ID A0A2C9JW90_BIOGL Unreviewed; 530 AA.
AC A0A2C9JW90;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=106070536 {ECO:0000313|EnsemblMetazoa:BGLB008997-PB};
OS Biomphalaria glabrata (Bloodfluke planorb) (Freshwater snail).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Panpulmonata; Hygrophila; Lymnaeoidea;
OC Planorbidae; Biomphalaria.
OX NCBI_TaxID=6526 {ECO:0000313|EnsemblMetazoa:BGLB008997-PB, ECO:0000313|Proteomes:UP000076420};
RN [1] {ECO:0000313|EnsemblMetazoa:BGLB008997-PB}
RP IDENTIFICATION.
RC STRAIN=BB02 {ECO:0000313|EnsemblMetazoa:BGLB008997-PB};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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 RefSeq; XP_013085916.1; XM_013230462.1.
DR AlphaFoldDB; A0A2C9JW90; -.
DR STRING; 6526.A0A2C9JW90; -.
DR EnsemblMetazoa; BGLB008997-RB; BGLB008997-PB; BGLB008997.
DR KEGG; bgt:106070536; -.
DR VEuPathDB; VectorBase:BGLB008997; -.
DR OrthoDB; 275312at2759; -.
DR UniPathway; UPA00074; UER00133.
DR Proteomes; UP000076420; 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 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 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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..87
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 530 AA; 57713 MW; CCEE3E123F602E56 CRC64;
MLGGRVKTLH PAVHGGILSR LREEDQADMK ERGYKMIKIV VCNLYPFSQT VASPNVSVED
AVEQIDIGGV TLLRAGAKNH SRVSVICDPQ DYQKVIDEIS ASPQKDTSLE TRKKLAVKAF
NHTAGYDAAI SDYFRRQYCA GESQLTLKYG MNPHQAPAQI YTTLPELPLK VVNGGPGFIN
LCDALNAWQL VSDLKRALGL PAATSFKHVS PAGAAVGTAL SPVEAKLCMV DDLKDLSPLA
IAYAKARGAD RMSSFGDFIA LSDVCDVPTA KIINREVSDG VVAPGYEPQA LEILKQKKGG
AYCVLQIDPS YVPPLMEART LFGLQLEQRR NDAVIDKDLF TNIVSKRNEL PEEAVRDLIV
ATVALKYTQS NSVCYAKDGQ VIGIGAGQQS RIHCTRLAGD KANNWWLRQH PKVLGMKFKK
GVKRADIANA IDGYVLDTIG QDLAAFENLL ENPPSPLTDA ERKEWISQMS GVSLSSDAFF
PFRDSVDRAV KSGVEYIASP AGSVGDQSVI AASDEHNVVL IHTKLRLFHH
//