ID Q12ZW5_RHOPS Unreviewed; 291 AA.
AC Q12ZW5;
DT 31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE RecName: Full=S-methyl-5'-thioadenosine phosphorylase {ECO:0000256|HAMAP-Rule:MF_01963};
DE EC=2.4.2.28 {ECO:0000256|HAMAP-Rule:MF_01963};
DE AltName: Full=5'-methylthioadenosine phosphorylase {ECO:0000256|HAMAP-Rule:MF_01963};
DE Short=MTA phosphorylase {ECO:0000256|HAMAP-Rule:MF_01963};
DE Short=MTAP {ECO:0000256|HAMAP-Rule:MF_01963};
GN Name=mtnP {ECO:0000256|HAMAP-Rule:MF_01963};
GN OrderedLocusNames=RPD_4408 {ECO:0000313|EMBL:ABE41624.1};
OS Rhodopseudomonas palustris (strain BisB5).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=316057 {ECO:0000313|EMBL:ABE41624.1, ECO:0000313|Proteomes:UP000001818};
RN [1] {ECO:0000313|EMBL:ABE41624.1, ECO:0000313|Proteomes:UP000001818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisB5 {ECO:0000313|EMBL:ABE41624.1,
RC ECO:0000313|Proteomes:UP000001818};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Pelletier D.A., Kyrpides N., Lykidis A., Oda Y., Harwood C.S.,
RA Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL Submitted (MAR-2006) 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_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:0000256|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:0000256|HAMAP-
CC Rule:MF_01963}.
CC -!- SUBUNIT: Homohexamer. Dimer of a homotrimer. {ECO:0000256|HAMAP-
CC Rule:MF_01963}.
CC -!- SIMILARITY: Belongs to the PNP/MTAP phosphorylase family. MTAP
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01963}.
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DR EMBL; CP000283; ABE41624.1; -; Genomic_DNA.
DR AlphaFoldDB; Q12ZW5; -.
DR STRING; 316057.RPD_4408; -.
DR KEGG; rpd:RPD_4408; -.
DR eggNOG; COG0005; Bacteria.
DR HOGENOM; CLU_054456_0_1_5; -.
DR BioCyc; RPAL316057:RPD_RS22175-MONOMER; -.
DR UniPathway; UPA00904; UER00873.
DR Proteomes; UP000001818; 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 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.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_01963,
KW ECO:0000313|EMBL:ABE41624.1};
KW Purine salvage {ECO:0000256|HAMAP-Rule:MF_01963};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01963, ECO:0000313|EMBL:ABE41624.1}.
FT DOMAIN 6..243
FT /note="Nucleoside phosphorylase"
FT /evidence="ECO:0000259|Pfam:PF01048"
FT BINDING 12
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT BINDING 54..55
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT BINDING 87..88
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT BINDING 186
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT BINDING 209..211
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT SITE 167
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT SITE 222
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
SQ SEQUENCE 291 AA; 31568 MW; 8B182F383AC10887 CRC64;
MTKAVLGIIG GSGIYDLPGL EDVREEAIES PWGEPSSAVR RGNIAGLPIV FMPRHDKGHR
LSPSDINYRA NIDVLKRAGV TDLISLSACG SFKEELPPGS FVLVDQFVDR TYKRESSFFG
RGCVAHVSMA HPVSPRLRIH LAAAAEAEGI AMARGGTYLC MEGPQFSSYA ESVTYKQAGY
SVIGMTNMPE AKLAREAEIC YASVAMVTDF DCWHPDHDAV TVQDIIRVLS SNAEKAKSLV
ARLAQDFPRE HEPCPIGSDR ALDTALITQP DARDPELLKK LDAVAGRILK G
//
