ID J9VWG3_CRYNH Unreviewed; 1355 AA.
AC J9VWG3;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 51.
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=CNAG_04192 {ECO:0000313|EMBL:AFR96924.1};
OS Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 /
OS CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=235443 {ECO:0000313|EMBL:AFR96924.1, ECO:0000313|Proteomes:UP000010091};
RN [1] {ECO:0000313|EMBL:AFR96924.1, ECO:0000313|Proteomes:UP000010091}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487
RC {ECO:0000313|Proteomes:UP000010091};
RX PubMed=24743168; DOI=10.1371/journal.pgen.1004261;
RA Janbon G., Ormerod K.L., Paulet D., Byrnes E.J.III., Yadav V.,
RA Chatterjee G., Mullapudi N., Hon C.C., Billmyre R.B., Brunel F., Bahn Y.S.,
RA Chen W., Chen Y., Chow E.W., Coppee J.Y., Floyd-Averette A., Gaillardin C.,
RA Gerik K.J., Goldberg J., Gonzalez-Hilarion S., Gujja S., Hamlin J.L.,
RA Hsueh Y.P., Ianiri G., Jones S., Kodira C.D., Kozubowski L., Lam W.,
RA Marra M., Mesner L.D., Mieczkowski P.A., Moyrand F., Nielsen K., Proux C.,
RA Rossignol T., Schein J.E., Sun S., Wollschlaeger C., Wood I.A., Zeng Q.,
RA Neuveglise C., Newlon C.S., Perfect J.R., Lodge J.K., Idnurm A.,
RA Stajich J.E., Kronstad J.W., Sanyal K., Heitman J., Fraser J.A.,
RA Cuomo C.A., Dietrich F.S.;
RT "Analysis of the genome and transcriptome of Cryptococcus neoformans var.
RT grubii reveals complex RNA expression and microevolution leading to
RT virulence attenuation.";
RL PLoS Genet. 10:E1004261-E1004261(2014).
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; CP003828; AFR96924.1; -; Genomic_DNA.
DR RefSeq; XP_012051651.1; XM_012196261.1.
DR GeneID; 23887631; -.
DR KEGG; cng:CNAG_04192; -.
DR VEuPathDB; FungiDB:CNAG_04192; -.
DR HOGENOM; CLU_001031_0_2_1; -.
DR OrthoDB; 2891567at2759; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000010091; Chromosome 9.
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}.
FT DOMAIN 52..169
FT /note="Phosphoribosylformylglycinamidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18076"
FT DOMAIN 195..243
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 458..617
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT DOMAIN 882..1016
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT REGION 325..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1185
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1312
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1314
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1355 AA; 145800 MW; C1634561B390CD8A CRC64;
MLVLPGSSAI TPSRRATLLK LFQSVIPSIT SVDAVHLHFV NPTSDEAESL LADTKSAERD
ILNALLAYGD NEQLDSTKSF VEAGMKGDVF ALYVLPRVGT ISPWSSKATD IAKLCRLAGH
VSRLERGALY LFTSNESISL LEMRHHLHFI HDRMTQLIHT ALPPSAAVFP PTPPNPSALI
SVPILGAENP HAVLGEANAR LGLALSETEI PYLVESFLAA GRNPTDAELF MFAQVNSEHC
RHKIFNAKWT IDGHEQKNSL FGMIRNTEKA VHSKGTLSAY EDNAAVMEGY EAPRFAVGGK
GDGSYTSQME KNPILIKVET HNHPTAVSPY PGAATGSGGE IRDEGATGRG SHPKAGLAGY
TTSDLLIPDF IQPWESDIGR PAHIASALDI MIEAPLGAAS FNNEFGRPAL GGYWRTWLMP
VKDAEGKEEW RGYHKPIMIA GGLGNVRPQF ARKDKISPGS KVIVLGGPGM LIGLGGGAAS
SMASGASSAD LDFASVQREN PEMERRCQQV IDACISRGDG AGNPIESIHD VGAGGLSNAL
PELVHDSGLG AVFEIRDVLV DDPSMSPMEI WCNESQERYV LAVAAENLAA FEEIARRERC
PFSVVGTATE EERLVVTDRL LGDNVIDISM SVLFGKPPRM HREAQTIHPK RDAFDSSLFT
YLPTYAGAPK TSLMAESINR VLRLPSVGSK SFLITIGDRT ITGLVTRDQM VGPWQVPVAD
VAVTRSSYGF DVVVGEAMSM GERTPLALLN AGASARMAIA ESLTNLAASS VADISQIKLS
ANWMSAANHS GEGSKLYEAV QAIGMDLCPK LGVGIPVGKD SMSMSMKWPG EKGEQKQVIA
PLSLIVTAFA PVDNVEKTWT PALRTDKGET VLVFVDLARG KQRLGGSAIA QVFKQLGADA
PDVEEAADVR AFFHAIQALK KAETVLAYHD RSDGGLLTTL VEMAFAGRSG IEVTVDAISS
SGDAVAALFN EELGAVMQVK TDKLSAFTDA FVKAGFPTQH IHVIGKVLGR ENQSVSIIHK
SDAIYTGTRG QLQQLWAETS YKIQAMRDEP TGAKEEFDAI LDDEDEGLIY NVPFKYLPDV
TDANRLASPP KVAILREQGV NGHIEMAWSF HAAGFEAVDV HMSDIISSKA SLSSFAGIAA
CGGFSYGDVL GAGNGWAKSV LLNPTARKEF EQFFQREDTF ALGVCNGCQF FAQLKEIIPG
TEHWPIFKAN RSERFEGRVV NVKVSPEAAK SNIFFSDMAD TIVPIAVAHG EGRPSFVTGS
LAGLNENNLI PLRYVDGTGA IATTYPKNPN GGPEGIAAVS TLNGRVLAVM PHPERVVTRE
SFSWFPEEMG KTWEGKGPWF RLFQNAYKFA TEGKQ
//
