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Database: UniProt/TrEMBL
Entry: A5GTQ0_SYNR3
LinkDB: A5GTQ0_SYNR3
Original site: A5GTQ0_SYNR3 
ID   A5GTQ0_SYNR3            Unreviewed;       313 AA.
AC   A5GTQ0;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   19-FEB-2014, entry version 37.
DE   RecName: Full=S-methyl-5'-thioadenosine phosphorylase;
DE            EC=2.4.2.28;
DE   AltName: Full=5'-methylthioadenosine phosphorylase;
GN   Name=mtnP; OrderedLocusNames=SynRCC307_1356;
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC   Synechococcus.
OX   NCBI_TaxID=316278;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307;
RG   Genoscope;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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
CC       salvage pathway after MTA has been generated from S-
CC       adenosylmethionine. Has broad substrate specificity with 6-
CC       aminopurine nucleosides as preferred substrates (By similarity).
CC   -!- CATALYTIC ACTIVITY: S-methyl-5'-thioadenosine + phosphate =
CC       adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via
CC       salvage pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from
CC       S-methyl-5'-thioadenosine (phosphorylase route): step 1/1.
CC   -!- SUBUNIT: Homohexamer. Dimer of a homotrimer (By similarity).
CC   -!- SIMILARITY: Belongs to the PNP/MTAP phosphorylase family. MTAP
CC       subfamily.
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DR   EMBL; CT978603; CAK28259.1; -; Genomic_DNA.
DR   RefSeq; YP_001227612.1; NC_009482.1.
DR   ProteinModelPortal; A5GTQ0; -.
DR   STRING; 316278.SynRCC307_1356; -.
DR   EnsemblBacteria; CAK28259; CAK28259; SynRCC307_1356.
DR   GeneID; 5156631; -.
DR   KEGG; syr:SynRCC307_1356; -.
DR   PATRIC; 23823609; VBISynSp108374_1357.
DR   eggNOG; COG0005; -.
DR   HOGENOM; HOG000228986; -.
DR   KO; K00772; -.
DR   OMA; MTNHTEA; -.
DR   OrthoDB; EOG6KHFXC; -.
DR   UniPathway; UPA00904; UER00873.
DR   GO; GO:0004645; F:phosphorylase activity; IEA:InterPro.
DR   GO; GO:0017061; F:S-methyl-5-thioadenosine phosphorylase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW.
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; IPR001369; PNP/MTAP.
DR   InterPro; IPR018099; Purine_phosphorylase-2_CS.
DR   PANTHER; PTHR11904; PTHR11904; 1.
DR   Pfam; PF01048; PNP_UDP_1; 1.
DR   TIGRFAMs; TIGR01694; MTAP; 1.
DR   PROSITE; PS01240; PNP_MTAP_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Glycosyltransferase; Purine salvage; Transferase.
FT   REGION       73     74       Phosphate binding (By similarity).
FT   REGION      106    107       Phosphate binding (By similarity).
FT   REGION      231    233       Substrate binding (By similarity).
FT   BINDING      31     31       Phosphate (By similarity).
FT   BINDING     207    207       Substrate; via amide nitrogen (By
FT                                similarity).
FT   BINDING     208    208       Phosphate (By similarity).
FT   SITE        189    189       Important for substrate specificity (By
FT                                similarity).
FT   SITE        244    244       Important for substrate specificity (By
FT                                similarity).
SQ   SEQUENCE   313 AA;  34165 MW;  BE467F1589960C02 CRC64;
     MVHEPSHKTM ATAQPPVSDL SNATIGILGG SGLYAMEELR DVEELEVPTP FGQPSDRLIR
     GNLDGTTVIF LARHGRHHSY LPSEVPYRAN IWAMRSLGVR WILSCSAVGS LQEQHRPLDL
     VIPDQFIDRT QGRAASFFGE GAVAHVAFAD PFCQTLSGLL ADAAQSVLPE GRRLHRGGTY
     LCMQGPAFST KAESELYRSW GCDVIGMTNH TEARLAREAE IAYSTLAMVT DYDCWHPDHD
     AVTVEMVINN LRANATTAQQ VVRHAAQAIQ KQKPSSPAHS ALQNGLLTAP EAVPAATRQK
     LDLFTRPYWG AAS
//
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