RIB2_SCHPO
ID RIB2_SCHPO Reviewed; 405 AA.
AC P87241;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Diaminohydroxyphosphoribosylamino-pyrimidine deaminase;
DE Short=DRAP deaminase;
DE EC=3.5.4.26;
DE AltName: Full=Riboflavin-specific deaminase;
GN Name=rib2 {ECO:0000250|UniProtKB:Q12362}; ORFNames=SPCC4G3.16;
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] {ECO:0000312|EMBL:CAB09771.1}
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] {ECO:0000305}
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: Involved in riboflavin biosynthesis. Converts 2,5-diamino-6-
CC (ribosylamino)-4(3H)-pyrimidinone 5'-phosphate into 5-amino-6-
CC (ribosylamino)-2,4(1H,3H)-pyrimidinedione 5'-phosphate (By similarity).
CC {ECO:0000250|UniProtKB:Q12362}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine +
CC H(+) + H2O = 5-amino-6-(5-phospho-D-ribosylamino)uracil + NH4(+);
CC Xref=Rhea:RHEA:21868, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:58453, ChEBI:CHEBI:58614; EC=3.5.4.26;
CC Evidence={ECO:0000250|UniProtKB:O66534};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion. {ECO:0000250};
CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-
CC ribitylamino)uracil from GTP: step 2/4.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. {ECO:0000255}.
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DR EMBL; CU329672; CAB09771.1; -; Genomic_DNA.
DR PIR; T41360; T41360.
DR RefSeq; NP_587822.1; NM_001022815.2.
DR AlphaFoldDB; P87241; -.
DR SMR; P87241; -.
DR STRING; 4896.SPCC4G3.16.1; -.
DR MaxQB; P87241; -.
DR PaxDb; P87241; -.
DR PRIDE; P87241; -.
DR EnsemblFungi; SPCC4G3.16.1; SPCC4G3.16.1:pep; SPCC4G3.16.
DR GeneID; 2539515; -.
DR KEGG; spo:SPCC4G3.16; -.
DR PomBase; SPCC4G3.16; rib2.
DR VEuPathDB; FungiDB:SPCC4G3.16; -.
DR eggNOG; KOG1018; Eukaryota.
DR HOGENOM; CLU_698602_0_0_1; -.
DR InParanoid; P87241; -.
DR OMA; KCEPTDS; -.
DR PhylomeDB; P87241; -.
DR Reactome; R-SPO-8876725; Protein methylation.
DR UniPathway; UPA00275; UER00401.
DR PRO; PR:P87241; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005739; C:mitochondrion; ISO:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0008835; F:diaminohydroxyphosphoribosylaminopyrimidine deaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0009982; F:pseudouridine synthase activity; ISO:PomBase.
DR GO; GO:0018022; P:peptidyl-lysine methylation; IBA:GO_Central.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0031119; P:tRNA pseudouridine synthesis; ISO:PomBase.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR002125; CMP_dCMP_dom.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR InterPro; IPR019410; Methyltransf_16.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR14614; PTHR14614; 1.
DR Pfam; PF00383; dCMP_cyt_deam_1; 1.
DR Pfam; PF10294; Methyltransf_16; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF53927; SSF53927; 1.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Metal-binding; Nucleus; Reference proteome;
KW Riboflavin biosynthesis; Zinc.
FT CHAIN 1..405
FT /note="Diaminohydroxyphosphoribosylamino-pyrimidine
FT deaminase"
FT /id="PRO_0000310862"
FT DOMAIN 256..383
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT ACT_SITE 307
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q12178"
FT BINDING 305
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 335
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 345
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 405 AA; 45605 MW; 47BEB10F087FBE63 CRC64;
MQIPEKYLSS VDNVEEETQI LFALSKQKDA DLGMLDSKQE QIALTIGNKP IKVKQSLQSL
HQSRGSTGSV LWKTSVKVVP WLLQQSWFMN SLTPKTSILE LGSGISGLAG ILLSPFVGNY
VASDKQLYLK KIRENLDQNN ASDVEVHELD WKSTPYPKDW TFDFLDYVLF FDCIYNPHLN
AHLVSCLASL AERYPGMQCL FAQELRDQET LVDFLERVRP YFEVDLIKME EINKTSVASS
TNLPPANMSL FIMKPYNHEE YMLKALNEAK KCEPTDSAFC VGAVIVQNGK IVSTGYSRER
PGNTHAEECA IEKFMLKNPT DSLEGAIMYS TMEPCSKRLS KKVSCTDLIV KQKFSTVVLG
SLEPDIFVKC EGVDLLKKAG IVVIEKLTFQ DDCLREAVRG HPPKH
