ID A0A1Y1V5V9_9FUNG Unreviewed; 303 AA.
AC A0A1Y1V5V9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 13-SEP-2023, entry version 21.
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=BCR36DRAFT_355919 {ECO:0000313|EMBL:ORX47314.1};
OS Piromyces finnis.
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC Neocallimastigaceae; Piromyces.
OX NCBI_TaxID=1754191 {ECO:0000313|EMBL:ORX47314.1, ECO:0000313|Proteomes:UP000193719};
RN [1] {ECO:0000313|EMBL:ORX47314.1, ECO:0000313|Proteomes:UP000193719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=finn {ECO:0000313|Proteomes:UP000193719};
RG DOE Joint Genome Institute;
RA Haitjema C.H., Gilmore S.P., Henske J.K., Solomon K.V., De Groot R.,
RA Kuo A., Mondo S.J., Salamov A.A., Labutti K., Zhao Z., Chiniquy J.,
RA Barry K., Brewer H.M., Purvine S.O., Wright A.T., Boxma B., Van Alen T.,
RA Hackstein J.H., Baker S.E., Grigoriev I.V., O'Malley M.A.;
RT "Genomes of anaerobic fungi encode conserved fungal cellulosomes for
RT biomass hydrolysis.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ORX47314.1, ECO:0000313|Proteomes:UP000193719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=finn {ECO:0000313|Proteomes:UP000193719};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (AUG-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:ORX47314.1}.
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DR EMBL; MCFH01000031; ORX47314.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1V5V9; -.
DR STRING; 1754191.A0A1Y1V5V9; -.
DR EnsemblFungi; ORX47314; ORX47314; BCR36DRAFT_355919.
DR OrthoDB; 168017at2759; -.
DR UniPathway; UPA00904; UER00873.
DR Proteomes; UP000193719; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003729; F:mRNA binding; IEA:EnsemblFungi.
DR GO; GO:0017061; F:S-methyl-5-thioadenosine phosphorylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006537; P:glutamate biosynthetic process; IEA:EnsemblFungi.
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:UP000193719};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_03155}.
FT DOMAIN 8..252
FT /note="Nucleoside phosphorylase"
FT /evidence="ECO:0000259|Pfam:PF01048"
FT BINDING 15
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03155"
FT BINDING 58..59
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03155"
FT BINDING 91..92
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03155"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03155"
FT BINDING 194
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03155"
FT BINDING 217..219
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03155"
FT SITE 175
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03155"
FT SITE 230
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03155"
SQ SEQUENCE 303 AA; 33409 MW; A4CE6A4A6D5A036B CRC64;
MSKYTDVKIA FIGGSGLYRL DTLKPVDEIE PETPWGKPSA KIVICETASG NHVAFLARHG
TGHHLNPSEV PARANIAALK SIGVEVIIAF SAVGSLREEI KPRDFILPSQ IIDRTKGIRP
STFFEKGCAA HIAFGEPFNK DLADIIYSQK NTLQGENVEM HRDKCLICME GPAFSTRAES
NMYRMVGGDI INMSVLPEAK LAMEAEIAYQ MICMATDYDS WRVSEEVVTV ETVVANLNAN
TSNANQLAVN ILPALEEALY ENKVELPRVK ALKGSMRFAS ITAKEARNLE AVRKIEYILP
GYF
//
