GenomeNet

Database: UniProt
Entry: P20772
LinkDB: P20772
Original site: P20772 
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   16-JAN-2019, entry version 144.
DE   RecName: Full=Bifunctional purine biosynthetic protein ADE1;
DE   Includes:
DE     RecName: Full=Phosphoribosylamine--glycine ligase;
DE              EC=6.3.4.13;
DE     AltName: Full=Glycinamide ribonucleotide synthetase;
DE              Short=GARS;
DE     AltName: Full=Phosphoribosylglycinamide synthetase;
DE   Includes:
DE     RecName: Full=Phosphoribosylformylglycinamidine cyclo-ligase;
DE              EC=6.3.3.1;
DE     AltName: Full=AIR synthase;
DE              Short=AIRS;
DE     AltName: Full=Phosphoribosyl-aminoimidazole synthetase;
GN   Name=ade1; ORFNames=SPBC405.01, SPBC4C3.02c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; 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
RT   pathway 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.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-phospho-D-ribosylamine + ATP + glycine = ADP + H(+) +
CC         N(1)-(5-phospho-D-ribosyl)glycinamide + phosphate;
CC         Xref=Rhea:RHEA:17453, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57305, ChEBI:CHEBI:58089,
CC         ChEBI:CHEBI:58457, ChEBI:CHEBI:456216; EC=6.3.4.13;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-(formamido)-N(1)-(5-phospho-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:58478,
CC         ChEBI:CHEBI:137981, ChEBI:CHEBI:456216; EC=6.3.3.1;
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC       5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-
CC       phospho-D-ribosyl)glycinamide: step 2/2.
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC       N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-
CC       ribose 1-diphosphate: step 2/2.
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}.
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   ProteinModelPortal; P20772; -.
DR   SMR; P20772; -.
DR   BioGrid; 277549; 1.
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   EuPathDB; FungiDB:SPBC405.01; -.
DR   PomBase; SPBC405.01; ade1.
DR   HOGENOM; HOG000030315; -.
DR   InParanoid; P20772; -.
DR   OMA; LLERHNC; -.
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   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Ligase; Manganese; Metal-binding;
KW   Multifunctional enzyme; Nucleotide-binding; Purine biosynthesis;
KW   Reference proteome.
FT   CHAIN         1    788       Bifunctional purine biosynthetic protein
FT                                ADE1.
FT                                /FTId=PRO_0000074939.
FT   DOMAIN      115    321       ATP-grasp.
FT   NP_BIND     141    202       ATP. {ECO:0000250}.
FT   REGION        1    430       GARS.
FT   REGION      440    750       AIRS.
FT   METAL       291    291       Manganese. {ECO:0000250}.
FT   METAL       293    293       Manganese. {ECO:0000250}.
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
//
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