RIFK_HALMA
ID RIFK_HALMA Reviewed; 320 AA.
AC Q5UY62;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Riboflavin kinase;
DE Short=RFK;
DE EC=2.7.1.161;
DE AltName: Full=CTP-dependent riboflavin kinase;
DE AltName: Full=CTP:riboflavin 5'-phosphotransferase;
DE AltName: Full=Flavokinase;
GN Name=ribK; OrderedLocusNames=rrnAC3074;
OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS B-1809) (Halobacterium marismortui).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=272569;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=15520287; DOI=10.1101/gr.2700304;
RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA Hood L., Ng W.V.;
RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT Dead Sea.";
RL Genome Res. 14:2221-2234(2004).
CC -!- FUNCTION: Catalyzes the CTP-dependent phosphorylation of riboflavin
CC (vitamin B2) to form flavin mononucleotide (FMN). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CTP + riboflavin = CDP + FMN + H(+); Xref=Rhea:RHEA:25021,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:37563, ChEBI:CHEBI:57986,
CC ChEBI:CHEBI:58069, ChEBI:CHEBI:58210; EC=2.7.1.161;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin
CC (CTP route): step 1/1.
CC -!- SIMILARITY: Belongs to the archaeal riboflavin kinase family.
CC {ECO:0000305}.
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DR EMBL; AY596297; AAV47791.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5UY62; -.
DR SMR; Q5UY62; -.
DR STRING; 272569.rrnAC3074; -.
DR EnsemblBacteria; AAV47791; AAV47791; rrnAC3074.
DR KEGG; hma:rrnAC3074; -.
DR PATRIC; fig|272569.17.peg.3620; -.
DR eggNOG; arCOG01904; Archaea.
DR HOGENOM; CLU_088476_0_0_2; -.
DR UniPathway; UPA00276; UER00929.
DR Proteomes; UP000001169; Chromosome I.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0008531; F:riboflavin kinase activity; IEA:InterPro.
DR GO; GO:0009398; P:FMN biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:InterPro.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 2.40.30.30; -; 1.
DR InterPro; IPR039063; RibK_CTP-dep.
DR InterPro; IPR023602; Riboflavin_kinase_CTP-dep.
DR InterPro; IPR023465; Riboflavin_kinase_dom_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR40706; PTHR40706; 1.
DR Pfam; PF01982; CTP-dep_RFKase; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF82114; SSF82114; 1.
PE 3: Inferred from homology;
KW Flavoprotein; FMN; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..320
FT /note="Riboflavin kinase"
FT /id="PRO_0000322084"
FT REGION 1..186
FT /note="H-T-H motif-like"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..320
FT /note="Riboflavin kinase"
FT COMPBIAS 8..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 196..201
FT /ligand="CDP"
FT /ligand_id="ChEBI:CHEBI:58069"
FT /evidence="ECO:0000250"
FT BINDING 225
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 287
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 295
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 300..303
FT /ligand="CDP"
FT /ligand_id="ChEBI:CHEBI:58069"
FT /evidence="ECO:0000250"
SQ SEQUENCE 320 AA; 35682 MW; 5C62619A06C09426 CRC64;
MRTRGSRNWR SRASSGSGTR SWSIEATDRN LSQQCDVAEH VRQRVKLYPA QTVKRAFRTN
PVSVSLRSKS GMHSTFGMLI RRESLLQRMA ESTGQGVGRD ELATLKLLAL DGALDESTKV
SCADLAERLD ASNQTASRRL QRLEDAGLLA RDIVSDGQEV ELTGDGERRL QSEYADYRRI
FESDASVDLT GVVTSGMGEG RHYITLPGYM EQFIERLGYE PFAGTLNLEL TAESVRKRAR
MSAIEPVTIE GWEDDERTYG PAYCYPASIE GSDSEYEPAH VIAPERTHHG EEQLEVIAPE
KLREVLELAD GDEVIVHVSE
