(data stored in ACNUC7421 zone)

HOGENOM: BACLD_1_PE1423

ID   BACLD_1_PE1423                       STANDARD;      PRT;   353 AA.
AC   BACLD_1_PE1423; Q65KK2; Q62W00;
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; (BACLD_1.PE1423).
GN   Name=mtnA; Synonyms=mtnS, ykrS; OrderedLocusNames=BLi01511, BL03632;
OS   BACILLUS LICHENIFORMIS ATCC 14580.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=279010;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS BACLD_1.PE1423.
CC       Bacillus licheniformis ATCC 14580, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:MTNA_BACLD
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; Q65KK2; Q62W00; -.
DR   EMBL; CP000002; AAU23058.1; -; Genomic_DNA.
DR   EMBL; AE017333; AAU40412.1; -; Genomic_DNA.
DR   RefSeq; YP_078696.1; NC_006270.3.
DR   RefSeq; YP_091105.1; NC_006322.1.
DR   HSSP; Q06489; 1W2W.
DR   ProteinModelPortal; Q65KK2; -.
DR   SMR; Q65KK2; 1-347.
DR   STRING; Q65KK2; -.
DR   EnsemblBacteria; EBBACT00000055214; EBBACP00000053745; EBBACG00000055205.
DR   EnsemblBacteria; EBBACT00000060955; EBBACP00000059388; EBBACG00000060946.
DR   GeneID; 3030591; -.
DR   GeneID; 3099817; -.
DR   GenomeReviews; AE017333_GR; BLi01511.
DR   GenomeReviews; CP000002_GR; BL03632.
DR   KEGG; bld:BLi01511; -.
DR   KEGG; bli:BL03632; -.
DR   NMPDR; fig|279010.5.peg.1063; -.
DR   eggNOG; COG0182; -.
DR   GeneTree; EBGT00050000000839; -.
DR   OMA; EDGWKVI; -.
DR   ProtClustDB; PRK05720; -.
DR   BioCyc; BLIC279010-1:BLI01511-MON; -.
DR   BioCyc; BLIC279010:BL03632-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; BACLD_1.PE1423; -.
KW   methylthioribose-1-phosphate isomerase;
KW   Amino-acid biosynthesis; Complete proteome; Isomerase;
KW   Methionine biosynthesis.
SQ   SEQUENCE   353 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MPEQFAVPRS VEWEETSVKI LNQQKLPEKT EYLHLTTKED IYDAIQTLKV RGAPAIGITA
     AFGLALCAQS IDTSDVSAFL RELRKIKDEL NQARPTAVNL SWALNRLLKS AEGAKSVNEA
     KTNLVHEAIQ IQVEDEETCR QIGQNALHLF KSGDSIMTIC NAGSIATSRY GTALSPFYLA
     KTKDLDLHIY ACETRPVLQG ARLTAWELMQ GGIDVTLITD SMAAHTMKEK NISAVIVGAD
     RIARNGDTAN KIGTFGLAIL AKAFQIPFFI AAPLSTFDVS ISCGDDIPIE ERDPDEVRRI
     NGTQIAPQEV PVFNPAFDIT PHDLISGIIT EKGIITDRFE EEIEALFSAE ALT
//

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