UniProt: D0RRI4

Database: UniProt
Entry: D0RRI4_9PROT

LinkDB:  D0RRI4_9PROT 
Original site:  D0RRI4_9PROT

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Ontology (7)   
   GO (7)   
Chemical reaction (2)   
   KEGG ENZYME (2)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (10)   
   InterPro (7)   
   Pfam (2)   
   SMART (1)   
All databases (20)   

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ID   D0RRI4_9PROT            Unreviewed;       302 AA.
AC   D0RRI4;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=Riboflavin biosynthesis protein {ECO:0000256|PIRNR:PIRNR004491};
DE   Includes:
DE     RecName: Full=Riboflavin kinase {ECO:0000256|PIRNR:PIRNR004491};
DE              EC=2.7.1.26 {ECO:0000256|PIRNR:PIRNR004491};
DE     AltName: Full=Flavokinase {ECO:0000256|PIRNR:PIRNR004491};
DE   Includes:
DE     RecName: Full=FMN adenylyltransferase {ECO:0000256|PIRNR:PIRNR004491};
DE              EC=2.7.7.2 {ECO:0000256|PIRNR:PIRNR004491};
DE     AltName: Full=FAD pyrophosphorylase {ECO:0000256|PIRNR:PIRNR004491};
DE     AltName: Full=FAD synthase {ECO:0000256|PIRNR:PIRNR004491};
GN   ORFNames=HIMB114_00000850 {ECO:0000313|EMBL:EMH79717.1};
OS   alpha proteobacterium HIMB114.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Candidatus Pelagibacterales;
OC   Candidatus Pelagibacteraceae.
OX   NCBI_TaxID=684719 {ECO:0000313|EMBL:EMH79717.1, ECO:0000313|Proteomes:UP000033990};
RN   [1] {ECO:0000313|EMBL:EMH79717.1, ECO:0000313|Proteomes:UP000033990}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HIMB114 {ECO:0000313|EMBL:EMH79717.1,
RC   ECO:0000313|Proteomes:UP000033990};
RA   Rappe M., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EMH79717.1, ECO:0000313|Proteomes:UP000033990}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HIMB114 {ECO:0000313|EMBL:EMH79717.1,
RC   ECO:0000313|Proteomes:UP000033990};
RA   Grote J., Thrash C., Huggett M.J., Landry Z., Carini P., Giovannoni S.J.,
RA   Rappe M.S., Brinkac L., Kim M., Beeson K., Ferriera S., Sutton G.,
RA   Friedman R., Venter J.C.;
RL   Submitted (SEP-2012) 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         ECO:0000256|PIRNR:PIRNR004491};
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         ECO:0000256|PIRNR:PIRNR004491};
CC   -!- PATHWAY: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step
CC       1/1. {ECO:0000256|ARBA:ARBA00004726, ECO:0000256|PIRNR:PIRNR004491}.
CC   -!- PATHWAY: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin
CC       (ATP route): step 1/1. {ECO:0000256|ARBA:ARBA00005201,
CC       ECO:0000256|PIRNR:PIRNR004491}.
CC   -!- SIMILARITY: Belongs to the ribF family.
CC       {ECO:0000256|PIRNR:PIRNR004491}.
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:EMH79717.1}.
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DR   EMBL; ADAC02000001; EMH79717.1; -; Genomic_DNA.
DR   AlphaFoldDB; D0RRI4; -.
DR   STRING; 684719.HIMB114_00000850; -.
DR   eggNOG; COG0196; Bacteria.
DR   OrthoDB; 9803667at2; -.
DR   UniPathway; UPA00276; UER00406.
DR   UniPathway; UPA00277; UER00407.
DR   Proteomes; UP000033990; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003919; F:FMN adenylyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008531; F:riboflavin kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006747; P:FAD biosynthetic process; IEA:UniProtKB-UniRule.
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; 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; IPR004821; Cyt_trans-like.
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; TIGR00125; cyt_tran_rel; 1.
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   PIRSF; PIRSF004491; FAD_Synth; 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, ECO:0000256|PIRNR:PIRNR004491};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRNR:PIRNR004491};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|PIRNR:PIRNR004491};
KW   FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|PIRNR:PIRNR004491};
KW   Kinase {ECO:0000256|PIRNR:PIRNR004491, ECO:0000313|EMBL:EMH79717.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR004491};
KW   Nucleotidyltransferase {ECO:0000256|PIRNR:PIRNR004491,
KW   ECO:0000313|EMBL:EMH79717.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033990};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR004491}.
FT   DOMAIN          176..300
FT                   /note="Riboflavin kinase"
FT                   /evidence="ECO:0000259|SMART:SM00904"
SQ   SEQUENCE   302 AA;  34903 MW;  121742F77303B8F3 CRC64;
     MKILRNKFNL QYTKNSILVI GNFDGLHKGH ISILNEAKKL SKKNNLKFGL LTFDPNPKEF
     FLKDKYFKIM SNTEKEKLLS KNKLDFLIIL KFNNSLRNKS ADTFIKKILK SKISPSKIIV
     GKEFKFGKNR TGSPSLLKNY FNTKIANQKK ISGVKISSSQ IRKLIQAGKI SKANRLLGRN
     WSVIGNVNSG NKIGRKLGYK TANLFINNCI QPYRGVYATR LYFKNRLYNG ISNFGIAPTL
     KLKKREVLET HLFSPVKNLY KKKVKIEFFK FIRKEKKFKT KKNLTDQIKK DITIAKKILN
     NV
//

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