MTAP_SACS2
ID MTAP_SACS2 Reviewed; 270 AA.
AC Q97W94;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=MTAPII {ECO:0000255|HAMAP-Rule:MF_01963};
GN Name=mtnP {ECO:0000255|HAMAP-Rule:MF_01963}; OrderedLocusNames=SSO2343;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [2]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF CYS-259; CYS-261
RP AND CYS-262, AND SUBUNIT.
RX PubMed=15819883; DOI=10.1111/j.1742-4658.2005.04619.x;
RA Cacciapuoti G., Forte S., Moretti M.A., Brio A., Zappia V., Porcelli M.;
RT "A novel hyperthermostable 5'-deoxy-5'-methylthioadenosine phosphorylase
RT from the archaeon Sulfolobus solfataricus.";
RL FEBS J. 272:1886-1899(2005).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH SUBSTRATES, AND
RP DISULFIDE BONDS.
RX PubMed=16414070; DOI=10.1016/j.jmb.2005.12.040;
RA Zhang Y., Porcelli M., Cacciapuoti G., Ealick S.E.;
RT "The crystal structure of 5'-deoxy-5'-methylthioadenosine phosphorylase II
RT from Sulfolobus solfataricus, a thermophilic enzyme stabilized by
RT intramolecular disulfide bonds.";
RL J. Mol. Biol. 357:252-262(2006).
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:15819883}.
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=0.7 mM for S-methyl-5'-thioadenosine
CC {ECO:0000269|PubMed:15819883};
CC KM=270 uM for adenosine {ECO:0000269|PubMed:15819883};
CC Temperature dependence:
CC Optimum temperature is 120 degrees Celsius. Highly thermostable.
CC {ECO:0000269|PubMed:15819883};
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:15819883,
CC ECO:0000269|PubMed:16414070}.
CC -!- SIMILARITY: Belongs to the PNP/MTAP phosphorylase family. MTAP
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01963}.
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DR EMBL; AE006641; AAK42494.1; -; Genomic_DNA.
DR PIR; G90404; G90404.
DR RefSeq; WP_009989516.1; NC_002754.1.
DR PDB; 2A8Y; X-ray; 1.45 A; A/B/C/D/E/F/G/H/I/J/K/L=1-270.
DR PDB; 3T94; X-ray; 1.45 A; A/B/C/D/E/F=1-270.
DR PDBsum; 2A8Y; -.
DR PDBsum; 3T94; -.
DR AlphaFoldDB; Q97W94; -.
DR SMR; Q97W94; -.
DR STRING; 273057.SSO2343; -.
DR EnsemblBacteria; AAK42494; AAK42494; SSO2343.
DR GeneID; 44128068; -.
DR KEGG; sso:SSO2343; -.
DR PATRIC; fig|273057.12.peg.2427; -.
DR eggNOG; arCOG01327; Archaea.
DR HOGENOM; CLU_054456_0_2_2; -.
DR InParanoid; Q97W94; -.
DR OMA; ADPFCPE; -.
DR PhylomeDB; Q97W94; -.
DR BRENDA; 2.4.2.1; 6163.
DR BRENDA; 2.4.2.28; 6163.
DR UniPathway; UPA00904; UER00873.
DR EvolutionaryTrace; Q97W94; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0017061; F:S-methyl-5-thioadenosine phosphorylase activity; IBA:GO_Central.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IBA:GO_Central.
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 3D-structure; Disulfide bond; Glycosyltransferase; Purine salvage;
KW Reference proteome; Transferase.
FT CHAIN 1..270
FT /note="S-methyl-5'-thioadenosine phosphorylase"
FT /id="PRO_0000415109"
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 190
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT BINDING 191
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT BINDING 214..216
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 225
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT DISULFID 138..205
FT /evidence="ECO:0000269|PubMed:16414070"
FT DISULFID 200..262
FT /evidence="ECO:0000269|PubMed:16414070"
FT DISULFID 259..261
FT /evidence="ECO:0000269|PubMed:16414070"
FT MUTAGEN 259
FT /note="C->S: Reduces thermostability of the enzyme; when
FT associated with S-261."
FT /evidence="ECO:0000269|PubMed:15819883"
FT MUTAGEN 261
FT /note="C->S: Reduces thermostability of the enzyme; when
FT associated with S-259."
FT /evidence="ECO:0000269|PubMed:15819883"
FT MUTAGEN 262
FT /note="C->S: Reduces thermostability of the enzyme."
FT /evidence="ECO:0000269|PubMed:15819883"
FT STRAND 9..14
FT /evidence="ECO:0007829|PDB:2A8Y"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:2A8Y"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:2A8Y"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:2A8Y"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:2A8Y"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:2A8Y"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:2A8Y"
FT HELIX 72..81
FT /evidence="ECO:0007829|PDB:2A8Y"
FT STRAND 86..97
FT /evidence="ECO:0007829|PDB:2A8Y"
FT STRAND 110..114
FT /evidence="ECO:0007829|PDB:2A8Y"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:2A8Y"
FT HELIX 139..152
FT /evidence="ECO:0007829|PDB:2A8Y"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:2A8Y"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:2A8Y"
FT HELIX 173..181
FT /evidence="ECO:0007829|PDB:2A8Y"
FT STRAND 187..191
FT /evidence="ECO:0007829|PDB:2A8Y"
FT HELIX 192..201
FT /evidence="ECO:0007829|PDB:2A8Y"
FT STRAND 205..214
FT /evidence="ECO:0007829|PDB:2A8Y"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:2A8Y"
FT HELIX 225..234
FT /evidence="ECO:0007829|PDB:2A8Y"
FT HELIX 236..249
FT /evidence="ECO:0007829|PDB:2A8Y"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:3T94"
FT TURN 260..263
FT /evidence="ECO:0007829|PDB:3T94"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:2A8Y"
SQ SEQUENCE 270 AA; 30141 MW; 682A166698935A88 CRC64;
MIEQNEKASI GIIGGSGLYD PGIFSESKEI KVYTPYGQPS DFITIGKIGN KSVAFLPRHG
RGHRIPPHKI NYRANIWALK ELGVRWVISV SAVGSLRMDY KLGDFVIPDQ FIDMTKNREY
SFFDGPVVAH VSMADPFCNS LRKLAIETAK ELNIKTHESG TYICIEGPRF STRAESRTWR
EVYKADIIGM TLVPEVNLAC EAQMCYATIA MVTDYDVFAE IPVTAEEVTR VMAENTEKAK
KLLYALIQKL PEKPEEGSCS CCNSLKTALV
