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Riboflavin kinase (RFK) (EC 2.7.1.161) (CTP-dependent riboflavin kinase) (CTP:riboflavin 5'-phosphotransferase) (Flavokinase)

 I3R1E0_HALMT            Unreviewed;       237 AA.
I3R1E0;
19-FEB-2014, integrated into UniProtKB/TrEMBL.
19-FEB-2014, sequence version 1.
05-DEC-2018, entry version 42.
RecName: Full=Riboflavin kinase {ECO:0000256|HAMAP-Rule:MF_01285};
Short=RFK {ECO:0000256|HAMAP-Rule:MF_01285};
EC=2.7.1.161 {ECO:0000256|HAMAP-Rule:MF_01285};
AltName: Full=CTP-dependent riboflavin kinase {ECO:0000256|HAMAP-Rule:MF_01285};
AltName: Full=CTP:riboflavin 5'-phosphotransferase {ECO:0000256|HAMAP-Rule:MF_01285};
AltName: Full=Flavokinase {ECO:0000256|HAMAP-Rule:MF_01285};
Name=ribK {ECO:0000256|HAMAP-Rule:MF_01285};
OrderedLocusNames=HFX_0311 {ECO:0000313|EMBL:AFK18050.1};
ORFNames=BM92_07690 {ECO:0000313|EMBL:AHZ22537.1},
C439_08825 {ECO:0000313|EMBL:EMA02674.1};
Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC
14739 / NCIMB 2177 / R-4) (Halobacterium mediterranei).
Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria;
Haloferacales; Haloferacaceae; Haloferax.
NCBI_TaxID=523841 {ECO:0000313|EMBL:AFK18050.1, ECO:0000313|Proteomes:UP000006469};
[1] {ECO:0000313|EMBL:AFK18050.1}
NUCLEOTIDE SEQUENCE.
STRAIN=CGMCC 1.2087 {ECO:0000313|EMBL:AFK18050.1};
PubMed=22247127; DOI=10.1128/AEM.07114-11;
Cai S., Cai L., Liu H., Liu X., Han J., Zhou J., Xiang H.;
"Identification of the haloarchaeal phasin (PhaP) that functions in
polyhydroxyalkanoate accumulation and granule formation in Haloferax
mediterranei.";
Appl. Environ. Microbiol. 78:1946-1952(2012).
[2] {ECO:0000313|EMBL:AFK18050.1, ECO:0000313|Proteomes:UP000006469}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 /
R-4 {ECO:0000313|Proteomes:UP000006469}, and
CGMCC 1.2087 {ECO:0000313|EMBL:AFK18050.1};
PubMed=22843593; DOI=10.1128/JB.00880-12;
Han J., Zhang F., Hou J., Liu X., Li M., Liu H., Cai L., Zhang B.,
Chen Y., Zhou J., Hu S., Xiang H.;
"Complete genome sequence of the metabolically versatile halophilic
archaeon Haloferax mediterranei, a poly(3-hydroxybutyrate-co-3-
hydroxyvalerate) producer.";
J. Bacteriol. 194:4463-4464(2012).
[3] {ECO:0000313|Proteomes:UP000011603}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 /
R-4 {ECO:0000313|Proteomes:UP000011603};
Becker E.A., Seitzer P., Tritt A., Larsen D., Yao A., Wu D.,
Darling A., Eisen J.A., Facciotti M.T.;
Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
[4] {ECO:0000313|EMBL:EMA02674.1, ECO:0000313|Proteomes:UP000011603}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 33500 {ECO:0000313|EMBL:EMA02674.1}, and
ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4
{ECO:0000313|Proteomes:UP000011603};
PubMed=25393412;
Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I.,
Wu D., Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
"Phylogenetically driven sequencing of extremely halophilic archaea
reveals strategies for static and dynamic osmo-response.";
PLoS Genet. 10:E1004784-E1004784(2014).
[5] {ECO:0000313|EMBL:AHZ22537.1, ECO:0000313|Proteomes:UP000027075}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 33500 {ECO:0000313|EMBL:AHZ22537.1}, and
ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4
{ECO:0000313|Proteomes:UP000027075};
Bautista V.;
"Transcriptional profiles of Haloferax mediterranei on the basis of
nitrogen availability.";
Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
[6] {ECO:0000313|EMBL:AFK18050.1}
NUCLEOTIDE SEQUENCE.
STRAIN=CGMCC 1.2087;
Wang L., Yang H., Xiang H.;
Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes the CTP-dependent phosphorylation of
riboflavin (vitamin B2) to form flavin mononucleotide (FMN).
{ECO:0000256|HAMAP-Rule:MF_01285}.
-!- CATALYTIC ACTIVITY:
Reaction=CTP + riboflavin = CDP + FMN + H(+);
Xref=Rhea:RHEA:25021, ChEBI:CHEBI:15378, ChEBI:CHEBI:37563,
ChEBI:CHEBI:57986, ChEBI:CHEBI:58069, ChEBI:CHEBI:58210;
EC=2.7.1.161; Evidence={ECO:0000256|HAMAP-Rule:MF_01285};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_01285};
Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-
Rule:MF_01285};
-!- PATHWAY: Cofactor biosynthesis; FMN biosynthesis; FMN from
riboflavin (CTP route): step 1/1. {ECO:0000256|HAMAP-
Rule:MF_01285}.
-!- SIMILARITY: Belongs to the archaeal riboflavin kinase family.
{ECO:0000256|HAMAP-Rule:MF_01285}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01285}.
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EMBL; CP001868; AFK18050.1; -; Genomic_DNA.
EMBL; CP007551; AHZ22537.1; -; Genomic_DNA.
EMBL; AOLO01000007; EMA02674.1; -; Genomic_DNA.
RefSeq; WP_004058219.1; NZ_CP007551.1.
EnsemblBacteria; AFK18050; AFK18050; HFX_0311.
EnsemblBacteria; AHZ22537; AHZ22537; BM92_07690.
EnsemblBacteria; EMA02674; EMA02674; C439_08825.
GeneID; 13026481; -.
KEGG; hme:HFX_0311; -.
PATRIC; fig|523841.21.peg.1792; -.
KO; K07732; -.
OMA; FTPYPGT; -.
OrthoDB; POG093Z0F8C; -.
BioCyc; HMED523841:G1HBL-307-MONOMER; -.
UniPathway; UPA00276; UER00929.
Proteomes; UP000006469; Chromosome.
Proteomes; UP000011603; Unassembled WGS sequence.
Proteomes; UP000027075; Chromosome.
GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-UniRule.
GO; GO:0008531; F:riboflavin kinase activity; IEA:InterPro.
GO; GO:0009398; P:FMN biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0009231; P:riboflavin biosynthetic process; IEA:InterPro.
CDD; cd00090; HTH_ARSR; 1.
Gene3D; 1.10.10.10; -; 1.
Gene3D; 2.40.30.30; -; 1.
HAMAP; MF_01285; Riboflavin_kinase; 1.
InterPro; IPR011991; ArsR-like_HTH.
InterPro; IPR039063; RibK_CTP-dep.
InterPro; IPR023470; Riboflavin_kinase_archaeal.
InterPro; IPR023602; Riboflavin_kinase_CTP-dep.
InterPro; IPR023465; Riboflavin_kinase_dom_sf.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
PANTHER; PTHR40706; PTHR40706; 1.
Pfam; PF01982; CTP-dep_RFKase; 1.
SUPFAM; SSF46785; SSF46785; 1.
SUPFAM; SSF82114; SSF82114; 1.
3: Inferred from homology;
Coiled coil {ECO:0000256|SAM:Coils};
Complete proteome {ECO:0000313|Proteomes:UP000006469};
Flavoprotein {ECO:0000256|HAMAP-Rule:MF_01285};
FMN {ECO:0000256|HAMAP-Rule:MF_01285};
Kinase {ECO:0000256|HAMAP-Rule:MF_01285, ECO:0000313|EMBL:AFK18050.1};
Magnesium {ECO:0000256|HAMAP-Rule:MF_01285};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_01285};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01285};
Reference proteome {ECO:0000313|Proteomes:UP000006469};
Transferase {ECO:0000256|HAMAP-Rule:MF_01285,
ECO:0000313|EMBL:AFK18050.1}.
DOMAIN 106 231 CTP-dep_RFKase.
{ECO:0000259|Pfam:PF01982}.
NP_BIND 109 114 CDP. {ECO:0000256|HAMAP-Rule:MF_01285}.
NP_BIND 213 216 CDP. {ECO:0000256|HAMAP-Rule:MF_01285}.
COILED 39 59 {ECO:0000256|SAM:Coils}.
METAL 138 138 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_01285}.
METAL 140 140 Magnesium. {ECO:0000256|HAMAP-
Rule:MF_01285}.
BINDING 200 200 FMN. {ECO:0000256|HAMAP-Rule:MF_01285}.
BINDING 208 208 FMN. {ECO:0000256|HAMAP-Rule:MF_01285}.
SEQUENCE 237 AA; 26109 MW; 47AD46D8AAB12914 CRC64;
MSESAVAATV GFDELATLKL VALDGGRSGP VKVSCSGLAN RLDVSNQTAS RRLQRLEEAD
FIDREVVADG QWITITDSGE SALRHEYADY RRIFETPSVV VLEGEVTGGM GEGRHYISLP
GYMEQFTERL GYEPFPGTLN VRLDDDAIRT RAGMSALDAV PIDGWEDDER TFGPATCYAA
VIEVGDESYD PVHIIVPERT HHDESQLEII APDKLRDELD LSDGDTITVR VEEADFE


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