(data stored in SCRATCH zone)

SWISSPROT: C4KK52_SULIK

ID   C4KK52_SULIK            Unreviewed;       270 AA.
AC   C4KK52;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 44.
DE   RecName: Full=S-methyl-5'-thioadenosine phosphorylase {ECO:0000256|HAMAP-Rule:MF_01963};
DE            EC=2.4.2.28 {ECO:0000256|HAMAP-Rule:MF_01963};
DE   AltName: Full=5'-methylthioadenosine phosphorylase {ECO:0000256|HAMAP-Rule:MF_01963};
DE            Short=MTA phosphorylase {ECO:0000256|HAMAP-Rule:MF_01963};
DE            Short=MTAP {ECO:0000256|HAMAP-Rule:MF_01963};
GN   Name=mtnP {ECO:0000256|HAMAP-Rule:MF_01963};
GN   OrderedLocusNames=M164_0159 {ECO:0000313|EMBL:ACR40793.1};
OS   Sulfolobus islandicus (strain M.16.4 / Kamchatka #3).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=426118 {ECO:0000313|EMBL:ACR40793.1, ECO:0000313|Proteomes:UP000001479};
RN   [1] {ECO:0000313|EMBL:ACR40793.1, ECO:0000313|Proteomes:UP000001479}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M.16.4 / Kamchatka #3 {ECO:0000313|Proteomes:UP000001479};
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(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_01963}.
CC   -!- CATALYTIC ACTIVITY: S-methyl-5'-thioadenosine + phosphate =
CC       adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate.
CC       {ECO:0000256|HAMAP-Rule:MF_01963}.
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_01963}.
CC   -!- SUBUNIT: Homohexamer. Dimer of a homotrimer. {ECO:0000256|HAMAP-
CC       Rule:MF_01963}.
CC   -!- SIMILARITY: Belongs to the PNP/MTAP phosphorylase family. MTAP
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01963}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001402; ACR40793.1; -; Genomic_DNA.
DR   RefSeq; WP_012710318.1; NC_012726.1.
DR   ProteinModelPortal; C4KK52; -.
DR   EnsemblBacteria; ACR40793; ACR40793; M164_0159.
DR   GeneID; 8759984; -.
DR   KEGG; sid:M164_0159; -.
DR   HOGENOM; HOG000228987; -.
DR   KO; K00772; -.
DR   OMA; NLYRSWG; -.
DR   OrthoDB; POG093Z08FG; -.
DR   BioCyc; SISL426118:GI01-161-MONOMER; -.
DR   UniPathway; UPA00904; UER00873.
DR   Proteomes; UP000001479; Chromosome.
DR   GO; GO:0017061; F:S-methyl-5-thioadenosine phosphorylase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW.
DR   HAMAP; MF_01963; MTAP; 1.
DR   InterPro; IPR010044; MTAP.
DR   InterPro; IPR000845; Nucleoside_phosphorylase_d.
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;
DR   PRODOM; C4KK52.
DR   SWISS-2DPAGE; C4KK52.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001479};
KW   Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_01963};
KW   Purine salvage {ECO:0000256|HAMAP-Rule:MF_01963};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01963}.
FT   DOMAIN       10    247       PNP_UDP_1. {ECO:0000259|Pfam:PF01048}.
FT   REGION       58     59       Phosphate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01963}.
FT   REGION       91     92       Phosphate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01963}.
FT   REGION      214    216       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01963}.
FT   BINDING      16     16       Phosphate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01963}.
FT   BINDING     190    190       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01963}.
FT   BINDING     191    191       Phosphate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01963}.
FT   SITE        171    171       Important for substrate specificity.
FT                                {ECO:0000256|HAMAP-Rule:MF_01963}.
FT   SITE        225    225       Important for substrate specificity.
FT                                {ECO:0000256|HAMAP-Rule:MF_01963}.
SQ   SEQUENCE   270 AA;  30301 MW;  248455F948E06D8E CRC64;
     MIEENEKASI GIIGGSGLYD PGIFSESKER KVYTPYGEPS DLITIGKIGN KTVAFLPRHG
     RRHRIPPHKI NYRANIWALK ELGVRWVISV SAVGSLRIDY KPGDFVIPDQ FIDMTKKRDY
     TFFDGPVVAH VSMADPFCNS LRKLALETAK ELNIRTHESG TYICIEGPRF STRAESRTWR
     EVYKADIIGM TLVPEVNLAC EAQMCYATIA MVTDYDVFAE IPVTAEEVTR VMAENTEKAK
     KLLYALIQRL PEKPEEGSCS CCNSLKTALV
//

If you have problems or comments...

PBIL Back to PBIL home page