ID   MTAP_PYRHO              Reviewed;         257 AA.
AC   O57865;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2001, sequence version 2.
DT   27-MAR-2024, entry version 120.
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}; OrderedLocusNames=PH0125;
OS   Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS   100139 / OT-3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=70601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX   PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA   Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA   Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA   Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA   Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA   Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT   "Complete sequence and gene organization of the genome of a hyper-
RT   thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL   DNA Res. 5:55-76(1998).
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   -!- 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   -!- SEQUENCE CAUTION:
CC       Sequence=BAA29194.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; BA000001; BAA29194.1; ALT_INIT; Genomic_DNA.
DR   PIR; C71233; C71233.
DR   RefSeq; WP_048053039.1; NC_000961.1.
DR   AlphaFoldDB; O57865; -.
DR   SMR; O57865; -.
DR   MINT; O57865; -.
DR   STRING; 70601.gene:9377033; -.
DR   EnsemblBacteria; BAA29194; BAA29194; BAA29194.
DR   GeneID; 1444021; -.
DR   KEGG; pho:PH0125; -.
DR   eggNOG; arCOG01327; Archaea.
DR   OrthoDB; 7681at2157; -.
DR   UniPathway; UPA00904; UER00873.
DR   Proteomes; UP000000752; 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; 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:SF3; 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   Glycosyltransferase; Purine salvage; Transferase.
FT   CHAIN           1..257
FT                   /note="S-methyl-5'-thioadenosine phosphorylase"
FT                   /id="PRO_0000184561"
FT   BINDING         10
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         180
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT   BINDING         181
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT   BINDING         204..206
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT   SITE            163
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT   SITE            215
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
SQ   SEQUENCE   257 AA;  29175 MW;  35A162D939A89E90 CRC64;
     MPKIGIIGGS GVYGVFEPKE VVKVHTPYGR PSAPIEIGEI EGVEVAFIPR HGKYHEFPPH
     QVPYRANIWA LHELGVERVI AINAVGSLKE EYKPGDIVII DQFIDFTKKR EYTFYNGPKV
     AHVSMADPFC PELRKIFIET AKELNLPVHE RGTYVCIEGP RFSTRAESRM FRQFADVIGM
     TLVPEVNLAR ELGMCYVNIS TVTDYDVWAE KPVDAQEVLR VMKENEEKVQ KLLKRAIPKI
     PEERKCGCAD VLKTMFV
//