MTAP_MYCS2
ID MTAP_MYCS2 Reviewed; 259 AA.
AC A0QR54; I7FF12;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=S-methyl-5'-thioadenosine phosphorylase {ECO:0000255|HAMAP-Rule:MF_01963};
DE EC=2.4.2.28 {ECO:0000255|HAMAP-Rule:MF_01963};
DE AltName: Full=5'-methylthioadenosine phosphorylase {ECO:0000255|HAMAP-Rule:MF_01963};
DE Short=MTA phosphorylase {ECO:0000255|HAMAP-Rule:MF_01963};
DE Short=MTAP {ECO:0000255|HAMAP-Rule:MF_01963};
GN Name=mtnP {ECO:0000255|HAMAP-Rule:MF_01963}; Synonyms=pnp;
GN OrderedLocusNames=MSMEG_0990, MSMEI_0963;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=21821769; DOI=10.1128/jb.05394-11;
RA Buckoreelall K., Wilson L., Parker W.B.;
RT "Identification and characterization of two adenosine phosphorylase
RT activities in Mycobacterium smegmatis.";
RL J. Bacteriol. 193:5668-5674(2011).
CC -!- FUNCTION: Catalyzes the reversible phosphorylation of S-methyl-5'-
CC thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate.
CC Involved in the breakdown of MTA, a major by-product of polyamine
CC biosynthesis. Responsible for the first step in the methionine salvage
CC pathway after MTA has been generated from S-adenosylmethionine. Has
CC broad substrate specificity with 6-aminopurine nucleosides as preferred
CC substrates. {ECO:0000255|HAMAP-Rule:MF_01963}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=phosphate + S-methyl-5'-thioadenosine = adenine + S-methyl-5-
CC thio-alpha-D-ribose 1-phosphate; Xref=Rhea:RHEA:11852,
CC ChEBI:CHEBI:16708, ChEBI:CHEBI:17509, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58533; EC=2.4.2.28; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01963};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.6 uM for S-methyl-5'-thioadenosine
CC {ECO:0000269|PubMed:21821769};
CC KM=310 uM for adenosine {ECO:0000269|PubMed:21821769};
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 (phosphorylase route): step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_01963}.
CC -!- SUBUNIT: Homohexamer. Dimer of a homotrimer. {ECO:0000255|HAMAP-
CC Rule:MF_01963}.
CC -!- SIMILARITY: Belongs to the PNP/MTAP phosphorylase family. MTAP
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01963}.
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; CP000480; ABK70512.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP37443.1; -; Genomic_DNA.
DR RefSeq; WP_011727338.1; NC_018289.1.
DR RefSeq; YP_885392.1; NC_008596.1.
DR AlphaFoldDB; A0QR54; -.
DR SMR; A0QR54; -.
DR STRING; 246196.MSMEI_0963; -.
DR EnsemblBacteria; ABK70512; ABK70512; MSMEG_0990.
DR EnsemblBacteria; AFP37443; AFP37443; MSMEI_0963.
DR GeneID; 66739154; -.
DR KEGG; msg:MSMEI_0963; -.
DR KEGG; msm:MSMEG_0990; -.
DR PATRIC; fig|246196.19.peg.978; -.
DR eggNOG; COG0005; Bacteria.
DR OMA; ADPFCPE; -.
DR SABIO-RK; A0QR54; -.
DR UniPathway; UPA00904; UER00873.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0017061; F:S-methyl-5-thioadenosine phosphorylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniRule.
DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW.
DR CDD; cd09010; MTAP_SsMTAPII_like_MTIP; 1.
DR Gene3D; 3.40.50.1580; -; 1.
DR HAMAP; MF_01963; MTAP; 1.
DR InterPro; IPR010044; MTAP.
DR InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR PANTHER; PTHR42679; PTHR42679; 1.
DR Pfam; PF01048; PNP_UDP_1; 1.
DR SUPFAM; SSF53167; SSF53167; 1.
DR TIGRFAMs; TIGR01694; MTAP; 1.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Purine salvage; Reference proteome; Transferase.
FT CHAIN 1..259
FT /note="S-methyl-5'-thioadenosine phosphorylase"
FT /id="PRO_0000415095"
FT BINDING 9
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT BINDING 50..51
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT BINDING 175
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT BINDING 176
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT BINDING 199..201
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT SITE 157
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT SITE 212
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
SQ SEQUENCE 259 AA; 27723 MW; 8D379609536F84FF CRC64;
MMLGVIGGSG FYTFFGSDAR AVSVETPYGP PSAPITVGTV GDHEVAFLPR HGVKHEFSPH
TVPYRANLWA LRSLGVRRVF APCAVGSLTP DLGPGSIVVP DQLVDRTSGR DDTYFDSGGI
HVAFADPYCP TLRAAATGLP GVVDGGTMVV IQGPRFSTRA ESRWFASQGF TLVNMTGYPE
AVLARELEMC YAAVALVTDL DAGIEVGSGV RAVDVFAEFE RNMPPFKKLV FEALEAVEVE
RTCTHCLTHS GVQLPFELP
