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Riboflavin kinase (EC 2.7.1.26) (ATP:riboflavin 5'-phosphotransferase) (Flavin mononucleotide kinase 1) (Flavokinase)

 RIFK_SCHPO              Reviewed;         163 AA.
O74866;
31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
11-DEC-2019, entry version 123.
RecName: Full=Riboflavin kinase;
EC=2.7.1.26;
AltName: Full=ATP:riboflavin 5'-phosphotransferase;
AltName: Full=Flavin mononucleotide kinase 1;
AltName: Full=Flavokinase;
Name=fmn1; ORFNames=SPCC18.16c;
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
Schizosaccharomyces.
NCBI_TaxID=284812;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=972 / ATCC 24843;
PubMed=11859360; DOI=10.1038/nature724;
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
Nurse P.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
[2]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
PubMed=12595258; DOI=10.1016/s0022-2836(03)00059-7;
Bauer S., Kemter K., Bacher A., Huber R., Fischer M., Steinbacher S.;
"Crystal structure of Schizosaccharomyces pombe riboflavin kinase reveals a
novel ATP and riboflavin-binding fold.";
J. Mol. Biol. 326:1463-1473(2003).
-!- FUNCTION: Catalyzes the phosphorylation of riboflavin (vitamin B2) to
form flavin mononucleotide (FMN) coenzyme.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + riboflavin = ADP + FMN + H(+); Xref=Rhea:RHEA:14357,
ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57986,
ChEBI:CHEBI:58210, ChEBI:CHEBI:456216; EC=2.7.1.26;
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Note=Binds 1 zinc ion per subunit.;
-!- PATHWAY: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin
(ATP route): step 1/1.
-!- SUBUNIT: Monomer.
-!- SIMILARITY: Belongs to the flavokinase family. {ECO:0000305}.
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EMBL; CU329672; CAA21430.1; -; Genomic_DNA.
PIR; T41159; T41159.
RefSeq; NP_588395.1; NM_001023386.2.
PDB; 1N05; X-ray; 2.10 A; A=1-163.
PDB; 1N06; X-ray; 2.00 A; A/B=1-163.
PDB; 1N07; X-ray; 2.45 A; A/B=1-163.
PDB; 1N08; X-ray; 1.60 A; A/B=1-163.
PDBsum; 1N05; -.
PDBsum; 1N06; -.
PDBsum; 1N07; -.
PDBsum; 1N08; -.
SMR; O74866; -.
STRING; 4896.SPCC18.16c.1; -.
iPTMnet; O74866; -.
MaxQB; O74866; -.
PaxDb; O74866; -.
PRIDE; O74866; -.
EnsemblFungi; SPCC18.16c.1; SPCC18.16c.1:pep; SPCC18.16c.
GeneID; 2539192; -.
KEGG; spo:SPCC18.16c; -.
EuPathDB; FungiDB:SPCC18.16c; -.
PomBase; SPCC18.16c; fmn1.
HOGENOM; HOG000260803; -.
InParanoid; O74866; -.
KO; K00861; -.
OMA; EDIRVDC; -.
PhylomeDB; O74866; -.
BRENDA; 2.7.1.26; 5613.
Reactome; R-SPO-196843; Vitamin B2 (riboflavin) metabolism.
UniPathway; UPA00276; UER00406.
EvolutionaryTrace; O74866; -.
PRO; PR:O74866; -.
Proteomes; UP000002485; Chromosome III.
GO; GO:0005829; C:cytosol; HDA:PomBase.
GO; GO:0005743; C:mitochondrial inner membrane; ISS:PomBase.
GO; GO:0005634; C:nucleus; HDA:PomBase.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008531; F:riboflavin kinase activity; IDA:PomBase.
GO; GO:0008270; F:zinc ion binding; IDA:PomBase.
GO; GO:0009398; P:FMN biosynthetic process; IDA:PomBase.
GO; GO:0009231; P:riboflavin biosynthetic process; IDA:PomBase.
Gene3D; 2.40.30.30; -; 1.
InterPro; IPR023468; Riboflavin_kinase.
InterPro; IPR015865; Riboflavin_kinase_bac/euk.
InterPro; IPR023465; Riboflavin_kinase_dom_sf.
PANTHER; PTHR22749; PTHR22749; 1.
Pfam; PF01687; Flavokinase; 1.
SMART; SM00904; Flavokinase; 1.
SUPFAM; SSF82114; SSF82114; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Flavoprotein; FMN; Kinase; Metal-binding;
Nucleotide-binding; Reference proteome; Transferase; Zinc.
CHAIN 1..163
/note="Riboflavin kinase"
/id="PRO_0000194151"
ACT_SITE 96
/note="Nucleophile"
/evidence="ECO:0000305"
METAL 45
/note="Zinc"
STRAND 24..31
/evidence="ECO:0000244|PDB:1N08"
STRAND 34..36
/evidence="ECO:0000244|PDB:1N08"
HELIX 38..41
/evidence="ECO:0000244|PDB:1N08"
STRAND 46..48
/evidence="ECO:0000244|PDB:1N08"
HELIX 50..52
/evidence="ECO:0000244|PDB:1N08"
TURN 53..59
/evidence="ECO:0000244|PDB:1N08"
STRAND 62..71
/evidence="ECO:0000244|PDB:1N08"
STRAND 74..84
/evidence="ECO:0000244|PDB:1N08"
STRAND 93..99
/evidence="ECO:0000244|PDB:1N08"
STRAND 111..121
/evidence="ECO:0000244|PDB:1N08"
HELIX 129..147
/evidence="ECO:0000244|PDB:1N08"
HELIX 150..153
/evidence="ECO:0000244|PDB:1N08"
HELIX 154..157
/evidence="ECO:0000244|PDB:1N08"
HELIX 159..161
/evidence="ECO:0000244|PDB:1N08"
SEQUENCE 163 AA; 18913 MW; ADFD49D12FD7472F CRC64;
MTVNLEEKRP EIVGPEKVQS PYPIRFEGKV VHGFGRGSKE LGIPTANISE DAIQELLRYR
DSGVYFGYAM VQKRVFPMVM SVGWNPYYKN KLRSAEVHLI ERQGEDFYEE IMRVIVLGYI
RPELNYAGLD KLIEDIHTDI RVALNSMDRP SYSSYKKDPF FKV


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