ID   MQNB_ACIC1              Reviewed;         244 AA.
AC   A0LR22;
DT   22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Futalosine hydrolase {ECO:0000255|HAMAP-Rule:MF_00991};
DE            Short=FL hydrolase {ECO:0000255|HAMAP-Rule:MF_00991};
DE            EC=3.2.2.26 {ECO:0000255|HAMAP-Rule:MF_00991};
DE   AltName: Full=Futalosine nucleosidase {ECO:0000255|HAMAP-Rule:MF_00991};
DE   AltName: Full=Menaquinone biosynthetic enzyme MqnB {ECO:0000255|HAMAP-Rule:MF_00991};
GN   Name=mqnB {ECO:0000255|HAMAP-Rule:MF_00991}; OrderedLocusNames=Acel_0106;
OS   Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B).
OC   Bacteria; Actinobacteria; Acidothermales; Acidothermaceae; Acidothermus.
OX   NCBI_TaxID=351607;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43068 / DSM 8971 / 11B;
RX   PubMed=19270083; DOI=10.1101/gr.084848.108;
RA   Barabote R.D., Xie G., Leu D.H., Normand P., Necsulea A., Daubin V.,
RA   Medigue C., Adney W.S., Xu X.C., Lapidus A., Parales R.E., Detter C.,
RA   Pujic P., Bruce D., Lavire C., Challacombe J.F., Brettin T.S., Berry A.M.;
RT   "Complete genome of the cellulolytic thermophile Acidothermus
RT   cellulolyticus 11B provides insights into its ecophysiological and
RT   evolutionary adaptations.";
RL   Genome Res. 19:1033-1043(2009).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND PATHWAY.
RX   PubMed=21098241; DOI=10.1128/aac.01362-10;
RA   Arakawa C., Kuratsu M., Furihata K., Hiratsuka T., Itoh N., Seto H.,
RA   Dairi T.;
RT   "Diversity of the early step of the futalosine pathway.";
RL   Antimicrob. Agents Chemother. 55:913-916(2011).
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). Cannot directly use aminodeoxyfutalosine
CC       (AFL) as a substrate. {ECO:0000255|HAMAP-Rule:MF_00991,
CC       ECO:0000269|PubMed:21098241}.
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:0000255|HAMAP-Rule:MF_00991,
CC         ECO:0000269|PubMed:21098241};
CC   -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00991, ECO:0000269|PubMed:21098241}.
CC   -!- SIMILARITY: Belongs to the PNP/UDP phosphorylase family. Futalosine
CC       hydrolase subfamily. {ECO:0000255|HAMAP-Rule:MF_00991}.
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DR   EMBL; CP000481; ABK51882.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0LR22; -.
DR   SMR; A0LR22; -.
DR   STRING; 351607.Acel_0106; -.
DR   EnsemblBacteria; ABK51882; ABK51882; Acel_0106.
DR   KEGG; ace:Acel_0106; -.
DR   eggNOG; COG0775; Bacteria.
DR   HOGENOM; CLU_031248_3_0_11; -.
DR   OMA; MEGYGVA; -.
DR   UniPathway; UPA00079; -.
DR   Proteomes; UP000008221; Chromosome.
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   Gene3D; 3.40.50.1580; -; 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   Pfam; PF01048; PNP_UDP_1; 1.
DR   SUPFAM; SSF53167; SSF53167; 1.
DR   TIGRFAMs; TIGR03664; fut_nucase; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Menaquinone biosynthesis; Reference proteome.
FT   CHAIN           1..244
FT                   /note="Futalosine hydrolase"
FT                   /id="PRO_0000425137"
SQ   SEQUENCE   244 AA;  24588 MW;  E3DFAABA74CDB3EA CRC64;
     MSVKRLIITA VAAEADAVAS GLDGAQPHPQ GSANVRHTAT ADILVAGVGS AAAAAATAAA
     LARRHYSLVI CTGIAGGIGI AGIGDIVVAD AVHPADLGAM SPDGFIPLEH LGIATTANAI
     DPPVVEELTG PLRYAGLAPV IGGILTVNTV TGTDAHADDL RRRYPGAVAE AMEGYGVAVA
     ATRAGVRYGE LRVVSNRVGR RDRRAWDIPG ALRRLEHAFA ALGAAWCNDG SGQAAAREID
     GGCP