ID   MTAP_RHORT              Reviewed;         294 AA.
AC   Q2RXH9;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 92.
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, ECO:0000269|PubMed:23042035, ECO:0000269|PubMed:31950558};
DE   AltName: Full=5'-methylthioadenosine phosphorylase {ECO:0000255|HAMAP-Rule:MF_01963};
DE            Short=MTA phosphorylase {ECO:0000255|HAMAP-Rule:MF_01963, ECO:0000303|PubMed:23042035};
DE            Short=MTAP {ECO:0000255|HAMAP-Rule:MF_01963};
GN   Name=mtnP {ECO:0000255|HAMAP-Rule:MF_01963,
GN   ECO:0000303|PubMed:31950558}; OrderedLocusNames=Rru_A0361;
OS   Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 /
OS   NCIMB 8255 / S1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Rhodospirillum.
OX   NCBI_TaxID=269796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1;
RX   PubMed=21886856; DOI=10.4056/sigs.1804360;
RA   Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K.,
RA   Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C.,
RA   Mavromatis K., Richardson P., Rohde M., Goeker M., Klenk H.P., Zhang Y.,
RA   Roberts G.P., Reslewic S., Schwartz D.C.;
RT   "Complete genome sequence of Rhodospirillum rubrum type strain (S1).";
RL   Stand. Genomic Sci. 4:293-302(2011).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1;
RX   PubMed=23042035; DOI=10.1038/nchembio.1087;
RA   Erb T.J., Evans B.S., Cho K., Warlick B.P., Sriram J., Wood B.M.,
RA   Imker H.J., Sweedler J.V., Tabita F.R., Gerlt J.A.;
RT   "A RubisCO-like protein links SAM metabolism with isoprenoid
RT   biosynthesis.";
RL   Nat. Chem. Biol. 8:926-932(2012).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=31950558; DOI=10.1111/mmi.14459;
RA   North J.A., Wildenthal J.A., Erb T.J., Evans B.S., Byerly K.M., Gerlt J.A.,
RA   Tabita F.R.;
RT   "A bifunctional salvage pathway for two distinct S-adenosylmethionine by-
RT   products that is widespread in bacteria, including pathogenic Escherichia
RT   coli.";
RL   Mol. Microbiol. 113:923-937(2020).
CC   -!- FUNCTION: Catalyzes the reversible phosphorylation of S-methyl-5'-
CC       thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate
CC       (PubMed:23042035, PubMed:31950558). Involved in the breakdown of MTA, a
CC       major by-product of polyamine biosynthesis. Responsible for the first
CC       step in the methionine salvage pathway after MTA has been generated
CC       from S-adenosylmethionine. Has broad substrate specificity with 6-
CC       aminopurine nucleosides as preferred substrates (By similarity). Also
CC       catalyzes the phosphorylation of 5'-deoxyadenosine (5'dAdo) to 5-
CC       deoxyribose 1-phosphate (PubMed:31950558). Part of a bifunctional DHAP-
CC       shunt salvage pathway for SAM by-products (PubMed:31950558).
CC       {ECO:0000255|HAMAP-Rule:MF_01963, ECO:0000269|PubMed:23042035,
CC       ECO:0000269|PubMed:31950558}.
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, ECO:0000269|PubMed:23042035,
CC         ECO:0000269|PubMed:31950558};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11853;
CC         Evidence={ECO:0000269|PubMed:31950558};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5'-deoxyadenosine + phosphate = 5-deoxy-alpha-D-ribose 1-
CC         phosphate + adenine; Xref=Rhea:RHEA:24869, ChEBI:CHEBI:16708,
CC         ChEBI:CHEBI:17319, ChEBI:CHEBI:43474, ChEBI:CHEBI:58749; EC=2.4.2.28;
CC         Evidence={ECO:0000269|PubMed:31950558};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24870;
CC         Evidence={ECO:0000269|PubMed:31950558};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=14 uM for 5'-methylthioadenosine {ECO:0000269|PubMed:23042035};
CC         KM=40 uM for 5'-deoxyadenosine {ECO:0000269|PubMed:23042035};
CC         KM=41 uM for adenine {ECO:0000269|PubMed:31950558};
CC         Note=kcat is 4.5 sec(-1) with 5'-methylthioadenosine as substrate.
CC         kcat is 6.7 sec(-1) with 5'-deoxyadenosine as substrate
CC         (PubMed:23042035). kcat is 0.06 sec(-1) with adenine as substrate
CC         (PubMed:31950558). {ECO:0000269|PubMed:23042035,
CC         ECO:0000269|PubMed:31950558};
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   -!- DISRUPTION PHENOTYPE: Mutant cannot release methanethiol upon 5'-
CC       methylthioadenosine (MTA) feeding (PubMed:23042035). Deletion mutant
CC       accumulates both MTA and 5'-deoxyadenosine extracellularly
CC       (PubMed:31950558). {ECO:0000269|PubMed:23042035,
CC       ECO:0000269|PubMed:31950558}.
CC   -!- SIMILARITY: Belongs to the PNP/MTAP phosphorylase family. MTAP
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01963}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000230; ABC21166.1; -; Genomic_DNA.
DR   RefSeq; WP_011388114.1; NC_007643.1.
DR   RefSeq; YP_425453.1; NC_007643.1.
DR   AlphaFoldDB; Q2RXH9; -.
DR   SMR; Q2RXH9; -.
DR   STRING; 269796.Rru_A0361; -.
DR   EnsemblBacteria; ABC21166; ABC21166; Rru_A0361.
DR   KEGG; rru:Rru_A0361; -.
DR   PATRIC; fig|269796.9.peg.417; -.
DR   eggNOG; COG0005; Bacteria.
DR   HOGENOM; CLU_054456_0_1_5; -.
DR   PhylomeDB; Q2RXH9; -.
DR   BioCyc; MetaCyc:MONOMER-17874; -.
DR   UniPathway; UPA00904; UER00873.
DR   Proteomes; UP000001929; 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: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   1: Evidence at protein level;
KW   Glycosyltransferase; Purine salvage; Reference proteome; Transferase.
FT   CHAIN           1..294
FT                   /note="S-methyl-5'-thioadenosine phosphorylase"
FT                   /id="PRO_0000415099"
FT   BINDING         16
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT   BINDING         58..59
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT   BINDING         91..92
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT   BINDING         189
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT   BINDING         190
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT   BINDING         213..215
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT   SITE            171
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT   SITE            226
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
SQ   SEQUENCE   294 AA;  32078 MW;  58481196C7CCFB4B CRC64;
     MSEAYRQPVL GVIGGSGVYD IDGLEGARWQ TVESPFGDVS DQILRGTLDG LEMAFLPRHG
     RGHVLAPSDV NYRANIDALK RAGVTEILSV SAVGSLAEDL PPGTFVIADQ FIDRTFAREK
     SFFGKGLVAH VSMAHPVSAW LGDRVEEVLA DLAIPHRRGG TYLCMEGPQF STLAESNLYR
     QWGCHVIGMT NMPEAKLARE AEIAYCTVAM VTDFDCWHPD HDHVSVEAVV RVLLQNADKA
     RSLVKAMPAK LKDRPYPLPD GSHRSLDNAI ITHPDRRNPG MARKLSAVAG RVLG
//