ID B8MAR2_TALSN Unreviewed; 1363 AA.
AC B8MAR2;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 62.
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=TSTA_115500 {ECO:0000313|EMBL:EED17752.1};
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959 {ECO:0000313|EMBL:EED17752.1, ECO:0000313|Proteomes:UP000001745};
RN [1] {ECO:0000313|Proteomes:UP000001745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC {ECO:0000313|Proteomes:UP000001745};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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; EQ962655; EED17752.1; -; Genomic_DNA.
DR RefSeq; XP_002481744.1; XM_002481699.1.
DR STRING; 441959.B8MAR2; -.
DR GeneID; 8099577; -.
DR VEuPathDB; FungiDB:TSTA_115500; -.
DR eggNOG; KOG1907; Eukaryota.
DR HOGENOM; CLU_001031_0_2_1; -.
DR InParanoid; B8MAR2; -.
DR OMA; LSANWMW; -.
DR OrthoDB; 2891567at2759; -.
DR PhylomeDB; B8MAR2; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000001745; 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, ECO:0000313|EMBL:EED17752.1};
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:UP000001745}.
FT DOMAIN 38..158
FT /note="Phosphoribosylformylglycinamidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18076"
FT DOMAIN 182..234
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 448..602
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT DOMAIN 880..1016
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 1325
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1327
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1363 AA; 148736 MW; 9AC5C25E4A9679C4 CRC64;
MVASDEQTYL ALPGPVAFSR SRGRAIALDI GAIDVRAQWV HYVHTAQPLQ EAQEAVLEQL
LRYGDIVDIP PTFEPTDGAV QNFYVYPRVG TISPWSSQAT GISHVCGLST FVKRIERGLK
ISALFSEGST PEEGYLERLH DRMTQVISQE EPDLAKVFSD HPPLPLETVP LHAGDRTPTE
ILQEANRRLG LALDQSEIDY LVAAYASNGP VPRDPTDVEL FMFAQVNSEH CRHKQFNATW
IIDGKQMPNS LFSMIRNTHK KNPEYTVSAY SDNAAVLQGE NAGFWAPDPT TREWTQTKEQ
VHILAKVETH NHPTAVSPFP GAATGSGGEI RDEGAVGRGS RPKAGLAGYC VSDLLIPELR
QPWELDVGKP HHIASSLDIM LEAPIGSAAF NNEFGRPCTA GYFRTLLTEL DIGNGQKEIR
GYHKPIMIAG GVGTVRPQHA LKDPKLVKPG SFLVVLGGPA MLIGLGGGAA SSLASGEGSA
DLDFASVQRG NAEVQRRAQE VINACVAMGE DSPIKFIHDV GAGGLSNALP ELVHDAGLGA
TFELREIDSA DRGMSPMQIW CCEAQERYVM AIGEEGMNKF TAIARRERCG FSVVGRAEQS
QQYEEKRLVL LDRDSKEYPK PIDLPLSVLF GKPPKMTRQV DSRKLKQPAF DASLSTYLPA
APSEQRLFEE AASRVLSLPA VGSKSFLITI GDRTVGGLTA RDQMVGPWQT PVSDVSVTAT
SLTQGIRTGE SMAMGEKPTL ALISPAASAR MAVAESLMNI TAADLFDRLS RVKLSANWMS
ASSHPGEGAA IYEAVEAIGL GLCPQLGISI PVGKDSMSMK MKWNDEKTKE AKEVTAPLSV
VISAFAPVQD FRNTWTPTLH SFEDVGETVL MFVDLACGHK ALGGSAVAQV FKQVGQESPD
VRDVELFRDF FDATQQLHEQ GIVLAYHDRS DGGLFTTLAE MMFAGRCGVE IMLDELQKEG
DIRSTIETLF NEELGAVFQV RKADEIRFRS CFATCGPPPG LIRRIGRVSQ KPKQNLTIYH
KHKLIYRQPR GKIQQIWSHT SYHMQKIRDN AACADQEYAN ILEDADPGIS WNIKFDPKDK
CLPILTSLSQ FSPFSNKPRV AILREQGVNS QAEMAFAFNL AGFAVVDVHM TDIISGRVSL
AAFVGLAACG GFSYGDVLGA GQGWAKSVLL HEETRKEFKT FFERPDTFAL GVCNGCQFLS
RLKELIPGAQ SWPSFERNAS EQYEGRVAMV HVSDPDPSAP SVFLHGMHGS SLPIAVAHGE
GRASFTMTPD VTAQDFVRHN LAPVRYVDNT TLKPTMTYPY NPNGSPEGIA GIRSPDGRVL
AIMPHPERTV IGGVASWLPA DAEKWGDVGP WGRIFYSARR WVG
//
