MQMTN_CAMJE
ID MQMTN_CAMJE Reviewed; 229 AA.
AC Q0PC20;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Aminodeoxyfutalosine nucleosidase;
DE Short=AFL nucleosidase;
DE Short=Aminofutalosine nucleosidase;
DE EC=3.2.2.30 {ECO:0000269|PubMed:21489995};
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:21489995};
DE AltName: Full=6-amino-6-deoxyfutalosine N-ribosylhydrolase;
GN Name=pfs; OrderedLocusNames=Cj0117;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
RN [2]
RP FUNCTION AS AFL AND MTA NUCLEOSIDASE, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, AND MENAQUINONE BIOSYNTHESIS PATHWAY.
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=21489995; DOI=10.1074/jbc.m111.229781;
RA Li X., Apel D., Gaynor E.C., Tanner M.E.;
RT "5'-methylthioadenosine nucleosidase is implicated in playing a key role in
RT a modified futalosine pathway for menaquinone biosynthesis in Campylobacter
RT jejuni.";
RL J. Biol. Chem. 286:19392-19398(2011).
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 Campylobacter species.
CC Also catalyzes the hydrolysis of 5'-methylthioadenosine (MTA) to
CC adenine and 5'-methylthioribose. Can also probably use S-
CC adenosylhomocysteine (SAH) as substrate, leading to adenine and S-
CC ribosylhomocysteine. 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. Shows negligible activity with
CC futalosine (FL) as substrate. {ECO:0000269|PubMed:21489995}.
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:21489995};
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:21489995};
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:21489995};
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:21489995};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.03 uM for aminodeoxyfutalosine;
CC KM=0.93 uM for 5'-methylthioadenosine;
CC Note=kcat is 0.53 sec(-1) with aminodeoxyfutalosine as substrate.
CC kcat is 2.7 sec(-1) with 5'-methylthioadenosine as substrate.;
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 ---------------------------------------------------------------------------
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; AL111168; CAL34288.1; -; Genomic_DNA.
DR PIR; E81428; E81428.
DR RefSeq; WP_002859787.1; NC_002163.1.
DR RefSeq; YP_002343577.1; NC_002163.1.
DR PDB; 6AYM; X-ray; 1.25 A; A/B=2-229.
DR PDB; 6AYO; X-ray; 1.67 A; A/B=2-229.
DR PDB; 6AYQ; X-ray; 1.42 A; A/B=2-229.
DR PDB; 6AYR; X-ray; 1.95 A; A/B/C/D=2-229.
DR PDB; 6AYS; X-ray; 1.70 A; A/B/C/D/E/F/G/H=2-229.
DR PDB; 6AYT; X-ray; 1.85 A; A/B/C/D=2-229.
DR PDBsum; 6AYM; -.
DR PDBsum; 6AYO; -.
DR PDBsum; 6AYQ; -.
DR PDBsum; 6AYR; -.
DR PDBsum; 6AYS; -.
DR PDBsum; 6AYT; -.
DR AlphaFoldDB; Q0PC20; -.
DR SMR; Q0PC20; -.
DR IntAct; Q0PC20; 26.
DR STRING; 192222.Cj0117; -.
DR PaxDb; Q0PC20; -.
DR PRIDE; Q0PC20; -.
DR EnsemblBacteria; CAL34288; CAL34288; Cj0117.
DR GeneID; 904448; -.
DR KEGG; cje:Cj0117; -.
DR PATRIC; fig|192222.6.peg.115; -.
DR eggNOG; COG0775; Bacteria.
DR HOGENOM; CLU_031248_2_0_7; -.
DR OMA; DQFVHSK; -.
DR BioCyc; MetaCyc:MON-16549; -.
DR BRENDA; 3.2.2.26; 13746.
DR BRENDA; 3.2.2.30; 1087.
DR BRENDA; 3.2.2.9; 1087.
DR UniPathway; UPA00079; -.
DR UniPathway; UPA00904; UER00871.
DR Proteomes; UP000000799; Chromosome.
DR GO; GO:0102246; F:6-amino-6-deoxyfutalosine hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0008782; F:adenosylhomocysteine nucleosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0008930; F:methylthioadenosine nucleosidase activity; IEA:InterPro.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniPathway.
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..229
FT /note="Aminodeoxyfutalosine nucleosidase"
FT /id="PRO_0000425136"
FT ACT_SITE 13
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 197
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 173..174
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:6AYM"
FT HELIX 11..21
FT /evidence="ECO:0007829|PDB:6AYM"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:6AYM"
FT STRAND 32..39
FT /evidence="ECO:0007829|PDB:6AYM"
FT STRAND 42..48
FT /evidence="ECO:0007829|PDB:6AYM"
FT HELIX 53..65
FT /evidence="ECO:0007829|PDB:6AYM"
FT STRAND 70..80
FT /evidence="ECO:0007829|PDB:6AYM"
FT STRAND 90..98
FT /evidence="ECO:0007829|PDB:6AYM"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:6AYM"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:6AYQ"
FT HELIX 124..137
FT /evidence="ECO:0007829|PDB:6AYM"
FT STRAND 141..148
FT /evidence="ECO:0007829|PDB:6AYM"
FT HELIX 156..166
FT /evidence="ECO:0007829|PDB:6AYM"
FT STRAND 169..174
FT /evidence="ECO:0007829|PDB:6AYM"
FT HELIX 175..184
FT /evidence="ECO:0007829|PDB:6AYM"
FT STRAND 189..197
FT /evidence="ECO:0007829|PDB:6AYM"
FT HELIX 207..228
FT /evidence="ECO:0007829|PDB:6AYM"
SQ SEQUENCE 229 AA; 25225 MW; C22D548C70CBBB37 CRC64;
MMKIAILGAM SEEITPLLET LKDYTKIEHA NNTYYFAKYK NHELVLAYSK IGKVNSTLSA
SVMIEKFGAQ ALLFTGVAGA FNPELEIGDL LYATKLAQYD LDITAFGHPL GFVPGNEIFI
KTDEKLNNLA LEVAKELNIK LRAGIIATGD EFICDEAKKA KIREIFNADA CEMEGASVAL
VCDALKVPCF ILRAMSDKAG EKAEFDFDEF VINSAKISAN FVLKMCEKL
