MTAP_PYRFU
ID MTAP_PYRFU Reviewed; 257 AA.
AC Q8U4Q8;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 97.
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};
DE Short=PfMTAP;
GN Name=mtnP {ECO:0000255|HAMAP-Rule:MF_01963}; OrderedLocusNames=PF0016;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [2]
RP PROTEIN SEQUENCE OF 1-27, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBUNIT.
RX PubMed=12664268; DOI=10.1007/s00792-002-0307-2;
RA Cacciapuoti G., Bertoldo C., Brio A., Zappia V., Porcelli M.;
RT "Purification and characterization of 5'-methylthioadenosine phosphorylase
RT from the hyperthermophilic archaeon Pyrococcus furiosus: substrate
RT specificity and primary structure analysis.";
RL Extremophiles 7:159-168(2003).
RN [3]
RP FUNCTION, AND DISULFIDE BONDS.
RX PubMed=15606771; DOI=10.1111/j.1432-1033.2004.04449.x;
RA Cacciapuoti G., Moretti M.A., Forte S., Brio A., Camardella L., Zappia V.,
RA Porcelli M.;
RT "Methylthioadenosine phosphorylase from the archaeon Pyrococcus furiosus.
RT Mechanism of the reaction and assignment of disulfide bonds.";
RL Eur. J. Biochem. 271:4834-4844(2004).
RN [4]
RP FUNCTION.
RX PubMed=21683167; DOI=10.1016/j.bbapap.2011.06.001;
RA Cacciapuoti G., Marabotti A., Fuccio F., Porcelli M.;
RT "Unraveling the structural and functional differences between purine
RT nucleoside phosphorylase and 5'-deoxy-5'-methylthioadenosine phosphorylase
RT from the archaeon Pyrococcus furiosus.";
RL Biochim. Biophys. Acta 1814:1358-1366(2011).
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 ECO:0000269|PubMed:12664268, ECO:0000269|PubMed:15606771,
CC ECO:0000269|PubMed:21683167}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=147 uM for S-methyl-5'-thioadenosine
CC {ECO:0000269|PubMed:12664268};
CC KM=109 uM for adenosine {ECO:0000269|PubMed:12664268};
CC KM=963 uM for inosine {ECO:0000269|PubMed:12664268};
CC KM=916 uM for guanosine {ECO:0000269|PubMed:12664268};
CC pH dependence:
CC Optimum pH is 7.4. Active from pH 5 to 10.
CC {ECO:0000269|PubMed:12664268};
CC Temperature dependence:
CC Optimum temperature is 125 degrees Celsius. Thermostable up to 137
CC degrees Celsius. {ECO:0000269|PubMed:12664268};
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, ECO:0000269|PubMed:12664268}.
CC -!- SIMILARITY: Belongs to the PNP/MTAP phosphorylase family. MTAP
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01963}.
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DR EMBL; AE009950; AAL80140.1; -; Genomic_DNA.
DR RefSeq; WP_011011128.1; NZ_CP023154.1.
DR AlphaFoldDB; Q8U4Q8; -.
DR SMR; Q8U4Q8; -.
DR STRING; 186497.PF0016; -.
DR EnsemblBacteria; AAL80140; AAL80140; PF0016.
DR GeneID; 41713908; -.
DR KEGG; pfu:PF0016; -.
DR PATRIC; fig|186497.12.peg.17; -.
DR eggNOG; arCOG01327; Archaea.
DR HOGENOM; CLU_054456_0_2_2; -.
DR OMA; ADPFCPE; -.
DR OrthoDB; 63298at2157; -.
DR PhylomeDB; Q8U4Q8; -.
DR BRENDA; 2.4.2.28; 5243.
DR SABIO-RK; Q8U4Q8; -.
DR UniPathway; UPA00904; UER00873.
DR Proteomes; UP000001013; 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 Direct protein sequencing; Disulfide bond; Glycosyltransferase;
KW Purine salvage; Reference proteome; Transferase.
FT CHAIN 1..257
FT /note="S-methyl-5'-thioadenosine phosphorylase"
FT /id="PRO_0000415107"
FT BINDING 10
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT BINDING 50..51
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT BINDING 180
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT BINDING 181
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT BINDING 204..206
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT SITE 163
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT SITE 215
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT DISULFID 130..195
FT /evidence="ECO:0000269|PubMed:15606771"
FT DISULFID 246..248
FT /evidence="ECO:0000269|PubMed:15606771"
SQ SEQUENCE 257 AA; 29220 MW; A1B8194889A30AB8 CRC64;
MPKIGIIGGS GVYGIFEPKE TVKVHTPYGR PSAPVEIGEI EGVEVAFIPR HGKYHEFPPH
EVPYRANIWA LHELGVERVI AVNAVGSLKE EYKPGDIVII DQFIDFTKKR EYTFYNGPRV
AHISMADPFC PELRRIFIET AKELNLPVHE KGTYICIEGP RFSTRAESRM FRQFADVIGM
TLVPEVNLAR ELGMCYVNIS TVTDYDVWAE KPVDAQEVLR VMKENEEKVQ KLLKRAIPKI
PEERKCGCAD VLKTMFV
