MTAP_AERPE
ID MTAP_AERPE Reviewed; 275 AA.
AC Q9YAQ8;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 112.
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};
GN Name=mtnP {ECO:0000255|HAMAP-Rule:MF_01963}; OrderedLocusNames=APE_1885;
OS Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS K1).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Aeropyrum.
OX NCBI_TaxID=272557;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT Aeropyrum pernix K1.";
RL DNA Res. 6:83-101(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) IN COMPLEX WITH PHOSPHATE.
RA Tsunoda M., Murakami Y., Nakamura K.T.;
RT "Crystal structure of 5'-deoxy-5'-methylthioadenosine from Aeropyrum pernix
RT (R32 form).";
RL Submitted (NOV-2004) to the PDB data bank.
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 -!- 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 -!- 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 -!- SIMILARITY: Belongs to the PNP/MTAP phosphorylase family. MTAP
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01963}.
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DR EMBL; BA000002; BAA80890.1; -; Genomic_DNA.
DR PIR; E72575; E72575.
DR PDB; 1WTA; X-ray; 1.78 A; A=1-275.
DR PDBsum; 1WTA; -.
DR AlphaFoldDB; Q9YAQ8; -.
DR SMR; Q9YAQ8; -.
DR STRING; 272557.APE_1885; -.
DR EnsemblBacteria; BAA80890; BAA80890; APE_1885.
DR KEGG; ape:APE_1885; -.
DR PATRIC; fig|272557.25.peg.1264; -.
DR eggNOG; arCOG01327; Archaea.
DR OMA; ADPFCPE; -.
DR UniPathway; UPA00904; UER00873.
DR EvolutionaryTrace; Q9YAQ8; -.
DR Proteomes; UP000002518; 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 3D-structure; Disulfide bond; Glycosyltransferase; Purine salvage;
KW Reference proteome; Transferase.
FT CHAIN 1..275
FT /note="S-methyl-5'-thioadenosine phosphorylase"
FT /id="PRO_0000415102"
FT BINDING 20
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT BINDING 62..63
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT BINDING 95..96
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT BINDING 195
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT BINDING 196
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT BINDING 219..221
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT SITE 176
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT SITE 230
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT DISULFID 143..210
FT DISULFID 205..266
FT DISULFID 264..267
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:1WTA"
FT STRAND 13..18
FT /evidence="ECO:0007829|PDB:1WTA"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:1WTA"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:1WTA"
FT STRAND 29..36
FT /evidence="ECO:0007829|PDB:1WTA"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:1WTA"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:1WTA"
FT TURN 62..67
FT /evidence="ECO:0007829|PDB:1WTA"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:1WTA"
FT HELIX 76..86
FT /evidence="ECO:0007829|PDB:1WTA"
FT STRAND 90..101
FT /evidence="ECO:0007829|PDB:1WTA"
FT STRAND 114..118
FT /evidence="ECO:0007829|PDB:1WTA"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:1WTA"
FT HELIX 144..157
FT /evidence="ECO:0007829|PDB:1WTA"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:1WTA"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:1WTA"
FT HELIX 178..186
FT /evidence="ECO:0007829|PDB:1WTA"
FT STRAND 191..196
FT /evidence="ECO:0007829|PDB:1WTA"
FT HELIX 197..206
FT /evidence="ECO:0007829|PDB:1WTA"
FT STRAND 210..219
FT /evidence="ECO:0007829|PDB:1WTA"
FT STRAND 223..226
FT /evidence="ECO:0007829|PDB:1WTA"
FT HELIX 230..251
FT /evidence="ECO:0007829|PDB:1WTA"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:1WTA"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:1WTA"
FT TURN 265..268
FT /evidence="ECO:0007829|PDB:1WTA"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:1WTA"
SQ SEQUENCE 275 AA; 30737 MW; 86CC11C1FB2DB091 CRC64;
MFEITRPPGV RAHVGVIGGS GLYDPGIVEN PVEVKVSTPY GNPSDFIVVG DVAGVKVAFL
PRHGRGHRIP PHAINYRANI WALKALGVKW VISVSAVGSL REDYRPGDFV VPDQFIDMTK
NRRHYTFYDG PVTVHVSMAD PFCEDLRQRL IDSGRRLGYT VHERGTYVCI EGPRFSTRAE
SRVWKDVFKA DIIGMTLVPE INLACEAQLC YATLAMVTDY DVWADRPVTA EEVERVMISN
VERARRMLYD VIPKLAGEPE LERCSCCRAL DTAAI
