ID A0A3P3RDE5_9EURY Unreviewed; 232 AA.
AC A0A3P3RDE5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Riboflavin kinase {ECO:0000256|ARBA:ARBA00017394, ECO:0000256|HAMAP-Rule:MF_01285};
DE Short=RFK {ECO:0000256|HAMAP-Rule:MF_01285};
DE EC=2.7.1.161 {ECO:0000256|ARBA:ARBA00011987, ECO:0000256|HAMAP-Rule:MF_01285};
DE AltName: Full=CTP-dependent riboflavin kinase {ECO:0000256|ARBA:ARBA00030544, ECO:0000256|HAMAP-Rule:MF_01285};
DE AltName: Full=CTP:riboflavin 5'-phosphotransferase {ECO:0000256|ARBA:ARBA00033116, ECO:0000256|HAMAP-Rule:MF_01285};
DE AltName: Full=Flavokinase {ECO:0000256|ARBA:ARBA00029789, ECO:0000256|HAMAP-Rule:MF_01285};
GN Name=ribK {ECO:0000256|HAMAP-Rule:MF_01285};
GN ORFNames=EIK79_08955 {ECO:0000313|EMBL:RRJ30750.1};
OS Halomarina oriensis.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Halomarina.
OX NCBI_TaxID=671145 {ECO:0000313|EMBL:RRJ30750.1, ECO:0000313|Proteomes:UP000282322};
RN [1] {ECO:0000313|EMBL:RRJ30750.1, ECO:0000313|Proteomes:UP000282322}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPP-AMP-1 {ECO:0000313|EMBL:RRJ30750.1,
RC ECO:0000313|Proteomes:UP000282322};
RA Pal Y., Srinivasana K., Verma A., Kumar P.;
RT "Taxonoimc description of Halomarina strain SPP-AMP-1.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the CTP-dependent phosphorylation of riboflavin
CC (vitamin B2) to form flavin mononucleotide (FMN).
CC {ECO:0000256|ARBA:ARBA00003072, ECO:0000256|HAMAP-Rule:MF_01285}.
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 Evidence={ECO:0000256|ARBA:ARBA00000663, ECO:0000256|HAMAP-
CC Rule:MF_01285};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01285};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01285};
CC -!- PATHWAY: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin
CC (CTP route): step 1/1. {ECO:0000256|ARBA:ARBA00005219,
CC ECO:0000256|HAMAP-Rule:MF_01285}.
CC -!- SIMILARITY: Belongs to the archaeal riboflavin kinase family.
CC {ECO:0000256|ARBA:ARBA00006428, ECO:0000256|HAMAP-Rule:MF_01285}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01285}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RRJ30750.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; RRCH01000019; RRJ30750.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P3RDE5; -.
DR OrthoDB; 30955at2157; -.
DR UniPathway; UPA00276; UER00929.
DR Proteomes; UP000282322; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008531; F:riboflavin kinase activity; IEA:InterPro.
DR GO; GO:0009398; P:FMN biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:InterPro.
DR CDD; cd00090; HTH_ARSR; 1.
DR Gene3D; 2.40.30.30; Riboflavin kinase-like; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR HAMAP; MF_01285; Riboflavin_kinase; 1.
DR InterPro; IPR011991; ArsR-like_HTH.
DR InterPro; IPR039063; RibK_CTP-dep.
DR InterPro; IPR023470; Riboflavin_kinase_archaeal.
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; RIBOFLAVIN KINASE; 1.
DR PANTHER; PTHR40706:SF1; RIBOFLAVIN KINASE; 1.
DR Pfam; PF01982; CTP-dep_RFKase; 1.
DR Pfam; PF12840; HTH_20; 1.
DR SUPFAM; SSF82114; Riboflavin kinase-like; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
PE 3: Inferred from homology;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW Rule:MF_01285};
KW FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|HAMAP-Rule:MF_01285};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_01285};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01285};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01285};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01285};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01285}.
FT DOMAIN 105..228
FT /note="Riboflavin kinase"
FT /evidence="ECO:0000259|Pfam:PF01982"
FT BINDING 108..113
FT /ligand="CDP"
FT /ligand_id="ChEBI:CHEBI:58069"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01285"
FT BINDING 137
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01285"
FT BINDING 139
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01285"
FT BINDING 199
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01285"
FT BINDING 207
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01285"
FT BINDING 212..215
FT /ligand="CDP"
FT /ligand_id="ChEBI:CHEBI:58069"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01285"
SQ SEQUENCE 232 AA; 25550 MW; 854EB3F965383A5C CRC64;
MAESTGVAVG ADEREVLKLL ALDGALAGRA RVTCSELGDR LSVSTQTVSR RLQRLEDATL
IERRIVSDGQ LVETTESGER VLRGEYADYR RLFEHGQEIE LTGAVTGGMG EGSHYISLPG
YMRQFESKLG YTPFAGTLNV ELDDESAHTR AGLESIEPIR IDGWENDDRT YGPAFCWSAS
VEADGQMYES AHVIAPERTH HADDQLEVIA PDKLRDVLSI DDGDTLTTYV EK
//
