PUR4_ARATH
ID PUR4_ARATH Reviewed; 1407 AA.
AC Q9M8D3; A9Y5J1; F4HTW2;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 3.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Probable phosphoribosylformylglycinamidine synthase, chloroplastic/mitochondrial;
DE Short=FGAM synthase;
DE Short=FGAMS;
DE EC=6.3.5.3;
DE AltName: Full=Formylglycinamide ribonucleotide amidotransferase;
DE Short=FGAR amidotransferase;
DE Short=FGAR-AT;
DE AltName: Full=Formylglycinamide ribotide amidotransferase;
DE Flags: Precursor;
GN OrderedLocusNames=At1g74260; ORFNames=F1O17.7;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], DISRUPTION PHENOTYPE, FUNCTION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=18441219; DOI=10.1104/pp.108.120014;
RA Berthome R., Thomasset M., Maene M., Bourgeois N., Froger N., Budar F.;
RT "pur4 mutations are lethal to the male, but not the female, gametophyte and
RT affect sporophyte development in Arabidopsis.";
RL Plant Physiol. 147:650-660(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
CC -!- FUNCTION: Essential to the male gametophyte development.
CC Phosphoribosylformylglycinamidine synthase involved in the purines
CC biosynthetic pathway. Catalyzes the ATP-dependent conversion of
CC formylglycinamide ribonucleotide (FGAR) and glutamine to yield
CC formylglycinamidine ribonucleotide (FGAM) and glutamate.
CC {ECO:0000269|PubMed:18441219}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-
CC ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-
CC ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate;
CC Xref=Rhea:RHEA:17129, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58359, ChEBI:CHEBI:147286, ChEBI:CHEBI:147287,
CC ChEBI:CHEBI:456216; EC=6.3.5.3;
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 -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:18441219}. Mitochondrion
CC {ECO:0000269|PubMed:18441219}.
CC -!- DISRUPTION PHENOTYPE: Lethal to the male gametophyte.
CC {ECO:0000269|PubMed:18441219}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the FGAMS family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG52403.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=ABW87767.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; EU091297; ABW87767.1; ALT_INIT; mRNA.
DR EMBL; AC020579; AAG52403.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE35571.1; -; Genomic_DNA.
DR PIR; A96771; A96771.
DR RefSeq; NP_177566.3; NM_106086.5.
DR AlphaFoldDB; Q9M8D3; -.
DR SMR; Q9M8D3; -.
DR BioGRID; 28985; 9.
DR STRING; 3702.AT1G74260.1; -.
DR MEROPS; C56.972; -.
DR PaxDb; Q9M8D3; -.
DR PRIDE; Q9M8D3; -.
DR ProteomicsDB; 224869; -.
DR EnsemblPlants; AT1G74260.1; AT1G74260.1; AT1G74260.
DR GeneID; 843766; -.
DR Gramene; AT1G74260.1; AT1G74260.1; AT1G74260.
DR KEGG; ath:AT1G74260; -.
DR Araport; AT1G74260; -.
DR TAIR; locus:2019637; AT1G74260.
DR eggNOG; KOG1907; Eukaryota.
DR HOGENOM; CLU_001031_0_0_1; -.
DR InParanoid; Q9M8D3; -.
DR OMA; LSANWMW; -.
DR OrthoDB; 38224at2759; -.
DR BioCyc; ARA:AT1G74260-MON; -.
DR UniPathway; UPA00074; UER00128.
DR PRO; PR:Q9M8D3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9M8D3; baseline and differential.
DR Genevisible; Q9M8D3; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; HDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; TAS:TAIR.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0055046; P:microgametogenesis; IMP:TAIR.
DR GO; GO:0009555; P:pollen development; IMP:TAIR.
DR Gene3D; 3.30.1330.10; -; 2.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.90.650.10; -; 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 Pfam; PF02769; AIRS_C; 2.
DR Pfam; PF18072; FGAR-AT_linker; 1.
DR Pfam; PF18076; FGAR-AT_N; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR SUPFAM; SSF55326; SSF55326; 2.
DR SUPFAM; SSF56042; SSF56042; 2.
DR SUPFAM; SSF82697; SSF82697; 1.
DR TIGRFAMs; TIGR01735; FGAM_synt; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Chloroplast; Glutamine amidotransferase; Ligase; Magnesium;
KW Metal-binding; Mitochondrion; Nucleotide-binding; Plastid;
KW Purine biosynthesis; Reference proteome; Transit peptide.
FT TRANSIT 1..53
FT /note="Chloroplast and mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 54..1407
FT /note="Probable phosphoribosylformylglycinamidine synthase,
FT chloroplastic/mitochondrial"
FT /id="PRO_0000029880"
FT DOMAIN 1141..1381
FT /note="Glutamine amidotransferase type-1"
FT ACT_SITE 1235
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 1366
FT /evidence="ECO:0000250"
FT ACT_SITE 1368
FT /evidence="ECO:0000250"
FT BINDING 407..418
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 487..489
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 786
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 787
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 826
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 830
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 989
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 991
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1407 AA; 153954 MW; 49F270F0E2CEBDCB CRC64;
MNTSQATRAA LFLNGSNRQA MLLQRSSMSQ LWGSVRMRTS RLSLNRTKAV SLRCSAQPNK
PKAAVSTGSF VTADELPSLV EKPAAEVIHF YRVPLIQESA NAELLKAVQT KISNQIVSLT
TEQSFNIGLE SKLKDEKLSV LKWILQETYE PENLGTDSFL ERKKQEGLHA VIVEVGPRLS
FTTAWSTNAV SICRACGLDE VTRLERSRRY LLFSKEPLLE NQIKEFAAMV HDRMTECVYT
QKLVSFETNV VPEEVKYVPV MEKGRKALEE INQEMGLAFD EQDLQYYTRL FREDIKRDPT
NVELFDIAQS NSEHSRHWFF AGNMVIDGKP MDKSLMQIVK STWEANRNNS VIGFKDNSSA
IRGFLVNQLR PLLPGSVCLL DVSARDLDIL FTAETHNFPC AVAPYPGAET GAGGRIRDTH
ATGRGSFVVA STSGYCVGNL NMEGSYAPWE DSSFQYPSNL ASPLQILIDA SNGASDYGNK
FGEPMIQGYT RTFGMRLPSG DRREWLKPIM FSAGIGQIDH THITKGEPEV GMLVVKIGGP
AYRIGMGGGA ASSMVSGQND AELDFNAVQR GDAEMSQKLY RVVRACIEMG EKNPIISIHD
QGAGGNCNVV KEIIYPQGAE IDIRAVVVGD HTMSVLEIWG AEYQEQDAIL VKAESREILQ
SICKRERLSM AVIGTINGGG RCTLIDSTAA AKCSKEGLPP PPPAVDLELE KVLGDMPKKT
FKFNRIAYAR EPLDIAPGIT LMDALKRVLR LPSVSSKRFL TTKVDRCVTG LVAQQQTVGP
LQITLADVAV IAQTFTDLTG GACAIGEQPI KGLLDPKAMA RLAVGEALTN LVWAKVTALS
DVKASGNWMY AAKLEGEGSA MYDAAIALSE AMIELGIAID GGKDSLSMAA HADGEVVKAP
GNLVISAYVT CPDITKTVTP DLKLGGDDGI LLHVDLAKGK RRLGGSALAQ VFGQIGNDCP
DLDDVPYLKN VFDGVQALIA ENLVSAGHDI SDGGLVVTAL EMAFAGNKGI NLDLASNGIS
LFETLFSEEL GLVLEISKTN LDAVMEKLRA FDVTAEIIGN VTDSPLIEVK VDGITHLSEK
TSFLRDMWED TSFQLEKLQR LASCVEMEKE GLKFRHEPNW KLSFIPSSTN NNYMSQDVKP
KVAVIREEGS NGDREMSAAF YAAGFEPWDV TVSDLLAGDI TLDQFRGIVF VGGFSYADVL
DSAKGWAASI RFNEPVLSQF QEFYKRPDTF SLGICNGCQL MALLGWVPGP QVGGSLDTSQ
PRFVHNESGR FECRFTSVTI KDSPSIMLKG MEGSTLGVWA AHGEGRAYFP DEGVLDHMLH
SDLAPLRYCD DDGNVTEAYP FNLNGSPLGI AAICSPDGRH LAMMPHPERC FLMWQFPWYP
TSWDVEKAGP SPWLKMFQNA RDWLESC
