MTAP_RHORT
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 03-AUG-2022, entry version 87.
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, ECO:0000303|PubMed:31950558};
GN OrderedLocusNames=Rru_A0361;
OS Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 /
OS NCIMB 8255 / S1).
OC Bacteria; Proteobacteria; 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 OMA; ADPFCPE; -.
DR OrthoDB; 1364220at2; -.
DR PhylomeDB; Q2RXH9; -.
DR BioCyc; MetaCyc:MON-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; -; 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 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
