(data stored in ACNUC7421 zone)

HOGENOM: BATHU1_1_PE3733

ID   BATHU1_1_PE3733                      STANDARD;      PRT;   351 AA.
AC   BATHU1_1_PE3733; Q6HED3;
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; (BATHU1_1.PE3733).
GN   Name=mtnA2; OrderedLocusNames=BT9727_3774;
OS   BACILLUS THURINGIENSIS SEROVAR KONKUKIAN STR. 97-27.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus; Bacillus cereus
OC   group.
OX   NCBI_TaxID=281309;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS BATHU1_1.PE3733.
CC       Bacillus thuringiensis serovar konkukian str. 97-27 chromosome, complet
CC       genome.
CC   -!- ANNOTATIONS ORIGIN:MTNA2_BACHK
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; Q6HED3; -.
DR   EMBL; AE017355; AAT60702.1; -; Genomic_DNA.
DR   RefSeq; YP_038093.1; NC_005957.1.
DR   HSSP; Q06489; 1W2W.
DR   ProteinModelPortal; Q6HED3; -.
DR   SMR; Q6HED3; 1-348.
DR   EnsemblBacteria; EBBACT00000072285; EBBACP00000070371; EBBACG00000072276.
DR   GeneID; 2857485; -.
DR   GenomeReviews; AE017355_GR; BT9727_3774.
DR   KEGG; btk:BT9727_3774; -.
DR   NMPDR; fig|281309.1.peg.3733; -.
DR   GeneTree; EBGT00050000000839; -.
DR   OMA; EDGWKVI; -.
DR   ProtClustDB; PRK05720; -.
DR   BioCyc; BTHU281309:BT9727_3774-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; BATHU1_1.PE3733; -.
KW   Amino-acid biosynthesis; Complete proteome; Isomerase;
KW   Methionine biosynthesis.
SQ   SEQUENCE   351 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSTVVTIPRS VSWKGDAIAV LNQTKLPHST 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 REIVSLFEKT S
//

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