ID A0A1B8DA47_9PEZI Unreviewed; 1360 AA.
AC A0A1B8DA47;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=phosphoribosylformylglycinamidine synthase {ECO:0000256|ARBA:ARBA00012747};
DE EC=6.3.5.3 {ECO:0000256|ARBA:ARBA00012747};
DE AltName: Full=Formylglycinamide ribonucleotide amidotransferase {ECO:0000256|ARBA:ARBA00032632};
DE AltName: Full=Formylglycinamide ribotide amidotransferase {ECO:0000256|ARBA:ARBA00029823};
GN ORFNames=VE04_04003 {ECO:0000313|EMBL:OBT55881.1};
OS Pseudogymnoascus sp. 24MN13.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1622150 {ECO:0000313|EMBL:OBT55881.1, ECO:0000313|Proteomes:UP000092157};
RN [1] {ECO:0000313|EMBL:OBT55881.1, ECO:0000313|Proteomes:UP000092157}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=24MN13 {ECO:0000313|EMBL:OBT55881.1,
RC ECO:0000313|Proteomes:UP000092157};
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Comparative genomics of Pseudogymnoascus destructans, the fungus causing
RT white-nose syndrome of bats.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000092157}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=24MN13 {ECO:0000313|Proteomes:UP000092157};
RX PubMed=29295979; DOI=10.1038/s41467-017-02441-z;
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Extreme sensitivity to ultraviolet light in the fungal pathogen causing
RT white-nose syndrome of bats.";
RL Nat. Commun. 9:35-35(2018).
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-
CC phospho-D-ribosyl)glycinamide: step 1/2.
CC {ECO:0000256|ARBA:ARBA00004920}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the FGAMS family.
CC {ECO:0000256|ARBA:ARBA00008608}.
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DR EMBL; KV456161; OBT55881.1; -; Genomic_DNA.
DR STRING; 1622150.A0A1B8DA47; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000092157; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01740; GATase1_FGAR_AT; 1.
DR CDD; cd02203; PurL_repeat1; 1.
DR CDD; cd02204; PurL_repeat2; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 1.10.8.750; Phosphoribosylformylglycinamidine synthase, linker domain; 1.
DR Gene3D; 3.90.650.10; PurM-like C-terminal domain; 2.
DR Gene3D; 3.30.1330.10; PurM-like, N-terminal domain; 2.
DR HAMAP; MF_00419; PurL_1; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR040707; FGAR-AT_N.
DR InterPro; IPR010073; PurL_large.
DR InterPro; IPR041609; PurL_linker.
DR InterPro; IPR010918; PurM-like_C_dom.
DR InterPro; IPR036676; PurM-like_C_sf.
DR InterPro; IPR036921; PurM-like_N_sf.
DR InterPro; IPR036604; PurS-like_sf.
DR NCBIfam; TIGR01735; FGAM_synt; 1.
DR PANTHER; PTHR10099; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; 1.
DR PANTHER; PTHR10099:SF1; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; 1.
DR Pfam; PF02769; AIRS_C; 2.
DR Pfam; PF18072; FGAR-AT_linker; 1.
DR Pfam; PF18076; FGAR-AT_N; 1.
DR Pfam; PF13507; GATase_5; 1.
DR SMART; SM01211; GATase_5; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF109736; FGAM synthase PurL, linker domain; 1.
DR SUPFAM; SSF56042; PurM C-terminal domain-like; 2.
DR SUPFAM; SSF55326; PurM N-terminal domain-like; 2.
DR SUPFAM; SSF82697; PurS-like; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW ECO:0000256|PROSITE-ProRule:PRU00605};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW Reference proteome {ECO:0000313|Proteomes:UP000092157}.
FT DOMAIN 39..159
FT /note="Phosphoribosylformylglycinamidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18076"
FT DOMAIN 183..232
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 445..597
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT DOMAIN 882..995
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT ACT_SITE 1193
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1321
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1323
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1360 AA; 147825 MW; 7CE75A821A986030 CRC64;
MEYLTLLGED AYTSSSARKI QDLIAKTSSA KVDEVSAVYI HYARLKQATN DVAKETDAKL
RQLLPNPRPD FFREVSGPSA ANFKVYYVTP RNISPWSSKA TSIAAVCGVK SLERIERGRA
ILVKFAEPFE GSDDSFKHVL FDRMTENISS SEPDVKGMFA EGQRIPLEVV DIFAEGANPI
DILKGYNKER GLALDEPEME YLIQAYSKIG RSPYDVELFM FAQVNSEHCR HKQFNANWTI
DDVPMGKSLF EMIKNTHKNN PKWTVSAYSD NAAVLEGNFA SFWAPDYNTG SWKATKEMVH
YIIKVETHNH PTAISPFAGA ATGSGGEIRD EGAVGRGSQP KAGLCGFWVS DLLIPDFEQP
WEIDFGKPAH YASSLDIMLE APIGSARFNN EFGRPCLTGC FRTLLTDTGS NDAEDYRGYH
KPIMIAGGVG TVRPQFAIKR QGDVKPGAHV IVLGGPAMLI GLGGGAASSN ASGEGSAELD
FDSVQRGNPE IERRAQMVIN ACCALNDANP IAMIHDVGAG GLSNALPELV KDAGYGGRFE
LRQIESADSS MSPLQIWCCE AQERYVLCVN EEGLNKFVNI CNRERCGFSD VGSVTGTIGG
NESTLVVTDR EGNEYPKPID LPMTTLFPRD RKLERNVKTK KNNLKAFDSF QSLCSLKTTK
SCRGSAEFLH RAMEIVLKVP AVGSKAFLIT IGDRTVGGMT TRDQMVGPWQ TPVADVAVTI
TSLATGGIQT GEAMAVGEKP ALALISPAAS SRMAVAESLL NLAAADIQGG LDRVRLSANW
MAAVNHEGEG SALYEAVQAI GMDMCPKLGI SIPVGKDSTS MKASWKDSSN GESKSVTAPV
TVVISAFAPV QRVSHTWTPA LRRLEDVGET VLMFVDLAQG KQAMGGSAFA QACGQLGNES
PDVHDVDLIA DYFDAVTQLH ESGIVLAYHD RSDGGLFTTI VEMMFAGRCG AEIMLDGVAK
SDETGDVLDA LFNEELGAVF QVKKSDEINF IRCFATCGPP PGLVKKIGRI PAATKQELSI
RYKAETVTHL DRSTMQEWWS STSYQMQRLR DNPASADSEY ALIKDMNDPG LSYNLTFDPK
ESILPMTTLL SSPFIKAPRV AILREQGVNG YAEMAFAFKA AGFDAIDVHM TDIIGGRSLA
DFVGIAACGG FSYGDVLGAG QGWAKSILMH EENARPEFKK FFERKDTFAL GVCNGCQMLS
RLSELIPGAE NWPIFVDNES QQFEGRVSML QIKDNSENPS VFFHGMDGSS LPIVVSHGEG
RAQFKNNTDL EALTAAGLVP IRYTDNYGKV TEKYPLNPNG SAQGIAGVTS RDGRVLAMMP
HPERSIMASV GSYIPDGMTE EWGEYGPWVR MFKSARRWVG
//
