ID A0A1H7IML9_9RHOB Unreviewed; 285 AA.
AC A0A1H7IML9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
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 ORFNames=SAMN04488526_1108 {ECO:0000313|EMBL:SEK63743.1};
OS Jannaschia helgolandensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Jannaschia.
OX NCBI_TaxID=188906 {ECO:0000313|EMBL:SEK63743.1, ECO:0000313|Proteomes:UP000199283};
RN [1] {ECO:0000313|EMBL:SEK63743.1, ECO:0000313|Proteomes:UP000199283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14858 {ECO:0000313|EMBL:SEK63743.1,
RC ECO:0000313|Proteomes:UP000199283};
RA de Groot N.N.;
RL Submitted (OCT-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_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; FNZQ01000001; SEK63743.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7IML9; -.
DR STRING; 188906.SAMN04488526_1108; -.
DR OrthoDB; 1523230at2; -.
DR UniPathway; UPA00904; UER00873.
DR Proteomes; UP000199283; Unassembled WGS sequence.
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 Purine salvage {ECO:0000256|HAMAP-Rule:MF_01963};
KW Reference proteome {ECO:0000313|Proteomes:UP000199283};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01963}.
FT DOMAIN 4..240
FT /note="Nucleoside phosphorylase"
FT /evidence="ECO:0000259|Pfam:PF01048"
FT BINDING 10
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT BINDING 52..53
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT BINDING 85..86
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT BINDING 184
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT BINDING 207..209
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT SITE 165
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT SITE 220
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
SQ SEQUENCE 285 AA; 30203 MW; 8348767D43C3019D CRC64;
MAVIGIIGGS GLYQVDGLQN AEWRALDTPW GAPSDALLHG MLDGTAMVFL PRHGRGHVHT
PSSVPYRANI AAMKAAGVTH LVSVSATGSF RDDMAPGDFV IVDQFIDRTV QRAASFFGPG
LVAHVSIAHP VCPLLSAACA DAARGAGATV HEGGTYLAME GPQFSTVAES RLYREWGCDV
IGMTNMPEAR LAREAELHYA SVAMITDFDS WHPDHGSVQI TDILRTLQGN VGRAAEMVAA
LPGLLTDAAC SEGCDHALDH AIMTAPDMRD PAMVYRMKTI AGRVL
//
