(data stored in ACNUC7421 zone)

HOGENOM: BACA2_1_PE1248

ID   BACA2_1_PE1248                       STANDARD;      PRT;   353 AA.
AC   BACA2_1_PE1248; A7Z3X0;
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; (BACA2_1.PE1248).
GN   Name=mtnA; OrderedLocusNames=RBAM_013330;
OS   BACILLUS AMYLOLIQUEFACIENS FZB42.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=326423;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS BACA2_1.PE1248.
CC       Bacillus amyloliquefaciens FZB42, complete genome.
CC       genome.
CC   -!- ANNOTATIONS ORIGIN:MTNA_BACA2
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   -!- SUBUNIT: Homodimer.
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; A7Z3X0; -.
DR   EMBL; CP000560; ABS73696.1; -; Genomic_DNA.
DR   RefSeq; YP_001420927.1; NC_009725.1.
DR   ProteinModelPortal; A7Z3X0; -.
DR   SMR; A7Z3X0; 1-347.
DR   STRING; A7Z3X0; -.
DR   EnsemblBacteria; EBBACT00000004712; EBBACP00000004590; EBBACG00000004704.
DR   GeneID; 5462386; -.
DR   GenomeReviews; CP000560_GR; RBAM_013330.
DR   KEGG; bay:RBAM_013330; -.
DR   eggNOG; COG0182; -.
DR   GeneTree; EBGT00050000000839; -.
DR   OMA; EDGWKVI; -.
DR   ProtClustDB; PRK05720; -.
DR   BioCyc; BAMY326423:RBAM_013330-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; BACA2_1.PE1248; -.
KW   Amino-acid biosynthesis; Complete proteome; Isomerase;
KW   Methionine biosynthesis.
SQ   SEQUENCE   353 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTNEFAIPRS VEWKETYIRI LNQQKLPDVT EYVELETKED VFDAIVTLKV RGAPAIGITA
     AFGLALSAKS FEARDLSDFR RQFADVKTYL NSSRPTAVNL AWALDRLTDS IRDAISINEA
     KTTLVHEAIQ IQIEDEETCR MIGQNALHLF KKGDQIMTIC NAGSIATSRY GTALAPFYLA
     KQKDLGLHIY ACETRPVLQG SRLTAWELMQ GGIDVTLITD SMAAHTMKEK HISAVIVGAD
     RIAKNGDTAN KIGTYGLAIL ANAFQIPFFV AAPLSTFDLQ IENGDQIPIE ERDPDEVRQI
     SGIRTAPEDV PVFNPAFDIT PGSLISGIIT EKGIVTGSYT EEIEQLFADC QLS
//

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