ID A0A0G2HZ66_9PEZI Unreviewed; 599 AA.
AC A0A0G2HZ66;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 13-SEP-2023, entry version 25.
DE SubName: Full=Putative bifunctional purine biosynthesis protein {ECO:0000313|EMBL:KKY39923.1};
GN ORFNames=UCDDA912_g00076 {ECO:0000313|EMBL:KKY39923.1};
OS Diaporthe ampelina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX NCBI_TaxID=1214573 {ECO:0000313|EMBL:KKY39923.1, ECO:0000313|Proteomes:UP000034680};
RN [1] {ECO:0000313|EMBL:KKY39923.1, ECO:0000313|Proteomes:UP000034680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA912 {ECO:0000313|EMBL:KKY39923.1};
RA Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT "Distinctive expansion of gene families associated with plant cell wall
RT degradation and secondary metabolism in the genomes of grapevine trunk
RT pathogens.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY39923.1, ECO:0000313|Proteomes:UP000034680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA912 {ECO:0000313|EMBL:KKY39923.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAY-2015) 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:KKY39923.1}.
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DR EMBL; LCUC01000006; KKY39923.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2HZ66; -.
DR STRING; 1214573.A0A0G2HZ66; -.
DR OrthoDB; 275312at2759; -.
DR UniPathway; UPA00074; UER00133.
DR Proteomes; UP000034680; 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:UP000034680};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 3..152
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 599 AA; 65333 MW; 02DDA2A496CC3676 CRC64;
MATQKESAGQ RIAIVSVYDK TGLLDLAKGL IQQNVRILAS GGTSKMIRES GFPVEDISAI
TKAPEMLAGR VKTLHPAVHA GILARNLASD EKDLAEQSID KVDYVICNLY PFKDTVAKIN
VTVPEAVEEI DIGGVTLIRA AAKNHSRVTI LSDPADYAEF LKELEVGEVK ESSRRLYALK
AFEHTADYDA AISDFFRKQY AADGLQYMAL RYGANPHQKP AASYVKEGKL PFKVLGGAPG
YINLLDALNS WPLVKELKRA LGKPAAASFK HVSPAGAAIG LPLTAEEKKV YFVEDIPGID
ESGLAQAYAR ARGADRMSSF GDFIALSDVV DVATASIISK EVSDGVIAPG YEDAALEILR
KKKGGKYLVL QMDPEFEPNP KETRTVYGIT LAQQRNDFEI SPKSFNTVIT PKDANVPEDA
LRDLTIATIA LKYTQSNSVC YAARGQVVGL GAGQQSRIHC TRLAGDKADN WWLRFHPRVL
GIKWKKGTKR PDKSNAIDLL VSGQLPKDGP EREAFEATFD GVPKAFTPEE REEWLGKLTD
VAVSSDAFFP FTDNVYRAAK SGAKYIAAPG GSQNDQPVFE TAENLGITFI EQNIRLFHH
//