ID A0A162JL92_9HYPO Unreviewed; 595 AA.
AC A0A162JL92;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 13-SEP-2023, entry version 25.
DE SubName: Full=Bifunctional purine biosynthesis protein {ECO:0000313|EMBL:OAA45908.1};
GN ORFNames=BBO_03549 {ECO:0000313|EMBL:OAA45908.1};
OS Beauveria brongniartii RCEF 3172.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria;
OC Beauveria brongniartii.
OX NCBI_TaxID=1081107 {ECO:0000313|EMBL:OAA45908.1, ECO:0000313|Proteomes:UP000076863};
RN [1] {ECO:0000313|EMBL:OAA45908.1, ECO:0000313|Proteomes:UP000076863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 3172 {ECO:0000313|EMBL:OAA45908.1,
RC ECO:0000313|Proteomes:UP000076863};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
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:OAA45908.1}.
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DR EMBL; AZHA01000008; OAA45908.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A162JL92; -.
DR OrthoDB; 275312at2759; -.
DR UniPathway; UPA00074; UER00133.
DR Proteomes; UP000076863; 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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..147
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 595 AA; 64213 MW; 11DA1F52508DCBC4 CRC64;
MASSQKIAIV SVYDKTGLLD LAKGLVAQNV RILASGGTSR MIRESGFPVE DVSAITKAPE
MLGGRVKTLH PSVHAGILAR DLESDEKDLA DQNINKVDYV VCNLYPFKET VAKVNVSIAE
AVEEVDIGGV TLIRAAAKNH KRVTILSDPS DYAGFLTELE KGEISDASRN RYALKAFEHT
ADYDTAISDF FRKEYAGAGD QYLPLRYGAN PHQKPAAAYA VEGKLPFKTL SGAPGYINLL
DALNAWPLVK ELKAATGKPA AASFKHVSPA GAAIGLPLSA DEAKVYMVAD IPGIETSSLA
QAYARARGAD RMSSFGDVIA LSDIVDVPTA SIISKEVSDG VIAPGYEDAA LELLKKKKGG
KYLVLQIDPD YNPGPTETRT VYGIHLQQHR NDVEISAAKS FSTIVTPKDG SLPANAARDL
AIATITLKYT QSNSVCYAYN GQVIGLGAGQ QSRIHCTRLA GDKADNWWMR FHQRVLGIKW
KKGAKRPDKS NAIDLLVSGQ LPKDGAEREA FEAIFEEVPA AFTQEERDAW MKQLTGVSVS
SDAFFPFIDN VFRAARSGVK YIAAPTGSQN DSAVFQTAES LGITFVEQSI RLFHH
//
