(data stored in ACNUC7421 zone)

HOGENOM: LEPBA_1_PE2757

ID   LEPBA_1_PE2757                       STANDARD;      PRT;   357 AA.
AC   LEPBA_1_PE2757; B0SFD6;
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; (LEPBA_1.PE2757).
GN   Name=mtnA; OrderedLocusNames=LBF_2827;
OS   LEPTOSPIRA BIFLEXA SEROVAR PATOC STRAIN 'PATOC 1 (AMES)'.
OC   Bacteria; Spirochaetes; Spirochaetales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=355278;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS LEPBA_1.PE2757.
CC       Leptospira biflexa serovar Patoc strain 'Patoc 1 (Ames)' chromosome
CC       chromosome I, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:MTNA_LEPBA
CC   -!- FUNCTION: Catalyzes the interconversion of methylthioribose-1-
CC       phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P)
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: S-methyl-5-thio-alpha-D-ribose 1-phosphate =
CC       S-methyl-5-thio-D-ribulose 1-phosphate.
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   -!- SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits
CC       family. MtnA subfamily.
CC   -!- GENE_FAMILY: HOG000224730 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; B0SFD6; -.
DR   EMBL; CP000777; ABZ95304.1; -; Genomic_DNA.
DR   RefSeq; YP_001963882.1; NC_010842.1.
DR   ProteinModelPortal; B0SFD6; -.
DR   STRING; B0SFD6; -.
DR   GeneID; 6389045; -.
DR   GenomeReviews; CP000777_GR; LBF_2827.
DR   KEGG; lbf:LBF_2827; -.
DR   OMA; RPRNQGA; -.
DR   ProtClustDB; CLSK574624; -.
DR   BioCyc; LBIF355278:LBF_2827-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; LEPBA_1.PE2757; -.
KW   translation initiation factor 2B;
KW   Amino-acid biosynthesis; Complete proteome; Isomerase;
KW   Methionine biosynthesis.
SQ   SEQUENCE   357 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSQPEFLPIQ WKSTFLSLLD QRVLPGKKEF LQIQTMEETI VAIREMAVRG APAIAITGIF
     GITLGAKKKS GNSNPVDVDS LIKQVFESRP TAVNLSFALK EAKKRVEGVS HWDSIAKVWE
     SYALEMMVQD LKANQTLGKN GADLFPKNQN EFHIITHCNT GALATAGHGT ALGVIRSLRD
     QGKKVVVYAD ETRPFLQGSR LTAFEMMEEG IECYIITDGM SGWLMNHRKI DAVLVGCDRV
     ATNGDTANKI GTYNLAIVAY EHKVPFYVCA TKDSFDLKLK TGDEIPIEMR KESEVTQFDF
     LKNEEGNFLF PEGKTSPIGA RALNPSFDIT KAKFIKNFIT ELGCFVPEEI SFRLKNV
//

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