MQMTN_HELPY
ID MQMTN_HELPY Reviewed; 231 AA.
AC O24915; O32636;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Aminodeoxyfutalosine nucleosidase;
DE Short=AFL nucleosidase;
DE Short=Aminofutalosine nucleosidase;
DE EC=3.2.2.30 {ECO:0000269|PubMed:21098241, ECO:0000269|PubMed:24083939};
DE AltName: Full=5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase;
DE Short=MTA/SAH nucleosidase;
DE Short=MTAN;
DE EC=3.2.2.9 {ECO:0000269|PubMed:21098241, ECO:0000269|PubMed:24083939};
DE AltName: Full=6-amino-6-deoxyfutalosine N-ribosylhydrolase;
GN Name=mtnN; Synonyms=mtn; OrderedLocusNames=HP_0089;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 4867 / CCUG 17874 / NCTC 11638;
RA Beier D., Scarlato V.;
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION AS AFL NUCLEOSIDASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY,
RP AND MENAQUINONE BIOSYNTHESIS PATHWAY.
RC STRAIN=ATCC 700392 / 26695;
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).
RN [4]
RP FUNCTION AS AFL NUCLEOSIDASE, CATALYTIC ACTIVITY, AND MENAQUINONE
RP BIOSYNTHESIS PATHWAY.
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=24083939; DOI=10.1021/ja408594p;
RA Mahanta N., Fedoseyenko D., Dairi T., Begley T.P.;
RT "Menaquinone biosynthesis: formation of aminofutalosine requires a unique
RT radical SAM enzyme.";
RL J. Am. Chem. Soc. 135:15318-15321(2013).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF WILD-TYPE AND MUTANTS GLN-14;
RP ALA-199 AND ASN-199 IN COMPLEX WITH 5'-METHYLTHIOADENOSINE.
RA Kim R.Q., Offen W.A., Stubbs K.A., Davies G.J.;
RT "Structural enzymology of H. pylori futalosine hydrolase.";
RL Submitted (SEP-2013) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the direct conversion of aminodeoxyfutalosine (AFL)
CC into dehypoxanthine futalosine (DHFL) and adenine via the hydrolysis of
CC the N-glycosidic bond; this reaction seems to represent an essential
CC step in the menaquinone biosynthesis pathway in Helicobacter species.
CC Can also probably catalyzes the hydrolysis of 5'-methylthioadenosine
CC (MTA) and S-adenosylhomocysteine (SAH) to adenine and the corresponding
CC thioribose, 5'-methylthioribose and S-ribosylhomocysteine,
CC respectively. These other activities highlight the tremendous
CC versatility of the enzyme, which also plays key roles in S-
CC adenosylmethionine recycling and in the biosynthesis of the quorum-
CC sensing molecule autoinducer-2. Does not act on futalosine (FL) as
CC substrate. {ECO:0000269|PubMed:21098241, ECO:0000269|PubMed:24083939}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-amino-6-deoxyfutalosine + H2O = adenine + dehypoxanthine
CC futalosine; Xref=Rhea:RHEA:33079, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16708, ChEBI:CHEBI:58864, ChEBI:CHEBI:64286; EC=3.2.2.30;
CC Evidence={ECO:0000269|PubMed:21098241, ECO:0000269|PubMed:24083939};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + S-adenosyl-L-homocysteine = adenine + S-(5-deoxy-D-
CC ribos-5-yl)-L-homocysteine; Xref=Rhea:RHEA:17805, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16708, ChEBI:CHEBI:57856, ChEBI:CHEBI:58195; EC=3.2.2.9;
CC Evidence={ECO:0000269|PubMed:21098241, ECO:0000269|PubMed:24083939};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + S-methyl-5'-thioadenosine = 5-(methylsulfanyl)-D-ribose
CC + adenine; Xref=Rhea:RHEA:13617, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16708, ChEBI:CHEBI:17509, ChEBI:CHEBI:78440; EC=3.2.2.9;
CC Evidence={ECO:0000269|PubMed:21098241, ECO:0000269|PubMed:24083939};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5'-deoxyadenosine + H2O = 5-deoxy-D-ribose + adenine;
CC Xref=Rhea:RHEA:29859, ChEBI:CHEBI:15377, ChEBI:CHEBI:16708,
CC ChEBI:CHEBI:17319, ChEBI:CHEBI:149540; EC=3.2.2.9;
CC Evidence={ECO:0000269|PubMed:21098241, ECO:0000269|PubMed:24083939};
CC -!- PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis.
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via salvage
CC pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-
CC thioadenosine (hydrolase route): step 1/2.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PNP/UDP phosphorylase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC64855.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE000511; AAD07157.1; -; Genomic_DNA.
DR EMBL; AF009177; AAC64855.1; ALT_INIT; Genomic_DNA.
DR PIR; A64531; A64531.
DR RefSeq; NP_206889.1; NC_000915.1.
DR RefSeq; WP_000250146.1; NC_018939.1.
DR PDB; 4BMX; X-ray; 1.76 A; A/B=1-231.
DR PDB; 4BMY; X-ray; 1.65 A; A/B=1-231.
DR PDB; 4BMZ; X-ray; 1.79 A; A/B=1-231.
DR PDB; 4BN0; X-ray; 2.11 A; A/B/C/D=1-231.
DR PDBsum; 4BMX; -.
DR PDBsum; 4BMY; -.
DR PDBsum; 4BMZ; -.
DR PDBsum; 4BN0; -.
DR AlphaFoldDB; O24915; -.
DR SMR; O24915; -.
DR IntAct; O24915; 2.
DR STRING; 85962.C694_00435; -.
DR PaxDb; O24915; -.
DR EnsemblBacteria; AAD07157; AAD07157; HP_0089.
DR KEGG; hpy:HP_0089; -.
DR PATRIC; fig|85962.47.peg.95; -.
DR eggNOG; COG0775; Bacteria.
DR OMA; DQFVHSK; -.
DR PhylomeDB; O24915; -.
DR BioCyc; MetaCyc:HP0089-MON; -.
DR BRENDA; 3.2.2.16; 2604.
DR BRENDA; 3.2.2.30; 2604.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA00904; UER00871.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0102246; F:6-amino-6-deoxyfutalosine hydrolase activity; IEA:UniProtKB-EC.
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:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniPathway.
DR GO; GO:0019284; P:L-methionine salvage from S-adenosylmethionine; IBA:GO_Central.
DR GO; GO:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009164; P:nucleoside catabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.1580; -; 1.
DR InterPro; IPR010049; MTA_SAH_Nsdase.
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; TIGR01704; MTA/SAH-Nsdase; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Hydrolase; Menaquinone biosynthesis;
KW Methionine biosynthesis; Reference proteome.
FT CHAIN 1..231
FT /note="Aminodeoxyfutalosine nucleosidase"
FT /id="PRO_0000164443"
FT ACT_SITE 14
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 199
FT /note="Proton donor"
FT /evidence="ECO:0000305"
FT BINDING 81
FT /ligand="substrate"
FT BINDING 155
FT /ligand="substrate"
FT BINDING 175..176
FT /ligand="substrate"
FT CONFLICT 25
FT /note="D -> G (in Ref. 2; AAC64855)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="D -> N (in Ref. 2; AAC64855)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="E -> K (in Ref. 2; AAC64855)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="V -> A (in Ref. 2; AAC64855)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="V -> L (in Ref. 2; AAC64855)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="E -> R (in Ref. 2; AAC64855)"
FT /evidence="ECO:0000305"
FT STRAND 3..11
FT /evidence="ECO:0007829|PDB:4BMY"
FT HELIX 12..22
FT /evidence="ECO:0007829|PDB:4BMY"
FT STRAND 27..31
FT /evidence="ECO:0007829|PDB:4BMY"
FT STRAND 34..41
FT /evidence="ECO:0007829|PDB:4BMY"
FT STRAND 44..50
FT /evidence="ECO:0007829|PDB:4BMY"
FT HELIX 55..69
FT /evidence="ECO:0007829|PDB:4BMY"
FT STRAND 72..82
FT /evidence="ECO:0007829|PDB:4BMY"
FT STRAND 92..100
FT /evidence="ECO:0007829|PDB:4BMY"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:4BMY"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:4BMY"
FT HELIX 126..139
FT /evidence="ECO:0007829|PDB:4BMY"
FT STRAND 143..150
FT /evidence="ECO:0007829|PDB:4BMY"
FT HELIX 158..168
FT /evidence="ECO:0007829|PDB:4BMY"
FT STRAND 171..176
FT /evidence="ECO:0007829|PDB:4BMY"
FT HELIX 177..187
FT /evidence="ECO:0007829|PDB:4BMY"
FT STRAND 191..199
FT /evidence="ECO:0007829|PDB:4BMY"
FT HELIX 211..228
FT /evidence="ECO:0007829|PDB:4BMY"
SQ SEQUENCE 231 AA; 25209 MW; 8704A43F0189CD08 CRC64;
MVQKIGILGA MREEITPILE LFGVDFEEIP LGGNVFHKGV YHNKEIIVAY SKIGKVHSTL
TTTSMILAFG VQKVLFSGVA GSLVKDLKIN DLLVAIQLVQ HDVDLSAFDH PLGFIPESAI
FIETSESLNA LAKEVANEQH IVLKEGVIAS GDQFVHSKER KEFLVSEFKA SAVEMEGASV
AFVCQKFGVP CCVLRSISDN ADEEANMSFD AFLEKSAQTS AKFLKSMVDE L
