(data stored in ACNUC7421 zone)

HOGENOM: BACAH_2_PE3459

ID   BACAH_2_PE3459                       STANDARD;      PRT;   351 AA.
AC   BACAH_2_PE3459; A0RI38;
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 2; Short=M1Pi 2;
DE   Short=MTR-1-P isomerase 2; EC=5.3.1 23;AltName:
DE   Full=S-methyl-5-thioribose-1-phosphate isomerase 2; (BACAH_2.PE3459).
GN   Name=mtnA2; OrderedLocusNames=BALH_3649;
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.PE3459.
CC       Bacillus thuringiensis str. Al Hakam chromosome, complete genome.
CC       genome.
CC   -!- ANNOTATIONS ORIGIN:MTNA2_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   -!- GENE_FAMILY: HOG000224730 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; A0RI38; -.
DR   EMBL; CP000485; ABK86881.1; -; Genomic_DNA.
DR   RefSeq; YP_896388.1; NC_008600.1.
DR   ProteinModelPortal; A0RI38; -.
DR   SMR; A0RI38; 1-348.
DR   STRING; A0RI38; -.
DR   EnsemblBacteria; EBBACT00000071110; EBBACP00000069347; EBBACG00000071101.
DR   GeneID; 4544742; -.
DR   GenomeReviews; CP000485_GR; BALH_3649.
DR   KEGG; btl:BALH_3649; -.
DR   NMPDR; fig|412694.5.peg.3511; -.
DR   eggNOG; COG0182; -.
DR   GeneTree; EBGT00050000000839; -.
DR   OMA; EDGWKVI; -.
DR   ProtClustDB; PRK05720; -.
DR   BioCyc; BTHU412694:BALH_3649-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.PE3459; -.
KW   Amino-acid biosynthesis; Complete proteome; Isomerase;
KW   Methionine biosynthesis.
SQ   SEQUENCE   351 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSTVVTIPRS VSWKGDAIAV LKQTKLPHST EYKTLTTIEE VWKSIVMLEV RGAPAIGIVA
     AFGLALASKK YTTLHIEEFQ KKFNRDCNYL GTSRPTAVNL FWAIDRMRES IQEITTIKEA
     QKILEEEALR IQQEDEAVCR SIGEHALTCF KDGDNILTIC NAGSIATARY GTALAPFYIG
     KEKGVRLHAY ACETRPVLQG GRLTTWELKQ AGIDVTLITD NTAAHAIQTK EINAIIVGAD
     RIVANGDTAN KIGTMNLAIL AKYFDIPFYV AAPLSTFDIT KQTGAEIVIE ERDETEVTKI
     FGKQVAPVGT TVYNPAFDVT PNKLITGIIT EKGIICGDYK REIASLFEKT S
//

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