ID A0A196SEJ8_BLAHN Unreviewed; 614 AA.
AC A0A196SEJ8;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 13-SEP-2023, entry version 24.
DE SubName: Full=Phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase {ECO:0000313|EMBL:OAO14741.1};
GN ORFNames=AV274_3444 {ECO:0000313|EMBL:OAO14741.1};
OS Blastocystis sp. subtype 1 (strain ATCC 50177 / NandII).
OC Eukaryota; Sar; Stramenopiles; Bigyra; Opalozoa; Opalinata; Blastocystidae;
OC Blastocystis.
OX NCBI_TaxID=478820 {ECO:0000313|EMBL:OAO14741.1, ECO:0000313|Proteomes:UP000078348};
RN [1] {ECO:0000313|EMBL:OAO14741.1, ECO:0000313|Proteomes:UP000078348}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50177 / NandII {ECO:0000313|Proteomes:UP000078348};
RA Gentekaki E., Curtis B., Stairs C., Eme L., Herman E., Klimes V.,
RA Arias M.C., Elias M., Hilliou F., Klute M., Malik S.-B., Pightling A.,
RA Rachubinski R., Salas D., Schlacht A., Suga H., Archibald J., Ball S.G.,
RA Clark G., Dacks J., Van Der Giezen M., Tsaousis A., Roger A.;
RT "Nuclear genome of Blastocystis sp. subtype 1 NandII.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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:OAO14741.1}.
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DR EMBL; LXWW01000210; OAO14741.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A196SEJ8; -.
DR STRING; 478820.A0A196SEJ8; -.
DR OrthoDB; 275312at2759; -.
DR UniPathway; UPA00074; UER00133.
DR Proteomes; UP000078348; 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, ECO:0000313|EMBL:OAO14741.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW Reference proteome {ECO:0000313|Proteomes:UP000078348};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OAO14741.1}.
FT DOMAIN 13..160
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 614 AA; 67312 MW; 94A7A62FDEFD0384 CRC64;
MAHTITAVQG TTQSLFKINR AILSVSDKTG LVDLAKFLES YGVEILSTGG TAKAMRDAGV
KVMDVSEYTG APEMMDGRVK TLHPKVHGGI LAVRGNAKHE QDMKDNGIKM IDLVVLNLYA
FEDTVAKGYN FETCIENIDI GGPSMLRSSA KNHAAVVICS SPAQYPALME EMKTHDGCTT
IELRRRFAAE AFALSAKYDA AISSWFAKQL NPEQKTDVIV TRPYLPVREL KYGVNPHQKP
AGLYRHLNGE LPFEIVHGNP GYINLCDALN SWMLVKEARQ ALGAPAAASF KHVSPAGAAI
AVPLTEEEMK AYEVTDASMS GAALAYLRAR NADPMSSFGD FAAISEVVDV PAAKYISTCI
SDGIIAAGYE PEALEILKKK KNGNFIILQG KVDFAMPAME YRELHGAVLA QRHNDVIPSK
EQMTNVVTEN KEIPESAMND MVLGNICLKY TQSNSVGYAL NGQMIGVGAG QQSRIDCVKL
AARKAAMWYL RQHPKVLGLQ FKKGVKKQDR VNARVRYIEG DFTEVEYEQW KTLFEVVPEP
LTQAEKDEFI KTMHDVALVS DAFFPFRDNI DQASKYGVKY IAQPGGSIQD AGVTEAANSY
GMAMVHTGLR LFHH
//
