ID A0A0D3G297_9ORYZ Unreviewed; 2053 AA.
AC A0A0D3G297;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
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};
OS Oryza barthii.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=65489 {ECO:0000313|EnsemblPlants:OBART05G00320.1};
RN [1] {ECO:0000313|EnsemblPlants:OBART05G00320.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 105608 {ECO:0000313|EnsemblPlants:OBART05G00320.1};
RX DOI=10.1007/s12284-009-9025-z;
RA Rounsley S., Marri P.R., Yu Y., He R., Sisneros N., Goicoechea J.L.,
RA Lee S.J., Angelova A., Kudrna D., Luo M., Affourtit J., Desany B.,
RA Knight J., Niazi F., Egholm M., Wing R.A.;
RT "De novo next generation sequencing of plant genomes.";
RL Rice 2:35-43(2009).
RN [2] {ECO:0000313|EnsemblPlants:OBART05G00320.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2015) to UniProtKB.
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 STRING; 65489.A0A0D3G297; -.
DR PaxDb; 65489-OBART05G00320-1; -.
DR EnsemblPlants; OBART05G00320.1; OBART05G00320.1; OBART05G00320.
DR Gramene; OBART05G00320.1; OBART05G00320.1; OBART05G00320.
DR eggNOG; KOG1907; Eukaryota.
DR HOGENOM; CLU_001031_1_0_1; -.
DR UniPathway; UPA00074; UER00128.
DR Proteomes; UP000026960; Chromosome 5.
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 Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR HAMAP; MF_00419; PurL_1; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR040707; FGAR-AT_N.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
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 Pfam; PF00560; LRR_1; 1.
DR Pfam; PF08263; LRRNT_2; 2.
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; SSF52058; L domain-like; 2.
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:UP000026960};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 13..46
FT /note="Leucine-rich repeat-containing N-terminal plant-
FT type"
FT /evidence="ECO:0000259|Pfam:PF08263"
FT DOMAIN 399..520
FT /note="Phosphoribosylformylglycinamidine synthase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF18076"
FT DOMAIN 547..596
FT /note="Phosphoribosylformylglycinamidine synthase linker"
FT /evidence="ECO:0000259|Pfam:PF18072"
FT DOMAIN 751..906
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT DOMAIN 1161..1291
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT DOMAIN 1740..1775
FT /note="Leucine-rich repeat-containing N-terminal plant-
FT type"
FT /evidence="ECO:0000259|Pfam:PF08263"
FT ACT_SITE 1455
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1590
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 1592
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 2053 AA; 223939 MW; FCB5BD65AB72E36C CRC64;
MPTDCGGVGA ERRRRLLAVK AAFNNASFFE YWTPEFPCCD WYGVDCGDDY LPSDDRVISL
AIPASLAKPP KLNSIDLSRN RLTGSIPRLL LSKAGQQAFL TLSHNNLTGR IPAEFGAVNF
VQIDLSRNQL TGDASMLFGS GKKELVSAYL SRNALSFNMS QLQLPEELNF LDVSHNSIYG
SIPAQMANMT DMQLLNVSYN RLCGEVPTGG NMPSFDAYCF QHNNKAKQAR STHHLLRALQ
PPALPPLTLS VHLPLRHGYT SNRSAAVPIS PVPLYILSPV ACCQESNPID FKFDQGKRNG
FIAARSSGLR RSQQCFHRHL CWPGVRRASV PNVRLLPTPG ALVSRGLDSS LVHKSDNASE
AGVIQLYRIP YLQDSETIEL LRQVQAKVSS NIVGIKTEQC FNIQLDNALA SEKLATLQWL
LAETYEPDKL QAQSFLEEEV ARNPYSVIVE VGPRMTFSTA FSTNAVSICK SLSLMEVTRL
ERSRRYLLCL DPGYGPLDES QLNDFTALVH DRMTECVYPK KLTSFHSDVV PEPVRIVPVI
ERGREALEEI NVKMGLAFDE QDIKYYTHLF RDDIKRNPTT VELFDIAQSN SEHSRHWFFN
GKLVIDGETM PRTLFQLVKS PLKANPDNNS VIGFNDNSSA IKGYPANQLR PTVPGSTSPL
SVMMRXYAPW EDPSFSYPSN LASPLQILID ASDGASDYGN KFGEPLIQGF TRNFGTRLLN
GERREWLKPI MFSGAIGQID HAHISKGDPE IGMLVVKIGG PAYRIGMGGG AASSMVSGQN
DAELDFNAVQ RGDAEMAQKL YRVVRACAEM GESNPIISIH DQGAGGNCNV VKEIIYPKGA
EIDIRSIVVG DHTLSVLEIW GAEYQEQDAL LVKPESRSLL ESLCERERVS MAVIGTINGC
GKIVLIDSAA VEHAKLNGLP PPTPVEDLEL EKVLGDMPQK TFEFKRVSVV SEPLDIARGV
TIMDALKRVL SLPSVCSKRF LTTKVDRCVT GLVAQQQTVG PLQLPLADVA VIAQTYTDLT
GGACAIGEQP TKGLLNPKAM ARLAIGEALT NLVWAKVSSL SDVKASGNWM YAAKLDGEGA
DMYDAAVALA DCMIQLGIAX DGGKDSLSMA AQCDGEVVKA PGNLVISAYV TCPDITLTVT
PDLKLGKDGV LLHIDLSKGK RRLGGSALAQ AFDQIGNDCP DIDDVLYLKK AFEAVQELLG
ERLISAGHDI SDGGLIVSVL EMAFAGNCGV KLNIDSEDSS LLQALFAEEL GLLLEVHLKD
LSVVKQKLQA GGISANVIGK VTASPDIELV VDGRLHLKEK TSDLRDIWEE TSFQLEGLQR
LKSCVRLEKE GLKHRTSPSW SLSFTPKFTD EKLLTASSKP KVAILREEGS NGDREMAAAF
YAAGFEPWDI TMSDLLAGKS SLEDYRGIAF VGGFSYADVL DSAKGWAASI RFNQPLIQQF
QNFYNRPDTF SLGVCNGCQL MALLGWVPGS DVGGSLGSGG DMSQPRFIHN ESGRFECRFT
SVSIGASPAI MFKGMEGSTM GIWSAHGEGR AFFPDENVLA SVVKSNLAPV RYCDDANNIT
EVYPFNPNGS PLGIAALCSP DGRHLAMMPH PERCFMMWQY PWSPKDWQLE KSGPSPWLRM
FQNARECCVT YRDLIDGRSR TRHLGQEDTN CRMRRLIVLF KAVGAKLLPS EQLANLITPS
PSTYIYPHTH IVQDKLRQNR SEVEMVRAIG PLLLLAHVLV FVVSIAAAAA PVRRPRCDAG
DRAALLAVKA AFNNASYFQS WTPDIACCHW YGVDCGGDDY DYDPTDGDRV LSLAIIRDDN
VTGGIPGDAI ARLTRLQELM FFKVPGVTGP IPAALATLTA LRELTISRTA LSGSIPSFIG
DKFTALQSLD LSFNSLTGAI PASLAKPPKL ISIDLSRNQL TGSIPRLLLS KAGQQAFLTL
SHNNLSGRIP AAFGAVNFVQ IDLSRNQLTG DASMLFGSGK KELGSVYLSR NALSFDMSEL
RLPERLSFLD VSHNAIRGGI PAQVANLSNL QLLNVSYNRM CGEVPTGGNM ARFDAYCFQH
NKCLCGAPLA ACH
//
