ID A0A0F9X882_TRIHA Unreviewed; 1355 AA.
AC A0A0F9X882;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=THAR02_07142 {ECO:0000313|EMBL:KKP00755.1};
OS Trichoderma harzianum (Hypocrea lixii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=5544 {ECO:0000313|EMBL:KKP00755.1, ECO:0000313|Proteomes:UP000034112};
RN [1] {ECO:0000313|Proteomes:UP000034112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T6776 {ECO:0000313|Proteomes:UP000034112};
RX PubMed=26067977; DOI=10.1128/genomeA.00647-15;
RA Baroncelli R., Piaggeschi G., Fiorini L., Bertolini E., Zapparata A.,
RA Pe M.E., Sarrocco S., Vannacci G.;
RT "Draft whole-genome sequence of the biocontrol agent Trichoderma harzianum
RT T6776.";
RL Genome Announc. 3:E0064715-E0064715(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}.
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:KKP00755.1}.
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DR EMBL; JOKZ01000232; KKP00755.1; -; Genomic_DNA.
DR OMA; LSANWMW; -.
DR OrthoDB; 2891567at2759; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000034112; 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; 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:UP000034112}.
FT DOMAIN 38..154
FT /note="Phosphoribosylformylglycinamidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18076"
FT DOMAIN 178..227
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 446..601
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT DOMAIN 880..976
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT ACT_SITE 1188
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1316
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1318
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1355 AA; 148408 MW; 9DE3712026E1BB5F CRC64;
MPYEVLVGGS CYTPSDAQKL RELINKSSPS KVKDIQGQWI YYVNLQVSSH DTLEQVEELL
QDVRGWGLGS EGPGNALTIY ATPRYISPWS SKATSIAHVC GLRERVLRIE RGRRISIQFE
EPLSEGQDAT FRDVLYDRMT ELWTAEPPSL VQMFESKAPS SLVAVDIFAD KEDPLRILRE
YNVKKGLSLD ESEMQYLVDV FTKLGRPPHD VELFMFAQVN SEHCRHKVFN SAWTIDGVPQ
DKSLFEMIKT THKTTPDFTV SAYSDNAAVL EGDNANVWAP DYSTGSWKLT PEVVHILTKV
ETHNHPTAIS PFPGAATGSG GEIRDEGAVG RGSTTKAGLS GFWVSDLLIP DNHAPWESDI
GRPRHYASSL DIMLEAPIGS ARFNNEFGRP ALAGVFRTLL TPEESQEDSD VSSVANWRGY
HKPIMIAGGL GSVRPQHALK EERYVQEGAH VIVLGGPAML IGLGGGAASS SAGGEQSADL
DFDSVQRGNP EMERRAQMVI NTCTALGEHN PIAMIHDVGA GGLSNALPEL VKDAGFGGNF
ELRQVESMDR SMSPLEIWCN EAQERYVLLI NADSMNRFTS ICRRERCGFS DVGTVISKNE
HGATSLILTD RESKEYPRPI DLPMDALFPP KRLLQRDVAS KKPTLLPFNA FSSLQKAYGE
LSGAELFKKA VERVFLMPSV GSKSFLITIG DRSVGGLTVR DQMVGPWQTP VADVAVTATS
FHIGTKQKTG EAMAMGEKPT LAMIDPAASA RMAIAESLMN IGAADVTEDL RRVKLSANWM
AAVNHAGEGA ALYEAVRAAM EMCTRLRVSI PVGKDSTSMK ASWKNEEDSK NVTAPVSVVI
SAFSAVRDIR STWTPQLRRV EDVGETSLMF VDLAEGRRAM GGSALAQSLG AVGDKAPDMK
NFDLITDYFD ALSQLHRSGV VLAYHDRSDG GLITTVAEMM FAGRCGVDMM LDGISKSGKP
EDIIEAMFNE ELGAVFQIRT EDEINFKRCF ATCGPPPGLI RKFGVVRSTS KQSLNIRHAG
MTFATLDRTE MQQWWSKTSY EMQKIRDNSA CAESEFGTIS DSADPGITYK LSYSPAENIL
PITSSITGFF GRIPRVAILR EQGVNGHAEL AYAFKAAGFE PIDVHMTDVL DGRSLADFTG
LACPGGFSYG DVLGAGQGWA KSILMHDNTR REFAAFFKRP DTFALGVCNG CQMLTRIKEL
IPGAQDWPNF VDNTSQQFEA RYSMVKVQVD KSKPSVFFHG MNGSELPIVV SHGEGRAKFG
SPNSLQTLTE SGMVPLRYVD NRGNVTEQYP YNPNGSPMGV AGVASPDGRV VAMMPHPERT
IMADITSYAS PEDVEEWGEF GPWLRMFRSA RRWVG
//
