(data stored in SCRATCH zone)

SWISSPROT: A1SDR5_NOCSJ

ID   A1SDR5_NOCSJ            Unreviewed;       409 AA.
AC   A1SDR5;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   08-MAY-2019, entry version 70.
DE   RecName: Full=Methylthioribose kinase {ECO:0000256|HAMAP-Rule:MF_01683};
DE            Short=MTR kinase {ECO:0000256|HAMAP-Rule:MF_01683};
DE            EC=2.7.1.100 {ECO:0000256|HAMAP-Rule:MF_01683};
GN   Name=mtnK {ECO:0000256|HAMAP-Rule:MF_01683};
GN   OrderedLocusNames=Noca_0407 {ECO:0000313|EMBL:ABL79950.1};
OS   Nocardioides sp. (strain ATCC BAA-499 / JS614).
OC   Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae;
OC   Nocardioides.
OX   NCBI_TaxID=196162 {ECO:0000313|EMBL:ABL79950.1, ECO:0000313|Proteomes:UP000000640};
RN   [1] {ECO:0000313|Proteomes:UP000000640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-499 / JS614 {ECO:0000313|Proteomes:UP000000640};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Thompson L.S., Brettin T., Bruce D., Han C., Tapia R.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Mattes T., Gossett J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Nocardioides sp. JS614.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABL79950.1, ECO:0000313|Proteomes:UP000000640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-499 / JS614 {ECO:0000313|Proteomes:UP000000640};
RX   PubMed=21551312; DOI=10.1128/JB.05109-11;
RA   Coleman N.V., Wilson N.L., Barry K., Brettin T.S., Bruce D.C.,
RA   Copeland A., Dalin E., Detter J.C., Del Rio T.G., Goodwin L.A.,
RA   Hammon N.M., Han S., Hauser L.J., Israni S., Kim E., Kyrpides N.,
RA   Land M.L., Lapidus A., Larimer F.W., Lucas S., Pitluck S.,
RA   Richardson P., Schmutz J., Tapia R., Thompson S., Tice H.N.,
RA   Spain J.C., Gossett J.G., Mattes T.E.;
RT   "Genome Sequence of the ethene- and vinyl chloride-oxidizing
RT   actinomycete Nocardioides sp. strain JS614.";
RL   J. Bacteriol. 193:3399-3400(2011).
CC   -!- FUNCTION: Catalyzes the phosphorylation of methylthioribose into
CC       methylthioribose-1-phosphate. {ECO:0000256|HAMAP-Rule:MF_01683}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + S-methyl-5-thio-D-ribose = ADP + H(+) + S-methyl-5-
CC         thio-alpha-D-ribose 1-phosphate; Xref=Rhea:RHEA:22312,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16895, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:58533, ChEBI:CHEBI:456216; EC=2.7.1.100;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01683};
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 (hydrolase route): step 2/2.
CC       {ECO:0000256|HAMAP-Rule:MF_01683}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01683}.
CC   -!- SIMILARITY: Belongs to the methylthioribose kinase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01683}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01683}.
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DR   EMBL; CP000509; ABL79950.1; -; Genomic_DNA.
DR   STRING; 196162.Noca_0407; -.
DR   EnsemblBacteria; ABL79950; ABL79950; Noca_0407.
DR   KEGG; nca:Noca_0407; -.
DR   eggNOG; ENOG4105CT5; Bacteria.
DR   eggNOG; COG4857; LUCA.
DR   HOGENOM; HOG000082744; -.
DR   KO; K00899; -.
DR   OMA; AHNADFE; -.
DR   UniPathway; UPA00904; UER00872.
DR   Proteomes; UP000000640; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046522; F:S-methyl-5-thioribose kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019284; P:L-methionine salvage from S-adenosylmethionine; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01683; Salvage_MtnK; 1.
DR   InterPro; IPR002575; Aminoglycoside_PTrfase.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR009212; Methylthioribose_kinase.
DR   Pfam; PF01636; APH; 1.
DR   PIRSF; PIRSF031134; MTRK; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   TIGRFAMs; TIGR01767; MTRK; 1.
PE   3: Inferred from homology;
DR   PRODOM; A1SDR5.
DR   SWISS-2DPAGE; A1SDR5.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01683};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01683};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000640};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_01683, ECO:0000313|EMBL:ABL79950.1};
KW   Methionine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01683};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01683};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000640};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01683,
KW   ECO:0000313|EMBL:ABL79950.1}.
FT   DOMAIN       35    289       APH. {ECO:0000259|Pfam:PF01636}.
FT   NP_BIND     114    116       ATP. {ECO:0000256|HAMAP-Rule:MF_01683}.
FT   BINDING      44     44       ATP. {ECO:0000256|HAMAP-Rule:MF_01683}.
FT   BINDING      60     60       ATP. {ECO:0000256|HAMAP-Rule:MF_01683}.
FT   BINDING     232    232       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01683}.
FT   BINDING     349    349       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01683}.
SQ   SEQUENCE   409 AA;  44995 MW;  E410790B54DC2D63 CRC64;
     MMSDYEFLTV DTVASYIESR PVLASRVDTV ALASVEEIGD GNLNLVFLVK DRHGRGLCLK
     QALPYVRMTG EAWPMTPDRA RHEVESLRAH HALIPDHVVE VFDYHPERYI IAMEDLSDHR
     VWRGALNEGL RHDGAAEAMG AYVGAVAFGT SAFGLERHAL ADAVSASVNP ALCTITEDLV
     FTEPLVDAGR NSVLPANEKD AAELAADDAM VRAMGRAKWL FMTQAEALIH GDLHTGSVMV
     RAVDGSSRCD SVKAFDSEFA FYGPVAFDLG ALWGNYAIAA ARALALGQDE RAAWALGLVQ
     QTWDGFEGEF RRRWPSRLDA RVWRDDTLQD LLREWENEAW LFAAAKMSRR IVGAAKTADI
     ETLPEELREG AARGVLRAAR TLVRHSTSEN GPRVVAGRVG EVLAEHCTR
//

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