MQNB_STRCO
ID MQNB_STRCO Reviewed; 235 AA.
AC Q9KXN0; B5MG04;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 22-JAN-2014, sequence version 2.
DT 25-MAY-2022, entry version 87.
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=SCO4327;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ROLE IN MENAQUINONE BIOSYNTHESIS,
RP PATHWAY, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=18801996; DOI=10.1126/science.1160446;
RA Hiratsuka T., Furihata K., Ishikawa J., Yamashita H., Itoh N., Seto H.,
RA Dairi T.;
RT "An alternative menaquinone biosynthetic pathway operating in
RT microorganisms.";
RL Science 321:1670-1673(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
RN [3]
RP IDENTIFICATION OF START SITE, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, AND PATHWAY.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
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). Does not accept aminodeoxyfutalosine
CC (AFL) as a substrate. {ECO:0000255|HAMAP-Rule:MF_00991,
CC ECO:0000269|PubMed:18801996, 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:18801996,
CC ECO:0000269|PubMed:21098241}.
CC -!- DISRUPTION PHENOTYPE: Mutants require menaquinone for their growth.
CC {ECO:0000269|PubMed:18801996}.
CC -!- SIMILARITY: Belongs to the PNP/UDP phosphorylase family. Futalosine
CC hydrolase subfamily. {ECO:0000255|HAMAP-Rule:MF_00991}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAG71675.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB93401.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB447889; BAG71675.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL939119; CAB93401.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_628498.1; NC_003888.3.
DR RefSeq; WP_011029581.1; NC_003888.3.
DR RefSeq; WP_016326870.1; NZ_CP042324.1.
DR AlphaFoldDB; Q9KXN0; -.
DR SMR; Q9KXN0; -.
DR STRING; 100226.SCO4327; -.
DR GeneID; 1099767; -.
DR KEGG; sco:SCO4327; -.
DR PATRIC; fig|100226.15.peg.4396; -.
DR eggNOG; COG0775; Bacteria.
DR HOGENOM; CLU_031248_3_0_11; -.
DR InParanoid; Q9KXN0; -.
DR BRENDA; 3.2.2.26; 5998.
DR UniPathway; UPA00079; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008782; F:adenosylhomocysteine nucleosidase activity; IBA:GO_Central.
DR GO; GO:0008930; F:methylthioadenosine nucleosidase activity; IBA:GO_Central.
DR GO; GO:0019284; P:L-methionine salvage from S-adenosylmethionine; IBA:GO_Central.
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..235
FT /note="Futalosine hydrolase"
FT /id="PRO_0000418618"
SQ SEQUENCE 235 AA; 23448 MW; 750CF9146BB6C64C CRC64;
MHLLVATAVS VERDAVARAF PAPGTEVSRP GITLHRLPDG WDLLAAGVGP ARAAASTAAA
LTAAALDGRP YDLVVSAGIG GGFAPEAPVG SLVVADAITA ADLGAETADG FLPVTDLGFG
TVTHLPPAPL VRAAAEATGA RPGTVLTGST VTGTAARAAL LRERHPGALA EAMEGFGVAE
AAAAHGVPVL ELRAVSNPVG PRDRAAWRIG EALAALTDAV GKLAPVLESW KPHER
