ID A5GTQ0_SYNR3 Unreviewed; 313 AA.
AC A5GTQ0;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 01-MAY-2013, entry version 33.
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; VVPDQFI; -.
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:HAMAP.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:HAMAP.
DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW.
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
//
