ID A0A1J7J460_9PEZI Unreviewed; 1362 AA.
AC A0A1J7J460;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=CONLIGDRAFT_626296 {ECO:0000313|EMBL:OIW34237.1};
OS Coniochaeta ligniaria NRRL 30616.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Coniochaetales; Coniochaetaceae; Coniochaeta.
OX NCBI_TaxID=1408157 {ECO:0000313|EMBL:OIW34237.1, ECO:0000313|Proteomes:UP000182658};
RN [1] {ECO:0000313|EMBL:OIW34237.1, ECO:0000313|Proteomes:UP000182658}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 30616 {ECO:0000313|EMBL:OIW34237.1,
RC ECO:0000313|Proteomes:UP000182658};
RG DOE Joint Genome Institute;
RA Jimenez D.J., Hector R.E., Riley R., Sun H., Grigoriev I.V.,
RA Van Elsas J.D., Nichols N.N.;
RT "Draft genome sequence of Coniochaeta ligniaria NRRL30616, a
RT lignocellulolytic fungus for bioabatement of inhibitors in plant biomass
RT hydrolysates.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; KV875093; OIW34237.1; -; Genomic_DNA.
DR STRING; 1408157.A0A1J7J460; -.
DR InParanoid; A0A1J7J460; -.
DR OrthoDB; 2891567at2759; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000182658; 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; 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:UP000182658}.
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 446..600
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT DOMAIN 870..998
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT REGION 311..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1195
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1323
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1325
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1362 AA; 148375 MW; 47408F222DAC0001 CRC64;
MEFLTLTGES CFAPWEAQKL TDLLNKLGPA KVSAVRGVWV YFASVEGDES SAQDKLRQLL
PLPRDTSTIP LSVDSAIKST RKCYVSPRNE SPWSSKATSI AQVCGFGDQI RRIERGRVVV
LEFEEPYDAP FDSTPFWNVI YDRMTENLTA EWPDLDTMFG EGEPRPLEVV DIFSGVKTPI
EILEEYNKKH GLALDHTEIE YLVKRFTELG RPPHDVELFM FGQVNSEHCR HKLFNANWTV
NGEAKAKSLF EMIRNTHKVT PDYTVSAYSD NACVLSGDVG NFWAPDYSTG SWTLTKETVL
PLAKVETHNH PTAIAPFPGA ATGSGGELRD EGSVGRGSTP KAGLTGFWVS DLLIPNHRAP
WELDVGRPAH YASSLDIMLE APIGSARYNN EFGRPCLSGV FRTLLTAEDS TKSDEWRGYH
KPIMIAGGVG TVREGNALKR EEDVHAGAHL IVLGGPGMLI GLGGGAASSN TSSGSTSADL
DFDSVQRGNP ELARRAQMVI NTCVALGAEN PIAFIHDVGA GGLSCAVPEI VKDAGFGGKF
ELRQVESADR SMSPLQLWCN ESQERYVILI NSDGMNRFVS ICKRERCGFS DIGIVIPKEV
EGVPKLVVSD RDSKEHPRPI DLPMDVLFPK GAKIERTDNS RKPTQPVFDT SASVKSALGD
SLSDAELFKK AVQQVFWMPS VGSKSFLITI GDRTVGGLTV RDQMVGPWQT PVADVAVTAA
SFSLDGAKRG EAMAMGEKPT IALINPTASA RMAVAESLLN LGAADIMGGK TRGDLRRVKL
SANWMAATNV PGEGAALYEA VEAIGMELCP KLGVSIPVGK DSMSMKASWR EGDATKTVTS
PVSVVISAFT VVENIRSTWT PQLRRKEEVG DTVLMYVDLA QGRKAMGGSA LAQSLGKLGH
EAPDVRDVDL LKDYFDALAQ LHETNVVLAY HDRSDGGLLT TIAEMMFAGR CGVDLMMDDI
SKSGSLADMT EALFNEELGA VFQIREKDQS NFMRCFATCG PPPGLVKRCG VVKSTSKQTL
TIRYGNVSPF VTLDRAEMQQ WWTKTSFEMQ KLRDNPMCAE SEYGTILDSE DPGLSYKLSF
VPSENILPMT ASISNFFGRR PRVAILRDQG VNGHAEMAFA FAAAGFEAID VHLSDILNGR
SLAEFVGMAA CGGFSYGDVL GAGQGWAKSI LLHENSRREF ETYFKRPDTF TLGVCNGCQM
LARLRELIPG TENWPVFVDN ASQQFEARYS MVKVIDDPDR PSVFLHGMSG SALPIVVSHG
EGRAQFASPN SLQALTESGQ IPVRYVDNRL KVTEQYPYNP NGSPAGVAGV SSKDGRVLAM
MPHPERTIMA DVASYTPDHV LEGCGDFGPW LRLFRSARLW VG
//