ID A0A1S2DF92_9GAMM Unreviewed; 373 AA.
AC A0A1S2DF92;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Bifunctional riboflavin kinase/FMN adenylyltransferase {ECO:0000256|ARBA:ARBA00018483};
DE EC=2.7.1.26 {ECO:0000256|ARBA:ARBA00012105};
DE EC=2.7.7.2 {ECO:0000256|ARBA:ARBA00012393};
DE AltName: Full=Riboflavin biosynthesis protein RibF {ECO:0000256|ARBA:ARBA00032176};
GN ORFNames=BC443_00420 {ECO:0000313|EMBL:OHZ03221.1};
OS Salinicola sp. MIT1003.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Salinicola.
OX NCBI_TaxID=1882734 {ECO:0000313|EMBL:OHZ03221.1, ECO:0000313|Proteomes:UP000179615};
RN [1] {ECO:0000313|EMBL:OHZ03221.1, ECO:0000313|Proteomes:UP000179615}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT1003 {ECO:0000313|EMBL:OHZ03221.1,
RC ECO:0000313|Proteomes:UP000179615};
RA Biller S.;
RT "Membrane vesicles in seawater: heterogeneous DNA content and implications
RT for viral abundance estimates.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the phosphorylation of riboflavin to FMN followed
CC by the adenylation of FMN to FAD. {ECO:0000256|ARBA:ARBA00002121}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + FMN + H(+) = diphosphate + FAD; Xref=Rhea:RHEA:17237,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58210; EC=2.7.7.2;
CC Evidence={ECO:0000256|ARBA:ARBA00001332};
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 Evidence={ECO:0000256|ARBA:ARBA00000372};
CC -!- PATHWAY: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step
CC 1/1. {ECO:0000256|ARBA:ARBA00004726}.
CC -!- PATHWAY: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin
CC (ATP route): step 1/1. {ECO:0000256|ARBA:ARBA00005201}.
CC -!- SIMILARITY: Belongs to the RibF family.
CC {ECO:0000256|ARBA:ARBA00010214}.
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:OHZ03221.1}.
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DR EMBL; MCAP01000010; OHZ03221.1; -; Genomic_DNA.
DR RefSeq; WP_071230758.1; NZ_MCAP01000010.1.
DR AlphaFoldDB; A0A1S2DF92; -.
DR STRING; 1882734.BC443_00420; -.
DR OrthoDB; 9803667at2; -.
DR UniPathway; UPA00276; UER00406.
DR UniPathway; UPA00277; UER00407.
DR Proteomes; UP000179615; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003919; F:FMN adenylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008531; F:riboflavin kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006747; P:FAD biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009398; P:FMN biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:InterPro.
DR CDD; cd02064; FAD_synthetase_N; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 2.40.30.30; Riboflavin kinase-like; 1.
DR InterPro; IPR015864; FAD_synthase.
DR InterPro; IPR023468; Riboflavin_kinase.
DR InterPro; IPR002606; Riboflavin_kinase_bac.
DR InterPro; IPR015865; Riboflavin_kinase_bac/euk.
DR InterPro; IPR023465; Riboflavin_kinase_dom_sf.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR NCBIfam; TIGR00083; ribF; 1.
DR PANTHER; PTHR22749:SF6; RIBOFLAVIN KINASE; 1.
DR PANTHER; PTHR22749; RIBOFLAVIN KINASE/FMN ADENYLYLTRANSFERASE; 1.
DR Pfam; PF06574; FAD_syn; 1.
DR Pfam; PF01687; Flavokinase; 1.
DR SMART; SM00904; Flavokinase; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF82114; Riboflavin kinase-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000179615};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 191..315
FT /note="Riboflavin kinase"
FT /evidence="ECO:0000259|SMART:SM00904"
FT REGION 350..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 373 AA; 40981 MW; A20A2310F6E202E4 CRC64;
MELIRGLHNL PSANDAAQGA AARGCVATIG NFDGVHLGHQ AILEQLQTLS RAQRLPVTVV
IFEPQPREYF AGDQAPPRLT RLRDKVALLK AHGADRILCL PFNDALRSLT AQQFVERVLI
EGLQVRHLVV GDDFRFGCDR AGDFALLQAV GRERGFAVEH TRTFALDDER VSSTRVRTLL
ASGNFFQAAR MLGRPYGYQG RVVRDRQLGR TIGVPTANIP LTRRPMALRG VFACATRLPS
GEWVAGVANI GWRPTVGADR PILEVHLLDR EVELYGQTLT VVPCARLRGE TKFDDFGALV
TQIHRDIDNA RRYFGQRDPH VPEAARADVN HAIEEICAAT LPQAQFPLAS APLSENSHGG
THAGPAPHES RDD
//
