(data stored in ACNUC7421 zone)

HOGENOM: BACAH_2_PE317

ID   BACAH_2_PE317                        STANDARD;      PRT;   348 AA.
AC   BACAH_2_PE317; A0R946;
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 1; Short=M1Pi 1;
DE   Short=MTR-1-P isomerase 1; EC=5.3.1 23;AltName:
DE   Full=S-methyl-5-thioribose-1-phosphate isomerase 1; (BACAH_2.PE317).
GN   Name=mtnA1; OrderedLocusNames=BALH_0338;
OS   BACILLUS THURINGIENSIS STR. AL HAKAM.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus; Bacillus cereus
OC   group.
OX   NCBI_TaxID=412694;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS BACAH_2.PE317.
CC       Bacillus thuringiensis str. Al Hakam chromosome, complete genome.
CC       genome.
CC   -!- ANNOTATIONS ORIGIN:MTNA1_BACAH
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   -!- SEQUENCE CAUTION:
CC       Sequence=ABK83739.1; Type=Erroneous initiation;
CC   -!- GENE_FAMILY: HOG000224730 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; A0R946; -.
DR   EMBL; CP000485; ABK83739.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_893246.1; NC_008600.1.
DR   ProteinModelPortal; A0R946; -.
DR   SMR; A0R946; 7-347.
DR   STRING; A0R946; -.
DR   EnsemblBacteria; EBBACT00000068116; EBBACP00000066353; EBBACG00000068107.
DR   GeneID; 4545300; -.
DR   GenomeReviews; CP000485_GR; BALH_0338.
DR   KEGG; btl:BALH_0338; -.
DR   eggNOG; COG0182; -.
DR   GeneTree; EBGT00050000000839; -.
DR   OMA; RPRNQGA; -.
DR   ProtClustDB; PRK05720; -.
DR   BioCyc; BTHU412694:BALH_0338-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; BACAH_2.PE317; -.
KW   Amino-acid biosynthesis; Complete proteome; Isomerase;
KW   Methionine biosynthesis.
SQ   SEQUENCE   348 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MMEEQLIPIQ WKDDALVLLD QTLLPNEVVY ESFNTAEGVW DAIQVMKVRG APAIGVSAAY
     GVYLGVKEFV ESTEAEFIDE VKRVCAYLAT SRPTAVNLFW ALERMESVAT DHTHLSITQL
     KDRLLEEAKE IHREDEEINR QIGEHALTLF HDGMGVLTHC NAGALATTKY GTATAPMYLA
     KEKGWDLKIY SDETRPRLQG STLTALELQR AGIDVTVITD NMAAMVMSQG KIDAVIVGCD
     RVAANGDVAN KIGTLGVSIL AKYYNIPFYV AAPTPTIDLK TPTGKEIPIE ERDASEVINR
     FGQYSAPKES KVYNPAFDVT PHENVTAIIT EKGIVKAPFT ENLKKLFQ
//

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