ID A0A1S8VLS0_9FUNG Unreviewed; 341 AA.
AC A0A1S8VLS0;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 13-SEP-2023, entry version 26.
DE RecName: Full=S-methyl-5'-thioadenosine phosphorylase {ECO:0000256|HAMAP-Rule:MF_03155};
DE EC=2.4.2.28 {ECO:0000256|HAMAP-Rule:MF_03155};
DE AltName: Full=5'-methylthioadenosine phosphorylase {ECO:0000256|HAMAP-Rule:MF_03155};
DE Short=MTA phosphorylase {ECO:0000256|HAMAP-Rule:MF_03155};
DE Short=MTAP {ECO:0000256|HAMAP-Rule:MF_03155};
DE Short=MTAPase {ECO:0000256|HAMAP-Rule:MF_03155};
GN ORFNames=BSLG_06769 {ECO:0000313|EMBL:OON02803.1};
OS Batrachochytrium salamandrivorans.
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Chytridiomycetes; Rhizophydiales;
OC Rhizophydiales incertae sedis; Batrachochytrium.
OX NCBI_TaxID=1357716 {ECO:0000313|EMBL:OON02803.1, ECO:0000313|Proteomes:UP000189906};
RN [1] {ECO:0000313|EMBL:OON02803.1, ECO:0000313|Proteomes:UP000189906}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BS {ECO:0000313|EMBL:OON02803.1,
RC ECO:0000313|Proteomes:UP000189906};
RA Lavstsen T., Jespersen J.S.;
RL Submitted (MAY-2016) 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 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:0000256|HAMAP-Rule:MF_03155}.
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:0000256|HAMAP-
CC Rule:MF_03155};
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:0000256|HAMAP-
CC Rule:MF_03155}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_03155}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03155}.
CC Nucleus {ECO:0000256|HAMAP-Rule:MF_03155}.
CC -!- SIMILARITY: Belongs to the PNP/MTAP phosphorylase family. MTAP
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_03155}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OON02803.1}.
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DR EMBL; LYON01001601; OON02803.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S8VLS0; -.
DR STRING; 1357716.A0A1S8VLS0; -.
DR VEuPathDB; FungiDB:BSLG_06769; -.
DR OrthoDB; 168017at2759; -.
DR UniPathway; UPA00904; UER00873.
DR Proteomes; UP000189906; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; Nucleoside phosphorylase domain; 1.
DR HAMAP; MF_01963; MTAP; 1.
DR InterPro; IPR010044; MTAP.
DR InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR InterPro; IPR018099; Purine_phosphorylase-2_CS.
DR NCBIfam; TIGR01694; MTAP; 1.
DR PANTHER; PTHR42679; S-METHYL-5'-THIOADENOSINE PHOSPHORYLASE; 1.
DR PANTHER; PTHR42679:SF2; S-METHYL-5'-THIOADENOSINE PHOSPHORYLASE; 1.
DR Pfam; PF01048; PNP_UDP_1; 1.
DR SUPFAM; SSF53167; Purine and uridine phosphorylases; 1.
DR PROSITE; PS01240; PNP_MTAP_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03155};
KW Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_03155};
KW Nucleus {ECO:0000256|HAMAP-Rule:MF_03155};
KW Purine salvage {ECO:0000256|ARBA:ARBA00022726, ECO:0000256|HAMAP-
KW Rule:MF_03155}; Reference proteome {ECO:0000313|Proteomes:UP000189906};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_03155}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..341
FT /note="S-methyl-5'-thioadenosine phosphorylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012390902"
FT DOMAIN 48..291
FT /note="Nucleoside phosphorylase"
FT /evidence="ECO:0000259|Pfam:PF01048"
FT BINDING 55
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03155"
FT BINDING 98..99
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03155"
FT BINDING 131..132
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03155"
FT BINDING 232
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03155"
FT BINDING 233
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03155"
FT BINDING 256..258
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03155"
FT SITE 214
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03155"
FT SITE 269
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03155"
SQ SEQUENCE 341 AA; 36909 MW; F77D4721B95EFDAB CRC64;
MKLFAVFIAI KLFLRTYPLA DPHSTTSLCL AFIMSEVPTM LTSVTGVDIA VIGGSGLYNL
DNLKVIGEIN PLTPWGYPSD HIVISETPNG TKIAFLARHG RGHYLTPTEV PSRANIAALK
HIGAKAIIAF SAVGSLRQEI APRDFVIPDQ IIDRTKGIRP FSFFEQGAVG HVSFADPFSN
DLGELIYNHR DACPKGVTVH NKKTLVCMEG PAFSTRAESN MYRSWGCDVI NMSVLPEAKL
AREAEMAYQM VCMSTDYDCW KIEEAAVTVE AVVANLNANA QTAKQLLLAV IPALESVLAA
KSLKSVTALE NCSAHAVMTS KSKQSPEVIA KLAYILPAVS N
//
