ID A0A1Z5T578_HORWE Unreviewed; 598 AA.
AC A0A1Z5T578;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 13-SEP-2023, entry version 17.
DE SubName: Full=Bifunctional purine biosynthesis protein ADE16 {ECO:0000313|EMBL:OTA31169.1};
GN ORFNames=BTJ68_08513 {ECO:0000313|EMBL:OTA31169.1};
OS Hortaea werneckii EXF-2000.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Hortaea.
OX NCBI_TaxID=1157616 {ECO:0000313|EMBL:OTA31169.1, ECO:0000313|Proteomes:UP000194280};
RN [1] {ECO:0000313|EMBL:OTA31169.1, ECO:0000313|Proteomes:UP000194280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-2000 {ECO:0000313|EMBL:OTA31169.1,
RC ECO:0000313|Proteomes:UP000194280};
RA Sinha S., Flibotte S., Neira M., Lenassi M., Gostincar C., Stajich J.E.,
RA Nislow C.E.;
RT "The recent genome duplication of the halophilic yeast Hortaea werneckii:
RT insights from long-read sequencing.";
RL Submitted (JAN-2017) 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:OTA31169.1}.
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DR EMBL; MUNK01000120; OTA31169.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z5T578; -.
DR STRING; 1157616.A0A1Z5T578; -.
DR VEuPathDB; FungiDB:BTJ68_08513; -.
DR InParanoid; A0A1Z5T578; -.
DR OrthoDB; 275312at2759; -.
DR UniPathway; UPA00074; UER00133.
DR Proteomes; UP000194280; 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:UP000194280};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..149
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 598 AA; 65508 MW; C6A3C8A92E79B4F4 CRC64;
MASEQPQKIA ILSVYDKTGL LDLAKGLVKQ NIRLLASGGT SKLIREAGFP VEDVSAITKA
PEMLAGRVKT LHPAVHAGIL ARDLASDEKD LAEQNIDKVD YVICNLYPFK DTVAKINVTI
PEAVEEIDIG GVTLIRAAAK NHTRVTILSD PNDYHDFLQE LEKGEVPEKS KQLYALKAFT
HTADYDSAIS DFFRKKYAGD GLQQLPLRYG TNPHQKPASA YMTDRPLPFK ALNGSPGYVN
LLDALNAWNL VKELSEALDF PAAASFKHVS PAGAAIGVPL SDVEKKVYMV EDIEGLESSG
LAQAYARARG ADRMSSFGDV IALSHEVDVA TAKIIGKEVS DGVVAPGFQP EALEILSKKK
GGKYLVLQMD KAYTPPAQES RTIFGVNLTQ HRNDATITPH NTFNSIIVPK ESAPLPESAL
RDMTVATIAL KFTQSNSVCY ALNGQVIGLG AGQQSRIHCT RLAGDKADNW WMRFHSRALN
VKWRKGAKRA DKSNAIDLLC SGIVQDSGPE REDWEKNFEE APQPFTQEER KAWLSKMGEV
AVSSDAFFPF TDNVYRVARS GVKYIAAPVG SQNDQACFET AEKLGITFVE QHVRLFHH
//
