(data stored in ACNUC7421 zone)

HOGENOM: BASUB1_1_PE1378

ID   BASUB1_1_PE1378                      STANDARD;      PRT;   353 AA.
AC   BASUB1_1_PE1378; O31662;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Methylthioribose-1-phosphate isomerase; Short=M1Pi;
DE   Short=MTR-1-P isomerase; EC=5.3.1 23;AltName:
DE   Full=S-methyl-5-thioribose-1-phosphate isomerase; (BASUB1_1.PE1378).
GN   Name=mtnA; Synonyms=ykrS; OrderedLocusNames=BSU13550;
OS   BACILLUS SUBTILIS SUBSP. SUBTILIS STR. 168.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS BASUB1_1.PE1378.
CC       Bacillus subtilis subsp. subtilis str. 168 chromosome, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:MTNA_BACSU
CC   -!- FUNCTION: Catalyzes the interconversion of methylthioribose-1-
CC       phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-
CC       P).
CC   -!- CATALYTIC ACTIVITY: S-methyl-5-thio-alpha-D-ribose 1-phosphate =
CC       S-methyl-5-thio-D-ribulose 1-phosphate.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=138 uM for methylthioribose-1-phosphate (at pH 8.5 and 35
CC         degrees Celsius);
CC         Vmax=20.4 umol/min/mg enzyme (at pH 8.5 and 35 degrees Celsius);
CC       pH dependence:
CC         Optimum pH is 8.1;
CC       Temperature dependence:
CC         Optimum temperature is 35 degrees Celsius;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via
CC       salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose
CC       1-phosphate: step 1/6.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits
CC       family. MtnA subfamily.
CC   -!- CAUTION: Was originally thought to be a translation initiation
CC       factor.
CC   -!- GENE_FAMILY: HOG000224730 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; O31662; -.
DR   EMBL; AL009126; CAB13228.1; -; Genomic_DNA.
DR   PIR; C69863; C69863.
DR   RefSeq; NP_389238.1; NC_000964.3.
DR   PDB; 2YRF; X-ray; 2.70 A; A/B=1-353.
DR   PDB; 2YVK; X-ray; 2.40 A; A/B/C/D=1-353.
DR   PDBsum; 2YRF; -.
DR   PDBsum; 2YVK; -.
DR   ProteinModelPortal; O31662; -.
DR   SMR; O31662; 1-349.
DR   EnsemblBacteria; EBBACT00000001624; EBBACP00000001624; EBBACG00000001622.
DR   GeneID; 939341; -.
DR   GenomeReviews; AL009126_GR; BSU13550.
DR   KEGG; bsu:BSU13550; -.
DR   NMPDR; fig|224308.1.peg.1357; -.
DR   GenoList; BSU13550; -.
DR   GeneTree; EBGT00050000000839; -.
DR   OMA; EDGWKVI; -.
DR   PhylomeDB; O31662; -.
DR   ProtClustDB; PRK05720; -.
DR   BioCyc; BSUB:BSU13550-MON; -.
DR   GO; GO:0046523; F:S-methyl-5-thioribose-1-phosphate isomerase activity; IEA:EC.
DR   GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR   HAMAP; MF_01678; Salvage_MtnA; 1; -.
DR   InterPro; IPR000649; IF-2B-related.
DR   InterPro; IPR005251; IF-2BI_MTNA.
DR   InterPro; IPR011559; Initiation_fac_2B_a/b/d.
DR   PANTHER; PTHR10233; IF-2B_related; 1.
DR   Pfam; PF01008; IF-2B; 1.
DR   TIGRFAMs; TIGR00524; EIF-2B_rel; 1.
DR   TIGRFAMs; TIGR00512; Salvage_mtnA; 1.
DR   HOGENOMDNA; BASUB1_1.PE1378; -.
KW   3D-structure; Amino-acid biosynthesis; Complete proteome; Isomerase;
KW   Methionine biosynthesis; Reference proteome.
SQ   SEQUENCE   353 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTHSFAVPRS VEWKETAITI LNQQKLPDET EYLELTTKED VFDAIVTLKV RGAPAIGITA
     AFGLALAAKD IETDNVTEFR RRLEDIKQYL NSSRPTAINL SWALERLSHS VENAISVNEA
     KTNLVHEAIQ IQVEDEETCR LIGQNALQLF KKGDRIMTIC NAGSIATSRY GTALAPFYLA
     KQKDLGLHIY ACETRPVLQG SRLTAWELMQ GGIDVTLITD SMAAHTMKEK QISAVIVGAD
     RIAKNGDTAN KIGTYGLAIL ANAFDIPFFV AAPLSTFDTK VKCGADIPIE ERDPEEVRQI
     SGVRTAPSNV PVFNPAFDIT PHDLISGIIT EKGIMTGNYE EEIEQLFKGE KVH
//

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