ID A0A2Z6RT40_9GLOM Unreviewed; 1380 AA.
AC A0A2Z6RT40;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=RclHR1_06660009 {ECO:0000313|EMBL:GBC06156.1};
OS Rhizophagus clarus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX NCBI_TaxID=94130 {ECO:0000313|EMBL:GBC06156.1, ECO:0000313|Proteomes:UP000247702};
RN [1] {ECO:0000313|EMBL:GBC06156.1, ECO:0000313|Proteomes:UP000247702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HR1 {ECO:0000313|EMBL:GBC06156.1,
RC ECO:0000313|Proteomes:UP000247702};
RA Kobayashi Y.;
RT "The genome of Rhizophagus clarus HR1 reveals common genetic basis of
RT auxotrophy among arbuscular mycorrhizal fungi.";
RL Submitted (NOV-2017) 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}.
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:GBC06156.1}.
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DR EMBL; BEXD01004055; GBC06156.1; -; Genomic_DNA.
DR STRING; 94130.A0A2Z6RT40; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000247702; 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:UP000247702}.
FT DOMAIN 54..180
FT /note="Phosphoribosylformylglycinamidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18076"
FT DOMAIN 214..265
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 479..635
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT DOMAIN 900..1033
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT REGION 346..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1208
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1341
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1343
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 1380 AA; 152452 MW; 4766CF877A4AA0C2 CRC64;
MLILPGNPAL SDFKKKSLLK NIQAYAPIDT ITAIYIHFIQ PRNEESLKIL NDSKSIERGV
LDNLLNYGIV SDNIANNSIN EIKEYITSPK PIADPRILTV IPRPGTISPW SSKATNILYM
CNLEQHVERI ERGIVYLFGI KLTVDMRHII SEKLVMLDHL LYDRMTQIIV NHLPSSETIF
KHGKPAPLRI IELSDNNKNS LDHNLAAKKK LIDGNKQLGL ALTDDEIDYL VDAFAGDSEN
SLARNPTDVE LFMFAQVNSE HCRHKIFRAD WIIDNEKKSY SLFGMIRNTH KLNPQFTLSA
YSDNAAVLEG FKAARFSPDN NDFKYNLFEE DVHIVAKVET HNHPTAVSPF PGAATGSGGE
IRDEGSVGQG SKPKAGLTGF SVSNLLIPGY VQPWETDFGK PSHIASSFDI MIDAPLGGAA
YNNEFGRPNI TGYFRTFAQE VPMTNETNEI RGYHKPIMIA GGLGTIRPHH VFKKQITSGA
HLFVLGGPSM LIGLGGGAAS SMTSGASDAR LDFGSVQREN PEMQRRCQQV IDVCTALGDK
NPIQSIHDVG AGGLSNAFPE IVHDSGLGCV IQLRAIPNDD PGMSPMEIWC NEAQERYVLA
VAQENIELFE KICKREKCLF ADVGVATEKQ ELILQDSLFK TTPINLPMSI LFGKPPKMLR
ETITLKPPRI PFDTSLKSYL VDVTDQGEIF KDAINRVLRL PTVASKSFLI TIGDRTITGL
VARDQMVGPW QVPVSDVAVT SSSYGVGIIT GEAMAMGERA PIALISHGAS ARMAVAEAIT
NLAAANIKSI SHIRLSANWM CAANHNGEGS GLYEAVQAIG LELCPALGIS IPVGKDSMSM
KMKWKDKNDD QKEVISPLSL VITGFATVVN THKTLTPQLR TDIVENTILV FLDLANCKQR
MGGSAIAQVY KQIGNEVPDV ESPELIKSFF KAIQDVRKGE YESILAYHDR SDGGLFVAII
EMAFAGHVGV NVNISCILRD NDIIGALFNE ELGAVIQLRQ NDFENVTNAF VNSGFPKENI
YHIGNVSPGK SQDILIKKDE LTIFKASRVE LQRIWSETSY QMQSIRDSSI CAKEEFDNIL
DVNNPGIHFQ LTFDPSHDVT LPFIKCPEEV KPKVAILREQ GINGQIEMAY AFHLAGFKAI
DVHMSDILSG KVTLKEFSGI AACGGFSYGD VLGAGSGWAK SILLHSNARK EFEDFFKSRQ
DTFALGICNG CQFMSQLKEL IPGTENWPVF KRNKSEQFEA RFSLVKIIKS EEESSKVIPS
IFLKDMTGSR FPIAVAHGEG KAEFSSEEQM KNLIKQGLVV IQYIDNYGNI TEKYPFNPNG
SPMGITGLQT PNGRVLIMMP HPERIIMKEA NSWYPIEEGK KWGEVGPWLR IFRNARVWVS
//
