PUR9_SCHPO
ID PUR9_SCHPO Reviewed; 585 AA.
AC O74928; P78892;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Bifunctional purine biosynthesis protein ade10;
DE Includes:
DE RecName: Full=Phosphoribosylaminoimidazolecarboxamide formyltransferase;
DE EC=2.1.2.3;
DE AltName: Full=5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase;
DE AltName: Full=AICAR transformylase;
DE Includes:
DE RecName: Full=IMP cyclohydrolase;
DE EC=3.5.4.10;
DE AltName: Full=ATIC;
DE AltName: Full=IMP synthase;
DE AltName: Full=Inosinicase;
GN Name=ade10; ORFNames=SPCPB16A4.03c;
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=9802209;
RX DOI=10.1002/(sici)1097-0061(1998100)14:14<1307::aid-yea308>3.0.co;2-4;
RA Liedtke C., Schmidt H.;
RT "Molecular cloning and sequence analysis of the Schizosaccharomyces pombe
RT ade10+ gene.";
RL Yeast 14:1307-1310(1998).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 166-585.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D-
CC ribosyl)imidazole-4-carboxamide = (6S)-5,6,7,8-tetrahydrofolate + 5-
CC formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide;
CC Xref=Rhea:RHEA:22192, ChEBI:CHEBI:57453, ChEBI:CHEBI:57454,
CC ChEBI:CHEBI:58467, ChEBI:CHEBI:58475; EC=2.1.2.3;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + IMP = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-
CC carboxamide; Xref=Rhea:RHEA:18445, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:58053, ChEBI:CHEBI:58467; EC=3.5.4.10;
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-
CC 1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route):
CC step 1/1.
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; IMP
CC from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide: step
CC 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- DOMAIN: The IMP cyclohydrolase activity resides in the N-terminal
CC region. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PurH family. {ECO:0000305}.
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DR EMBL; Y16419; CAA76207.1; -; Genomic_DNA.
DR EMBL; CU329672; CAC39322.1; -; Genomic_DNA.
DR EMBL; D89243; BAA13904.1; -; mRNA.
DR PIR; T43150; T43150.
DR RefSeq; NP_588027.1; NM_001023018.2.
DR AlphaFoldDB; O74928; -.
DR SMR; O74928; -.
DR BioGRID; 276129; 14.
DR STRING; 4896.SPCPB16A4.03c.1; -.
DR iPTMnet; O74928; -.
DR MaxQB; O74928; -.
DR PaxDb; O74928; -.
DR PRIDE; O74928; -.
DR EnsemblFungi; SPCPB16A4.03c.1; SPCPB16A4.03c.1:pep; SPCPB16A4.03c.
DR GeneID; 2539569; -.
DR KEGG; spo:SPCPB16A4.03c; -.
DR PomBase; SPCPB16A4.03c; ade10.
DR VEuPathDB; FungiDB:SPCPB16A4.03c; -.
DR eggNOG; KOG2555; Eukaryota.
DR HOGENOM; CLU_016316_3_2_1; -.
DR InParanoid; O74928; -.
DR OMA; WRVAKFV; -.
DR PhylomeDB; O74928; -.
DR Reactome; R-SPO-73817; Purine ribonucleoside monophosphate biosynthesis.
DR UniPathway; UPA00074; UER00133.
DR UniPathway; UPA00074; UER00135.
DR PRO; PR:O74928; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0003937; F:IMP cyclohydrolase activity; IDA:PomBase.
DR GO; GO:0004643; F:phosphoribosylaminoimidazolecarboxamide formyltransferase activity; IDA:PomBase.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IMP:PomBase.
DR GO; GO:0006188; P:IMP biosynthetic process; IMP:PomBase.
DR Gene3D; 1.10.287.440; -; 1.
DR Gene3D; 3.40.140.20; -; 2.
DR Gene3D; 3.40.50.1380; -; 1.
DR HAMAP; MF_00139; PurH; 1.
DR InterPro; IPR024051; AICAR_Tfase_dup_dom_sf.
DR InterPro; IPR024050; AICAR_Tfase_insert_dom_sf.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR InterPro; IPR011607; MGS-like_dom.
DR InterPro; IPR036914; MGS-like_dom_sf.
DR InterPro; IPR002695; PurH-like.
DR PANTHER; PTHR11692; PTHR11692; 1.
DR Pfam; PF01808; AICARFT_IMPCHas; 1.
DR Pfam; PF02142; MGS; 1.
DR PIRSF; PIRSF000414; AICARFT_IMPCHas; 1.
DR SMART; SM00798; AICARFT_IMPCHas; 1.
DR SMART; SM00851; MGS; 1.
DR SUPFAM; SSF52335; SSF52335; 1.
DR SUPFAM; SSF53927; SSF53927; 1.
DR TIGRFAMs; TIGR00355; purH; 1.
DR PROSITE; PS51855; MGS; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Multifunctional enzyme; Purine biosynthesis; Reference proteome;
KW Transferase.
FT CHAIN 1..585
FT /note="Bifunctional purine biosynthesis protein ade10"
FT /id="PRO_0000192158"
FT DOMAIN 1..142
FT /note="MGS-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
FT CONFLICT 404
FT /note="K -> Q (in Ref. 3; BAA13904)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 585 AA; 64123 MW; 103031D3F957529F CRC64;
MYALLSVYDK TGLLELAKAL TSKGVKLLGS GGTAKMIRES GMEVADVSSI TNAPEILGGR
VKTLHPAVHG GILARDIPSD EKDLVEQSIE KIDIVVCNLY PFRETIAKPN VTIPEAVEEI
DIGGVTLLRA AAKNHARVTI LSDPADYATF TDKFLSDKLT QDDRNTYALK AFASTASYDA
AITDYFRKQY AAGVDQLTLR YGANPHQSPA QAFMEQGPLP FKVLCGSPGY INLMDALNSW
PLVKELRENI GIPAAASFKH VSPAGAAVGL PLSDVEKKVY FVSDITEFTP LACAYARARG
ADRMSSFGDF IALSDTVDVC TARIISREVS DGVIAPGYEP EALELLKKKK GGKYCVLQMD
PKYVPAEIET RQVYGISLQQ HRNHAKIDFS LFEKVVSKNK DLPKSALIDL VIATTALKYT
QSNSVCYAKN GMVVGLGAGQ QSRIHCNRLA GDKADNWWLR HHPKVLGMQF KKSAKRPEKS
NAIDLYVLDA VPAEGSEREQ WESAFETIPE PLTKKEREEF LATCKDVVCA SDAFFPFPDN
IYRLAQSGVK YVAAPGGSVM DQAVRDTANE FNMVFSEIPL RLFHH
