     MSIKGELAVI SVWDKRGLVE FARRLAQSGL NLVASGGSAK TLRDNGLTLK DVSEITGAPE
     MLGGRVKTLH PAIHGGILAR KIDSDQRDMK NRGYQFIGVV VCNLYPFVQT ISSPNVTIAD
     AVEQVDIGGV TLLRAGAKNH DRVAVICDPN DYDLVASEIE RNGVVSKEVR QMLAVKAFNH
     TAQYDLAISN YFRSQYCSGV SQLSLRYGMN PHQKPAQLYT MEAKLPLRVV NGSPGFINLC
     DALNAWQLVR DLKKALNMPA ATSFKHVSPA GAAVGVPLSG AQLKLCCVED MAKDLTPLAT
     AYARARGADR MSSFGDFVAL SDVCDVPTAK IISREVSDGI IAPGYQEEAL NILKKKKGGS
     YCVLEIDPNY EPSDIESRTL FGLTLEQKRN DAIIDEKLFN VDRIISQNKN LPKEAVRDLV
     VATIALKYTQ SNSVCYAKDG QIIGIGAGQQ SRIHCTRLAG DKANNWWMRQ HPSLSEMVFK
     KSIKRAEQSN YTDVYVNRQV GLEMDLQKWK EAFEVAPPLL TEEKANDWIK EMKGVALSSD
     AFFPFRDNID RAAMSGVSYV ASPGGSTNDQ CVIEACNDHN MVLVHTGLRL FHH
//
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