GenomeNet

Database: UniProt
Entry: D3PQL8_MEIRD
LinkDB: D3PQL8_MEIRD
Original site: D3PQL8_MEIRD 
ID   D3PQL8_MEIRD            Unreviewed;       222 AA.
AC   D3PQL8;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   27-MAR-2024, entry version 74.
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   OrderedLocusNames=Mrub_0986 {ECO:0000313|EMBL:ADD27751.1};
GN   ORFNames=K649_04570 {ECO:0000313|EMBL:AGK04216.1};
OS   Meiothermus ruber (strain ATCC 35948 / DSM 1279 / VKM B-1258 / 21) (Thermus
OS   ruber).
OC   Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Meiothermus.
OX   NCBI_TaxID=504728 {ECO:0000313|EMBL:AGK04216.1, ECO:0000313|Proteomes:UP000013026};
RN   [1] {ECO:0000313|EMBL:ADD27751.1, ECO:0000313|Proteomes:UP000006655}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35948 / DSM 1279 / VKM B-1258 / 21
RC   {ECO:0000313|Proteomes:UP000006655}, and DSM 1279
RC   {ECO:0000313|EMBL:ADD27751.1};
RX   PubMed=21304689; DOI=10.4056/sigs.1032748;
RA   Tindall B.J., Sikorski J., Lucas S., Goltsman E., Copeland A.,
RA   Glavina Del Rio T., Nolan M., Tice H., Cheng J.F., Han C., Pitluck S.,
RA   Liolios K., Ivanova N., Mavromatis K., Ovchinnikova G., Pati A.,
RA   Fahnrich R., Goodwin L., Chen A., Palaniappan K., Land M., Hauser L.,
RA   Chang Y.J., Jeffries C.D., Rohde M., Goker M., Woyke T., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA   Lapidus A.;
RT   "Complete genome sequence of Meiothermus ruber type strain (21).";
RL   Stand. Genomic Sci. 3:26-36(2010).
RN   [2] {ECO:0000313|EMBL:AGK04216.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 1279 {ECO:0000313|EMBL:AGK04216.1};
RA   Klammer A., Drake J., Heiner C., Clum A., Copeland A., Huddleston J.,
RA   Eichler E., Turner S.W.;
RT   "Non-Hybrid, Finished Microbial Genome Assemblies from Long-Read SMRT
RT   Sequencing Data.";
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:AGK04216.1, ECO:0000313|Proteomes:UP000013026}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35948 / DSM 1279 / VKM B-1258 / 21
RC   {ECO:0000313|Proteomes:UP000013026}, and DSM 1279
RC   {ECO:0000313|EMBL:AGK04216.1};
RA   Chin J., Alexander D.H., Marks P., Korlach J., Clum A., Copeland A.;
RL   Submitted (APR-2013) 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001743; ADD27751.1; -; Genomic_DNA.
DR   EMBL; CP005385; AGK04216.1; -; Genomic_DNA.
DR   RefSeq; WP_013013270.1; NC_021081.1.
DR   AlphaFoldDB; D3PQL8; -.
DR   STRING; 504728.K649_04570; -.
DR   KEGG; mrb:Mrub_0986; -.
DR   KEGG; mre:K649_04570; -.
DR   PATRIC; fig|504728.9.peg.944; -.
DR   eggNOG; COG0775; Bacteria.
DR   OrthoDB; 9788270at2; -.
DR   UniPathway; UPA00079; -.
DR   Proteomes; UP000006655; Chromosome.
DR   Proteomes; UP000013026; 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   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   Menaquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_00991}.
FT   DOMAIN          36..220
FT                   /note="Nucleoside phosphorylase"
FT                   /evidence="ECO:0000259|Pfam:PF01048"
SQ   SEQUENCE   222 AA;  24357 MW;  B4F36316561F7C0E CRC64;
     MPTLPLLLLS PTRLEAPFLK GQKFDFHGRA GLRGAGWVWL ECGIGKVNTA ATLAAFVQRR
     RFERVLLFGI AGAYADSGLQ LGDCALAERE IQADLGVRDG GLKGLGFPSL VVASRPYHNR
     FPLDKAFTDE LKSKLGLPGK QFLTRDLVSE NPTEAHQLAR KWEADLENME GAAFAQTCLW
     LGLAGAELRA VSNMAGVRDK AQWRIRQAVE ALEHHILRII GS
//
DBGET integrated database retrieval system