PUR2_SCHPO
ID PUR2_SCHPO Reviewed; 788 AA.
AC P20772; Q9UUM5;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Bifunctional purine biosynthetic protein ADE1;
DE Includes:
DE RecName: Full=Phosphoribosylamine--glycine ligase;
DE EC=6.3.4.13 {ECO:0000269|PubMed:967158};
DE AltName: Full=Glycinamide ribonucleotide synthetase;
DE Short=GAR synthetase {ECO:0000303|PubMed:967158};
DE Short=GARS;
DE AltName: Full=Phosphoribosylglycinamide synthetase;
DE Includes:
DE RecName: Full=Phosphoribosylformylglycinamidine cyclo-ligase;
DE EC=6.3.3.1 {ECO:0000269|PubMed:967158};
DE AltName: Full=AIR synthase;
DE Short=AIR synthetase {ECO:0000303|PubMed:967158};
DE Short=AIRS;
DE AltName: Full=Phosphoribosyl-aminoimidazole synthetase;
GN Name=ade1 {ECO:0000303|PubMed:3502942};
GN ORFNames=SPBC405.01 {ECO:0000312|PomBase:SPBC405.01}, SPBC4C3.02c;
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 [GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=3502942; DOI=10.1007/bf00368061;
RA McKenzie R., Schuchert P., Kilbey B.;
RT "Sequence of the bifunctional ade1 gene in the purine biosynthetic pathway
RT of the fission yeast Schizosaccharomyces pombe.";
RL Curr. Genet. 12:591-597(1987).
RN [2]
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 [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).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Catalyzes the second and fifth step in the 'de novo' purine
CC biosynthesis pathway; contains phosphoribosylamine--glycine ligase
CC (GARS) and phosphoribosylformylglycinamidine cyclo-ligase (AIRS)
CC activities. {ECO:0000269|PubMed:967158}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) +
CC N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate;
CC Xref=Rhea:RHEA:17453, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57305, ChEBI:CHEBI:58681,
CC ChEBI:CHEBI:143788, ChEBI:CHEBI:456216; EC=6.3.4.13;
CC Evidence={ECO:0000269|PubMed:967158};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ATP
CC = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:23032, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:137981,
CC ChEBI:CHEBI:147287, ChEBI:CHEBI:456216; EC=6.3.3.1;
CC Evidence={ECO:0000269|PubMed:967158};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00409};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00409};
CC Note=Binds two magnesium or manganese ions per subunit. {ECO:0000305};
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 2/2. {ECO:0000305}.
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-
CC (5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-
CC diphosphate: step 2/2. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the GARS family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the AIR synthase
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X06601; CAA29820.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA16823.1; -; Genomic_DNA.
DR PIR; S00652; S00652.
DR RefSeq; NP_596304.1; NM_001022225.2.
DR AlphaFoldDB; P20772; -.
DR SMR; P20772; -.
DR BioGRID; 277549; 4.
DR STRING; 4896.SPBC405.01.1; -.
DR iPTMnet; P20772; -.
DR MaxQB; P20772; -.
DR PaxDb; P20772; -.
DR PRIDE; P20772; -.
DR EnsemblFungi; SPBC405.01.1; SPBC405.01.1:pep; SPBC405.01.
DR PomBase; SPBC405.01; ade1.
DR VEuPathDB; FungiDB:SPBC405.01; -.
DR eggNOG; KOG0237; Eukaryota.
DR HOGENOM; CLU_005361_1_0_1; -.
DR InParanoid; P20772; -.
DR OMA; EVMQACC; -.
DR PhylomeDB; P20772; -.
DR Reactome; R-SPO-73817; Purine ribonucleoside monophosphate biosynthesis.
DR UniPathway; UPA00074; UER00125.
DR UniPathway; UPA00074; UER00129.
DR PRO; PR:P20772; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA: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:0004637; F:phosphoribosylamine-glycine ligase activity; IDA:PomBase.
DR GO; GO:0004641; F:phosphoribosylformylglycinamidine cyclo-ligase activity; IDA:PomBase.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IMP:PomBase.
DR GO; GO:0046084; P:adenine biosynthetic process; IBA:GO_Central.
DR GO; GO:0009113; P:purine nucleobase biosynthetic process; IDA:PomBase.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IBA:GO_Central.
DR CDD; cd02196; PurM; 1.
DR Gene3D; 3.30.1330.10; -; 1.
DR Gene3D; 3.30.1490.20; -; 1.
DR Gene3D; 3.90.600.10; -; 1.
DR Gene3D; 3.90.650.10; -; 1.
DR HAMAP; MF_00741; AIRS; 1.
DR HAMAP; MF_00138; GARS; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR020561; PRibGlycinamid_synth_ATP-grasp.
DR InterPro; IPR000115; PRibGlycinamide_synth.
DR InterPro; IPR020560; PRibGlycinamide_synth_C-dom.
DR InterPro; IPR037123; PRibGlycinamide_synth_C_sf.
DR InterPro; IPR020559; PRibGlycinamide_synth_CS.
DR InterPro; IPR020562; PRibGlycinamide_synth_N.
DR InterPro; IPR010918; PurM-like_C_dom.
DR InterPro; IPR036676; PurM-like_C_sf.
DR InterPro; IPR016188; PurM-like_N.
DR InterPro; IPR036921; PurM-like_N_sf.
DR InterPro; IPR004733; PurM_cligase.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR PANTHER; PTHR10520; PTHR10520; 1.
DR Pfam; PF00586; AIRS; 1.
DR Pfam; PF02769; AIRS_C; 1.
DR Pfam; PF01071; GARS_A; 1.
DR Pfam; PF02843; GARS_C; 1.
DR Pfam; PF02844; GARS_N; 1.
DR SMART; SM01210; GARS_C; 1.
DR SUPFAM; SSF51246; SSF51246; 1.
DR SUPFAM; SSF52440; SSF52440; 1.
DR SUPFAM; SSF55326; SSF55326; 1.
DR SUPFAM; SSF56042; SSF56042; 1.
DR TIGRFAMs; TIGR00877; purD; 1.
DR TIGRFAMs; TIGR00878; purM; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS00184; GARS; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Ligase; Magnesium; Manganese; Metal-binding;
KW Multifunctional enzyme; Nucleotide-binding; Purine biosynthesis;
KW Reference proteome.
FT CHAIN 1..788
FT /note="Bifunctional purine biosynthetic protein ADE1"
FT /id="PRO_0000454642"
FT DOMAIN 115..321
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT REGION 1..430
FT /note="GARS"
FT /evidence="ECO:0000255"
FT REGION 437..769
FT /note="AIRS"
FT /evidence="ECO:0000255"
FT BINDING 141..202
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 291
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 293
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
SQ SEQUENCE 788 AA; 85231 MW; 0FDE64EEA5F9095D CRC64;
MEPIIALLIG NGGREHTIAW KLCESPLISK VYVAPGNGGT ASNGAESKME NVNIGVCDFE
QLVKFALDKD VNLVIPGPEL PLVEGIEGHF RRVGIPCFGP SALAARMEGS KVFSKDFMHR
NNIPTAVYKS FSNYDHAKSF LDTCTFDVVI KADGLAAGKG VIIPKTKKEA FEALESIMLN
EEFGSAGKNV VIEELLEGEE LSILTFSDGY TCRSLPPAQD HKRAFDGDKG PNTGGMGCYA
PTPVASPKLL ETVQSTIIQP TIDGMRHEGY PLVGILFTGL MLTPSGPRVL EYNVRFGDPE
TQAVLPLLES DLAEIILACV NHRLDAIDIV ISRKFSCAVV CVAGGYPGPY NKGDIITFDA
LKDKNTRIFH AGTSIRDGNV VTNGGRVLAV EATGDSVEAA VRLAYEGVKT VHFDKMFYRK
DIAHHALNPK RKTREILTYE NSGVSVDNGN EFVQRIKDLV KSTRRPGADA DIGGFGGIFD
LKQAGWNDPL LVSATDGVGS KLLIALSLNK HDTVGIDLVA MNVNDLVVQG AEPLIFLDYF
ATGSLDLKVS TSFVEGVVKG CKQAGCALVG GETSEMPGLY HDGHYDANGT SVGAVSRDDI
LPKPESFSKG DILLGLASDG VHSNGYSLVR KIVEYSDLEY TSVCPWDKNV RLGDSLLIPT
RIYVKPLLHV IRKNIVKGMA HITGGGLVEN VPRMLPSHLN AIIDVDTWEV PEVFKWLKDA
GNVPISDMAR TFNMGIGMVV AVASEDAEET MKELTSVGET VYRIGQLVDK ESSSERCHLV
NLNKWETF
