ID A0A0A7I2C0_9BIFI Unreviewed; 408 AA.
AC A0A0A7I2C0;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=FAD synthase {ECO:0000313|EMBL:AIZ14006.1};
GN ORFNames=AH68_01970 {ECO:0000313|EMBL:AIZ14006.1};
OS Bifidobacterium catenulatum PV20-2.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1447716 {ECO:0000313|EMBL:AIZ14006.1, ECO:0000313|Proteomes:UP000030625};
RN [1] {ECO:0000313|EMBL:AIZ14006.1, ECO:0000313|Proteomes:UP000030625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PV20-2 {ECO:0000313|EMBL:AIZ14006.1,
RC ECO:0000313|Proteomes:UP000030625};
RX PubMed=25614572;
RA Vazquez-Gutierrez P., Lacroix C., Chassard C., Klumpp J., Jans C.,
RA Stevens M.J.;
RT "Complete and Assembled Genome Sequence of Bifidobacterium kashiwanohense
RT PV20-2, Isolated from the Feces of an Anemic Kenyan Infant.";
RL Genome Announc. 3:0-0(2015).
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 -!- SIMILARITY: Belongs to the RibF family.
CC {ECO:0000256|ARBA:ARBA00010214}.
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DR EMBL; CP007456; AIZ14006.1; -; Genomic_DNA.
DR RefSeq; WP_039199682.1; NZ_CP007456.1.
DR AlphaFoldDB; A0A0A7I2C0; -.
DR STRING; 1447716.AH68_01970; -.
DR KEGG; bka:AH68_01970; -.
DR HOGENOM; CLU_048437_0_0_11; -.
DR OrthoDB; 9803667at2; -.
DR UniPathway; UPA00277; UER00407.
DR Proteomes; UP000030625; Chromosome.
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: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; IPR015865; Riboflavin_kinase_bac/euk.
DR InterPro; IPR023465; Riboflavin_kinase_dom_sf.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 245..408
FT /note="Riboflavin kinase"
FT /evidence="ECO:0000259|SMART:SM00904"
FT REGION 178..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 408 AA; 44419 MW; F4D0FE56E46292B4 CRC64;
MKTITLTPDA SGMVDWPTLS NDKKSVVTIG SFDGMHQGHQ AVIRRVVELA KKEQSFSVVV
LFDPRPALVH GYAAKNGGQE PPTGMVDTQA LTSMQERLRA INKLGVDYTL IVHYTLAFAA
KSYRFFLGQM VGKLGMRTLA LGSDAAMGAN RAGDVKAIEN LALATGVFQL EVVDDRGPGE
TRVPANAQPV MPTGHGEPTD PLEGASKAER RAWSKKNQAK PVRVWSSTNV RYLLGQGRIK
DADAILGHPH AVEGIVVHGE ERGRTIGFPT ANLNDNVAGY LPVDGVYAGW LVDLGAKTAE
DDHAEAAADG ISQQFDSSSV DARLADHSPY RWPAAISIGT KPTFNETTGM NERVVEAYAI
TDDWLDLYNH QVRVEFTGFL RPQIKFDSAQ DLIDELKRNV EETKRITA
//
