ID A0A0F5VZA0_9ACTN Unreviewed; 220 AA.
AC A0A0F5VZA0;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Futalosine hydrolase {ECO:0000256|HAMAP-Rule:MF_00991};
DE Short=FL hydrolase {ECO:0000256|HAMAP-Rule:MF_00991};
DE EC=3.2.2.26 {ECO:0000256|HAMAP-Rule:MF_00991};
DE AltName: Full=Futalosine nucleosidase {ECO:0000256|HAMAP-Rule:MF_00991};
DE AltName: Full=Menaquinone biosynthetic enzyme MqnB {ECO:0000256|HAMAP-Rule:MF_00991};
GN Name=mqnB {ECO:0000256|HAMAP-Rule:MF_00991};
GN ORFNames=TN53_15760 {ECO:0000313|EMBL:KKD07097.1};
OS Streptomyces sp. WM6386.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1415558 {ECO:0000313|EMBL:KKD07097.1, ECO:0000313|Proteomes:UP000033641};
RN [1] {ECO:0000313|EMBL:KKD07097.1, ECO:0000313|Proteomes:UP000033641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WM6386 {ECO:0000313|EMBL:KKD07097.1,
RC ECO:0000313|Proteomes:UP000033641};
RA Ju K.-S., Doroghazi J.R., Metcalf W.;
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the hydrolysis of futalosine (FL) to dehypoxanthine
CC futalosine (DHFL) and hypoxanthine, a step in the biosynthesis of
CC menaquinone (MK, vitamin K2). {ECO:0000256|HAMAP-Rule:MF_00991}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=futalosine + H2O = dehypoxanthine futalosine + hypoxanthine;
CC Xref=Rhea:RHEA:25904, ChEBI:CHEBI:15377, ChEBI:CHEBI:17368,
CC ChEBI:CHEBI:58863, ChEBI:CHEBI:58864; EC=3.2.2.26;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00991};
CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_00991}.
CC -!- SIMILARITY: Belongs to the PNP/UDP phosphorylase family. Futalosine
CC hydrolase subfamily. {ECO:0000256|HAMAP-Rule:MF_00991}.
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:KKD07097.1}.
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DR EMBL; JXTE01000021; KKD07097.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F5VZA0; -.
DR PATRIC; fig|1415558.3.peg.2764; -.
DR UniPathway; UPA00079; -.
DR Proteomes; UP000033641; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016799; F:hydrolase activity, hydrolyzing N-glycosyl compounds; IEA:UniProtKB-UniRule.
DR GO; GO:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
DR CDD; cd17766; futalosine_nucleosidase_MqnB; 1.
DR Gene3D; 3.40.50.1580; Nucleoside phosphorylase domain; 1.
DR HAMAP; MF_00991; MqnB; 1.
DR InterPro; IPR019963; FL_hydrolase_MqnB.
DR InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR NCBIfam; TIGR03664; fut_nucase; 1.
DR PANTHER; PTHR46832; 5'-METHYLTHIOADENOSINE/S-ADENOSYLHOMOCYSTEINE NUCLEOSIDASE; 1.
DR PANTHER; PTHR46832:SF2; FUTALOSINE HYDROLASE; 1.
DR Pfam; PF01048; PNP_UDP_1; 1.
DR SUPFAM; SSF53167; Purine and uridine phosphorylases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00991};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Menaquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_00991};
KW Reference proteome {ECO:0000313|Proteomes:UP000033641};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 28..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 21..188
FT /note="Nucleoside phosphorylase"
FT /evidence="ECO:0000259|Pfam:PF01048"
SQ SEQUENCE 220 AA; 22199 MW; 041A6F835D1503EC CRC64;
MARAFPGAAR EVPLPGVTLL RSGGGYDLLA AGVGPALAAA FVSAVLTAAA REGTPYRLVV
SAGIAGGFLP EAPVGSLVLA DAITAADLGA ETADGFLPVT ELGFGTVSHV PPPSLVREAA
TATGARRGTI LTVSTVTGTA ARAAALRERH PTALAEAMEG FGVAEAAALH GVPVLEMRAV
SNPVGPRDRA AWRIPDALAT LTDGFGKLAP VLESWNRHDR
//
