PUR4_SCHPO
ID PUR4_SCHPO Reviewed; 1323 AA.
AC O14228; Q9USF2;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Phosphoribosylformylglycinamidine synthase;
DE Short=FGAM synthase;
DE Short=FGAMS;
DE EC=6.3.5.3 {ECO:0000305|PubMed:967158};
DE AltName: Full=Formylglycinamide ribonucleotide amidotransferase;
DE Short=FGAR amidotransferase;
DE Short=FGAR-AT;
DE AltName: Full=Formylglycinamide ribotide amidotransferase;
GN Name=ade3; Synonyms=min11; ORFNames=SPAC6F12.10c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 925-1122, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=967158; DOI=10.1007/bf00582878;
RA Fluri R., Coddington A., Flury U.;
RT "The product of the ade1: gene in Schizosaccharomyces pombe: a bifunctional
RT enzyme catalysing two distinct steps in purine biosynthesis.";
RL Mol. Gen. Genet. 147:271-282(1976).
CC -!- FUNCTION: Phosphoribosylformylglycinamidine synthase involved in the
CC purines biosynthetic pathway (PubMed:967158). Catalyzes the ATP-
CC dependent conversion of formylglycinamide ribonucleotide (FGAR) and
CC glutamine to yield formylglycinamidine ribonucleotide (FGAM) and
CC glutamate (PubMed:967158). {ECO:0000269|PubMed:967158}.
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; Evidence={ECO:0000305|PubMed:967158};
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. {ECO:0000305|PubMed:967158}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10759889}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the FGAMS family.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAB11094.1; -; Genomic_DNA.
DR EMBL; AB027799; BAA87103.1; -; Genomic_DNA.
DR PIR; T11661; T11661.
DR RefSeq; NP_593296.1; NM_001018726.2.
DR AlphaFoldDB; O14228; -.
DR SMR; O14228; -.
DR BioGRID; 279316; 7.
DR STRING; 4896.SPAC6F12.10c.1; -.
DR MaxQB; O14228; -.
DR PaxDb; O14228; -.
DR PRIDE; O14228; -.
DR EnsemblFungi; SPAC6F12.10c.1; SPAC6F12.10c.1:pep; SPAC6F12.10c.
DR GeneID; 2542871; -.
DR KEGG; spo:SPAC6F12.10c; -.
DR PomBase; SPAC6F12.10c; ade3.
DR VEuPathDB; FungiDB:SPAC6F12.10c; -.
DR eggNOG; KOG1907; Eukaryota.
DR HOGENOM; CLU_001031_0_2_1; -.
DR InParanoid; O14228; -.
DR OMA; LSANWMW; -.
DR PhylomeDB; O14228; -.
DR Reactome; R-SPO-73817; Purine ribonucleoside monophosphate biosynthesis.
DR UniPathway; UPA00074; UER00128.
DR PRO; PR:O14228; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
DR GO; GO:0005774; C:vacuolar membrane; EXP:PomBase.
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; ISO:PomBase.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; EXP:PomBase.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:1904262; P:negative regulation of TORC1 signaling; EXP:PomBase.
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 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Glutamine amidotransferase; Ligase; Magnesium;
KW Metal-binding; Nucleotide-binding; Purine biosynthesis; Reference proteome.
FT CHAIN 1..1323
FT /note="Phosphoribosylformylglycinamidine synthase"
FT /id="PRO_0000100404"
FT DOMAIN 1062..1306
FT /note="Glutamine amidotransferase type-1"
FT ACT_SITE 1156
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 1284
FT /evidence="ECO:0000250"
FT ACT_SITE 1286
FT /evidence="ECO:0000250"
FT BINDING 312..323
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 391..393
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 691
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 692
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 733
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 737
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 903
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 905
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1323 AA; 144867 MW; 7D31A6BEFAE2997F CRC64;
MLVYYGGSAL SVQSKKKILE LTVSGVSDLN AVYFYLIYTK SNSSLNCESL RPILSDLQES
EFKPDGTTMV YVFPRPGTIS PWSSKATNIA NVCGYKDVIR IERGIAYSVV FKDDISEEML
KSALNHLYDR MTEALRFKLP EEDEVFDKHE PAPLVRIELN CGQGGDKQAA TERLNHANKK
FGLALAPDEI DYLVECYTSE PSLKSREPTD VELFMFGQVN SEHCRHKIFN ADWTIDGEKK
DYSLFKMIRN THLKNPQYTI SAYSDNAAVF EGNSGTLFAP VNGIWSMKDE PVEFLGKVET
HNHPTAVSPF PGAATGSGGE IRDEGAVGQG SLSKAGLAGY SVSDLNIPGY KQPWELDVGK
PYHIATSLDI MLEAPIGSSA FNNEFGRPCI NGYFRTFCME VPRGDGTLEI RGYHKPIMAA
GGIGRIRKQH AFKKSIAPGS PIIVLGGPAL LVGLGGGAAS SMNAGEGSEE LDFASVQRGN
PEMQRRAQMV IDACTTMDEN IIQSIHDVGA GGVSNALPEL VHDAGLGARF ELRDIPCIEP
SMSPMQIWCC ESQERYVLSV KSEDLDTFKS ICERERCPYG VVGYSTVEQR LILTDRLYNT
TPIDLPMEVL FGKPPKMSRV AETQTIPLSK FDSSLKSYLA PSSDPILDAV ERVLRMPAVA
SKSFLITIGD RSVTGLIARD QMVGPWQVPV ADVGVTVTSY GKGINTGEAL AMGEKPISAL
VSAAASARMA VAECIMNLVA ASIPALDRIR LSANWMAAPS HPGEGAKLYE AVQAIGLELC
PSLGISIPVG KDSMSMSMKW NEDGREKSVT APLSLIITGF SPVDDLYSIW TPQLRKVEDI
GSTSLIFIDL ANGKQRLGGS ILAQSYKQLG DEVPDLDNLD TFKNFINVIT QLHKTNYIQA
YHDKSDGGLF VTLSEMAFAG HVGIECELDS LSSDNIAALF NEELGAVIQV CDRDIAKVLE
LFAANGLSTC VHRIGKVLSG QAQTISFSRS GKIIFKSTRS KLHGIWHETS YKMQEIRDNP
ECARQEMENI ADNNDPGLGY HLTFDPNVSV TADLALTSRP KVAILREQGV NGYLEMAYAF
YASGFTAVDV HMTDILSGRV HLDDFVGIAA CGGFSYGDVL GSGNGWATSI LLHEDARNEF
YRFFNERKDT FGLGICNGCQ LFSRLKSLIP GAKSWPMFTF NESAQYEGRA VMLKIDETSG
SKSIFTESMA GSSLPVVVAH GEGRAVFDSE SDYEQFKKEG LDLIYYVNNY NERTSRYPFN
PNGSRDAIAG VRSPCGRFLA MMPHPERVVL KVANSYYPHS KASEWGVHGP WIRLFQSARK
WVG
