MTAP_PROMA
ID MTAP_PROMA Reviewed; 314 AA.
AC Q7VDN6;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=Pro_0332;
OS Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=167539;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SARG / CCMP1375 / SS120;
RX PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F., Makarova K.S.,
RA Ostrowski M., Oztas S., Robert C., Rogozin I.B., Scanlan D.J.,
RA Tandeau de Marsac N., Weissenbach J., Wincker P., Wolf Y.I., Hess W.R.;
RT "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120, a
RT nearly minimal oxyphototrophic genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(2003).
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}.
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DR EMBL; AE017126; AAP99378.1; -; Genomic_DNA.
DR RefSeq; NP_874726.1; NC_005042.1.
DR RefSeq; WP_011124487.1; NC_005042.1.
DR AlphaFoldDB; Q7VDN6; -.
DR SMR; Q7VDN6; -.
DR STRING; 167539.Pro_0332; -.
DR EnsemblBacteria; AAP99378; AAP99378; Pro_0332.
DR GeneID; 54199694; -.
DR KEGG; pma:Pro_0332; -.
DR PATRIC; fig|167539.5.peg.341; -.
DR eggNOG; COG0005; Bacteria.
DR HOGENOM; CLU_054456_0_1_3; -.
DR OMA; ADPFCPE; -.
DR OrthoDB; 1364220at2; -.
DR UniPathway; UPA00904; UER00873.
DR Proteomes; UP000001420; 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; -; 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 PANTHER; PTHR42679; PTHR42679; 1.
DR Pfam; PF01048; PNP_UDP_1; 1.
DR SUPFAM; SSF53167; SSF53167; 1.
DR TIGRFAMs; TIGR01694; MTAP; 1.
DR PROSITE; PS01240; PNP_MTAP_2; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase; Purine salvage; Reference proteome; Transferase.
FT CHAIN 1..314
FT /note="S-methyl-5'-thioadenosine phosphorylase"
FT /id="PRO_0000415097"
FT BINDING 31
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT BINDING 73..74
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT BINDING 106..107
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT BINDING 207
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT BINDING 208
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT BINDING 231..233
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT SITE 189
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT SITE 244
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
SQ SEQUENCE 314 AA; 35041 MW; 2E6812A63C762E3B CRC64;
MINKHFSSEE IEQDGKSCLL KNARLGVLGG SGLYSIDSIE NIKELDIETP YGKPSDSLRI
GNLGGMEVVF LARHGRHHIY TPTEIPYRAN IWALRSLNVR WILSPSAVGS LQEQVRPLDM
VVPDQFIDRT HQRPLTFFCD GAVAHVTMAD PFCPTLSRLL AEEGELLMPE ARQVHKGGTY
LAMEGPAFST RAESQLYRSW GCKVIGMTNH TEARLAREAE IAYTSLSMVT DYDCWHEGFG
NVSVDLVIEN LAANAKLASK IVEATAKRIS KLLPPSEAHT ALKNSLMTSK DKVSETTREK
INLFTENYWG KFNK
