ID   RIFK_SCHPO              Reviewed;         163 AA.
AC   O74866;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   27-MAR-2024, entry version 140.
DE   RecName: Full=Riboflavin kinase;
DE            EC=2.7.1.26;
DE   AltName: Full=ATP:riboflavin 5'-phosphotransferase;
DE   AltName: Full=Flavin mononucleotide kinase 1;
DE   AltName: Full=Flavokinase;
GN   Name=fmn1; ORFNames=SPCC18.16c;
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   X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
RX   PubMed=12595258; DOI=10.1016/s0022-2836(03)00059-7;
RA   Bauer S., Kemter K., Bacher A., Huber R., Fischer M., Steinbacher S.;
RT   "Crystal structure of Schizosaccharomyces pombe riboflavin kinase reveals a
RT   novel ATP and riboflavin-binding fold.";
RL   J. Mol. Biol. 326:1463-1473(2003).
CC   -!- FUNCTION: Catalyzes the phosphorylation of riboflavin (vitamin B2) to
CC       form flavin mononucleotide (FMN) coenzyme.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + riboflavin = ADP + FMN + H(+); Xref=Rhea:RHEA:14357,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57986,
CC         ChEBI:CHEBI:58210, ChEBI:CHEBI:456216; EC=2.7.1.26;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds 1 zinc ion per subunit.;
CC   -!- PATHWAY: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin
CC       (ATP route): step 1/1.
CC   -!- SUBUNIT: Monomer.
CC   -!- SIMILARITY: Belongs to the flavokinase family. {ECO:0000305}.
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DR   EMBL; CU329672; CAA21430.1; -; Genomic_DNA.
DR   PIR; T41159; T41159.
DR   RefSeq; NP_588395.1; NM_001023386.2.
DR   PDB; 1N05; X-ray; 2.10 A; A=1-163.
DR   PDB; 1N06; X-ray; 2.00 A; A/B=1-163.
DR   PDB; 1N07; X-ray; 2.45 A; A/B=1-163.
DR   PDB; 1N08; X-ray; 1.60 A; A/B=1-163.
DR   PDBsum; 1N05; -.
DR   PDBsum; 1N06; -.
DR   PDBsum; 1N07; -.
DR   PDBsum; 1N08; -.
DR   AlphaFoldDB; O74866; -.
DR   SMR; O74866; -.
DR   STRING; 284812.O74866; -.
DR   iPTMnet; O74866; -.
DR   MaxQB; O74866; -.
DR   PaxDb; 4896-SPCC18-16c-1; -.
DR   EnsemblFungi; SPCC18.16c.1; SPCC18.16c.1:pep; SPCC18.16c.
DR   GeneID; 2539192; -.
DR   KEGG; spo:SPCC18.16c; -.
DR   PomBase; SPCC18.16c; fmn1.
DR   VEuPathDB; FungiDB:SPCC18.16c; -.
DR   eggNOG; KOG3110; Eukaryota.
DR   HOGENOM; CLU_048437_3_2_1; -.
DR   InParanoid; O74866; -.
DR   OMA; YPIRFEG; -.
DR   PhylomeDB; O74866; -.
DR   BRENDA; 2.7.1.26; 5613.
DR   Reactome; R-SPO-196843; Vitamin B2 (riboflavin) metabolism.
DR   UniPathway; UPA00276; UER00406.
DR   EvolutionaryTrace; O74866; -.
DR   PRO; PR:O74866; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISS:PomBase.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008531; F:riboflavin kinase activity; IDA:PomBase.
DR   GO; GO:0008270; F:zinc ion binding; IDA:PomBase.
DR   GO; GO:0009398; P:FMN biosynthetic process; IDA:PomBase.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0009231; P:riboflavin biosynthetic process; IDA:PomBase.
DR   GO; GO:0006771; P:riboflavin metabolic process; IBA:GO_Central.
DR   Gene3D; 2.40.30.30; Riboflavin kinase-like; 1.
DR   InterPro; IPR023468; Riboflavin_kinase.
DR   InterPro; IPR015865; Riboflavin_kinase_bac/euk.
DR   InterPro; IPR023465; Riboflavin_kinase_dom_sf.
DR   PANTHER; PTHR22749:SF6; RIBOFLAVIN KINASE; 1.
DR   PANTHER; PTHR22749; RIBOFLAVIN KINASE/FMN ADENYLYLTRANSFERASE; 1.
DR   Pfam; PF01687; Flavokinase; 1.
DR   SMART; SM00904; Flavokinase; 1.
DR   SUPFAM; SSF82114; Riboflavin kinase-like; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Flavoprotein; FMN; Kinase; Metal-binding;
KW   Nucleotide-binding; Reference proteome; Transferase; Zinc.
FT   CHAIN           1..163
FT                   /note="Riboflavin kinase"
FT                   /id="PRO_0000194151"
FT   ACT_SITE        96
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000305"
FT   BINDING         45
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   STRAND          24..31
FT                   /evidence="ECO:0007829|PDB:1N08"
FT   STRAND          34..36
FT                   /evidence="ECO:0007829|PDB:1N08"
FT   HELIX           38..41
FT                   /evidence="ECO:0007829|PDB:1N08"
FT   STRAND          46..48
FT                   /evidence="ECO:0007829|PDB:1N08"
FT   HELIX           50..52
FT                   /evidence="ECO:0007829|PDB:1N08"
FT   TURN            53..59
FT                   /evidence="ECO:0007829|PDB:1N08"
FT   STRAND          62..71
FT                   /evidence="ECO:0007829|PDB:1N08"
FT   STRAND          74..84
FT                   /evidence="ECO:0007829|PDB:1N08"
FT   STRAND          93..99
FT                   /evidence="ECO:0007829|PDB:1N08"
FT   STRAND          111..121
FT                   /evidence="ECO:0007829|PDB:1N08"
FT   HELIX           129..147
FT                   /evidence="ECO:0007829|PDB:1N08"
FT   HELIX           150..153
FT                   /evidence="ECO:0007829|PDB:1N08"
FT   HELIX           154..157
FT                   /evidence="ECO:0007829|PDB:1N08"
FT   HELIX           159..161
FT                   /evidence="ECO:0007829|PDB:1N08"
SQ   SEQUENCE   163 AA;  18913 MW;  ADFD49D12FD7472F CRC64;
     MTVNLEEKRP EIVGPEKVQS PYPIRFEGKV VHGFGRGSKE LGIPTANISE DAIQELLRYR
     DSGVYFGYAM VQKRVFPMVM SVGWNPYYKN KLRSAEVHLI ERQGEDFYEE IMRVIVLGYI
     RPELNYAGLD KLIEDIHTDI RVALNSMDRP SYSSYKKDPF FKV
//