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MTIP_METJA
ID   MTIP_METJA              Reviewed;         252 AA.
AC   Q60367;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Probable S-methyl-5'-thioinosine phosphorylase {ECO:0000255|HAMAP-Rule:MF_01963};
DE            EC=2.4.2.44 {ECO:0000255|HAMAP-Rule:MF_01963};
DE   AltName: Full=5'-methylthioinosine phosphorylase {ECO:0000255|HAMAP-Rule:MF_01963};
DE            Short=MTI phosphorylase {ECO:0000255|HAMAP-Rule:MF_01963};
DE            Short=MTIP {ECO:0000255|HAMAP-Rule:MF_01963};
GN   OrderedLocusNames=MJ0060;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
CC   -!- FUNCTION: Catalyzes the reversible phosphorylation of S-methyl-5'-
CC       thioinosine (MTI) to hypoxanthine and 5-methylthioribose-1-phosphate.
CC       Involved in the breakdown of S-methyl-5'-thioadenosine (MTA), a major
CC       by-product of polyamine biosynthesis. Catabolism of (MTA) occurs via
CC       deamination to MTI and phosphorolysis to hypoxanthine.
CC       {ECO:0000255|HAMAP-Rule:MF_01963}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=phosphate + S-methyl-5'-thioinosine = hypoxanthine + S-methyl-
CC         5-thio-alpha-D-ribose 1-phosphate; Xref=Rhea:RHEA:30643,
CC         ChEBI:CHEBI:17368, ChEBI:CHEBI:43474, ChEBI:CHEBI:48595,
CC         ChEBI:CHEBI:58533; EC=2.4.2.44; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01963};
CC   -!- PATHWAY: Purine metabolism; purine nucleoside salvage.
CC       {ECO:0000255|HAMAP-Rule:MF_01963}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_01963}.
CC   -!- MISCELLANEOUS: Although this enzyme belongs to the family of MTA
CC       phosphorylases based on sequence homology, it has been shown that
CC       conserved amino acid substitutions in the substrate binding pocket
CC       convert the substrate specificity of this enzyme from 6-aminopurines to
CC       6-oxopurines. {ECO:0000255|HAMAP-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; L77117; AAB98042.1; -; Genomic_DNA.
DR   PIR; D64307; D64307.
DR   RefSeq; WP_010869552.1; NC_000909.1.
DR   AlphaFoldDB; Q60367; -.
DR   SMR; Q60367; -.
DR   STRING; 243232.MJ_0060; -.
DR   EnsemblBacteria; AAB98042; AAB98042; MJ_0060.
DR   GeneID; 1450899; -.
DR   KEGG; mja:MJ_0060; -.
DR   eggNOG; arCOG01327; Archaea.
DR   HOGENOM; CLU_054456_0_2_2; -.
DR   InParanoid; Q60367; -.
DR   OMA; MTQCPEA; -.
DR   OrthoDB; 63298at2157; -.
DR   PhylomeDB; Q60367; -.
DR   UniPathway; UPA00606; -.
DR   Proteomes; UP000000805; 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-UniRule.
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   3: Inferred from homology;
KW   Glycosyltransferase; Purine salvage; Reference proteome; Transferase.
FT   CHAIN           1..252
FT                   /note="Probable S-methyl-5'-thioinosine phosphorylase"
FT                   /id="PRO_0000184559"
FT   BINDING         8
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT   BINDING         44..45
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT   BINDING         173
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT   BINDING         174
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT   BINDING         197..199
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT   SITE            156
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT   SITE            209
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
SQ   SEQUENCE   252 AA;  28664 MW;  DFD7C01615774A79 CRC64;
     MIGIIGGTGI AEILKGDKEE IINTKYGKAR VIIDKENEVV LLFRHGVRHN IPPHKINYRA
     NIYALKKLGV ERILAINSVG SLKEDLKPGM FFVPNDFIEF TKKREETFYD EGKVVHIDMT
     DPYCPELRNI LKSILDKNNF SYGEGVYVCT EGPRFETKKE IAIYKNWGDV VGMTGYPEVV
     LARELEMCYV SLCNITNYAC GISKNILTVD EVLEKIKEME NKILKVVEDF INYGFGERKC
     ICKDALKHAV IG
 
 
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