(data stored in SCRATCH zone)

SWISSPROT: C5DCI5_LACTC

ID   C5DCI5_LACTC            Unreviewed;       320 AA.
AC   C5DCI5;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   08-MAY-2019, entry version 63.
DE   RecName: Full=S-methyl-5'-thioadenosine phosphorylase {ECO:0000256|HAMAP-Rule:MF_03155};
DE            EC=2.4.2.28 {ECO:0000256|HAMAP-Rule:MF_03155};
DE   AltName: Full=5'-methylthioadenosine phosphorylase {ECO:0000256|HAMAP-Rule:MF_03155};
DE            Short=MTA phosphorylase {ECO:0000256|HAMAP-Rule:MF_03155};
DE            Short=MTAP {ECO:0000256|HAMAP-Rule:MF_03155};
DE            Short=MTAPase {ECO:0000256|HAMAP-Rule:MF_03155};
GN   Name=MEU1 {ECO:0000256|HAMAP-Rule:MF_03155};
GN   OrderedLocusNames=KLTH0B03344g {ECO:0000313|EMBL:CAR21496.1};
OS   Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS   (Yeast) (Kluyveromyces thermotolerans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=559295 {ECO:0000313|EMBL:CAR21496.1, ECO:0000313|Proteomes:UP000002036};
RN   [1] {ECO:0000313|EMBL:CAR21496.1, ECO:0000313|Proteomes:UP000002036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284
RC   {ECO:0000313|Proteomes:UP000002036};
RX   PubMed=19525356; DOI=10.1101/gr.091546.109;
RG   The Genolevures Consortium;
RA   Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA   Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P.,
RA   Jubin C., Poulain J., Barbe V., Segurens B., Artiguenave F.,
RA   Anthouard V., Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R.,
RA   Durrens P., Jean G., Marck C., Martin T., Nikolski M., Rolland T.,
RA   Seret M.-L., Casaregola S., Despons L., Fairhead C., Fischer G.,
RA   Lafontaine I., Leh V., Lemaire M., de Montigny J., Neuveglise C.,
RA   Thierry A., Blanc-Lenfle I., Bleykasten C., Diffels J., Fritsch E.,
RA   Frangeul L., Goeffon A., Jauniaux N., Kachouri-Lafond R., Payen C.,
RA   Potier S., Pribylova L., Ozanne C., Richard G.-F., Sacerdot C.,
RA   Straub M.-L., Talla E.;
RT   "Comparative genomics of protoploid Saccharomycetaceae.";
RL   Genome Res. 19:1696-1709(2009).
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
CC       salvage pathway after MTA has been generated from S-
CC       adenosylmethionine. Has broad substrate specificity with 6-
CC       aminopurine nucleosides as preferred substrates.
CC       {ECO:0000256|HAMAP-Rule:MF_03155}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=phosphate + S-methyl-5'-thioadenosine = adenine + S-
CC         methyl-5-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:0000256|HAMAP-
CC         Rule:MF_03155};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via
CC       salvage pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from
CC       S-methyl-5'-thioadenosine (phosphorylase route): step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_03155}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_03155}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03155}.
CC       Nucleus {ECO:0000256|HAMAP-Rule:MF_03155}.
CC   -!- SIMILARITY: Belongs to the PNP/MTAP phosphorylase family. MTAP
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_03155}.
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DR   EMBL; CU928166; CAR21496.1; -; Genomic_DNA.
DR   RefSeq; XP_002551934.1; XM_002551888.1.
DR   STRING; 381046.XP_002551934.1; -.
DR   EnsemblFungi; CAR21496; CAR21496; KLTH0B03344g.
DR   GeneID; 8290767; -.
DR   KEGG; lth:KLTH0B03344g; -.
DR   HOGENOM; HOG000228986; -.
DR   InParanoid; C5DCI5; -.
DR   KO; K00772; -.
DR   OMA; DYDVWAE; -.
DR   OrthoDB; 1616485at2759; -.
DR   UniPathway; UPA00904; UER00873.
DR   Proteomes; UP000002036; Chromosome B.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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   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   PANTHER; PTHR42679; PTHR42679; 1.
DR   Pfam; PF01048; PNP_UDP_1; 1.
DR   SUPFAM; SSF53167; SSF53167; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5DCI5.
DR   SWISS-2DPAGE; C5DCI5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002036};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03155};
KW   Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_03155};
KW   Nucleus {ECO:0000256|HAMAP-Rule:MF_03155};
KW   Purine salvage {ECO:0000256|HAMAP-Rule:MF_03155};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002036};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_03155}.
FT   DOMAIN       16    272       PNP_UDP_1. {ECO:0000259|Pfam:PF01048}.
FT   REGION       71     72       Phosphate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_03155}.
FT   REGION      104    105       Phosphate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_03155}.
FT   REGION      237    239       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_03155}.
FT   BINDING      23     23       Phosphate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03155}.
FT   BINDING     213    213       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_03155}.
FT   BINDING     214    214       Phosphate. {ECO:0000256|HAMAP-Rule:
FT                                MF_03155}.
FT   SITE        195    195       Important for substrate specificity.
FT                                {ECO:0000256|HAMAP-Rule:MF_03155}.
FT   SITE        250    250       Important for substrate specificity.
FT                                {ECO:0000256|HAMAP-Rule:MF_03155}.
SQ   SEQUENCE   320 AA;  35195 MW;  0AC08AD53C80A1AB CRC64;
     MVNASELPKT FNGPIDLGII GGTGLYQLDC LEAIAVLPPV KTPWGQTSSP ITISKITGDS
     EEHFHVAFIS RHGLHHQFSP STVPFRANMA ALKHLRCKAV LSFSAVGSLQ QQIKPRDFVL
     PQQIIDRTKG VRDSSYFNDI GLVAHVGFGE PFSKSFAEYI SKFHGILENP GVDEPCELHF
     DIDTTVVCME GPQFSTRAES KMYRMLGGDV INMSVLPEAK LARECELPYQ MVCMSTDYDA
     WRDEAEPVTV ETVIGNLQNN GANANALASA IITDMANKMP EFMKTGDGLK GSIKMSISTK
     PAAMSKDALE KLKFLFPDYW
//

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