MQNB_THET8
ID MQNB_THET8 Reviewed; 225 AA.
AC Q5SKT7;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=TTHA0556;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
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 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND SUBUNIT.
RX PubMed=19420717; DOI=10.1271/bbb.80906;
RA Hiratsuka T., Itoh N., Seto H., Dairi T.;
RT "Enzymatic properties of futalosine hydrolase, an enzyme essential to a
RT newly identified menaquinone biosynthetic pathway.";
RL Biosci. Biotechnol. Biochem. 73:1137-1141(2009).
RN [4]
RP SUBSTRATE SPECIFICITY.
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). Is highly specific to futalosine since it
CC does not accept aminodeoxyfutalosine (AFL), or any structurally related
CC nucleotides and nucleosides as substrate. {ECO:0000255|HAMAP-
CC Rule:MF_00991, ECO:0000269|PubMed:18801996,
CC ECO:0000269|PubMed:19420717}.
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:18801996, ECO:0000269|PubMed:19420717};
CC -!- ACTIVITY REGULATION: No enhancing of inhibitory effects are observed
CC with divalent metal ions. Slightly inhibited by hypoxanthine.
CC {ECO:0000269|PubMed:19420717}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=154 uM for futalosine {ECO:0000269|PubMed:19420717};
CC Note=kcat is 1.02 sec(-1).;
CC pH dependence:
CC Optimum pH is 4.5. {ECO:0000269|PubMed:19420717};
CC Temperature dependence:
CC Optimum temperature is 80 degrees Celsius.
CC {ECO:0000269|PubMed:19420717};
CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00991, ECO:0000269|PubMed:19420717}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:19420717}.
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; AB447892; BAG71678.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD70379.1; -; Genomic_DNA.
DR RefSeq; WP_011228023.1; NC_006461.1.
DR RefSeq; YP_143822.1; NC_006461.1.
DR AlphaFoldDB; Q5SKT7; -.
DR SMR; Q5SKT7; -.
DR STRING; 300852.55771938; -.
DR PRIDE; Q5SKT7; -.
DR EnsemblBacteria; BAD70379; BAD70379; BAD70379.
DR GeneID; 3169130; -.
DR KEGG; ttj:TTHA0556; -.
DR PATRIC; fig|300852.9.peg.555; -.
DR eggNOG; COG0775; Bacteria.
DR HOGENOM; CLU_031248_3_0_0; -.
DR OMA; MEGYGVA; -.
DR BioCyc; MetaCyc:MON-14264; -.
DR BRENDA; 3.2.2.26; 2305.
DR UniPathway; UPA00079; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0016799; F:hydrolase activity, hydrolyzing N-glycosyl compounds; IDA:UniProtKB.
DR GO; GO:0009234; P:menaquinone biosynthetic process; IDA:UniProtKB.
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..225
FT /note="Futalosine hydrolase"
FT /id="PRO_0000418619"
SQ SEQUENCE 225 AA; 23829 MW; D98579BE2FDCFC83 CRC64;
MWLLLSPTRL EAPFLEGEPF AFLAWRGLKG TGFVYLETGI GKVNAAMALA AYAARNPVEK
ALLFGLAGAY PGGPSLGEAV LVEEEVEADL GLKEGLAPLG FPALALGERR YFNRFPLDPG
LTGELARGLG LKVAVGLTRD LVSETPEEAL ALARRWGASL ENMEGAAFAR ACLALGVRGA
ELRALSNPAG VRDKAHWRTK EALSALARAV RRLLAEEGGA RRPPG
