(data stored in ACNUC7421 zone)

HOGENOM: DEHSB_1_PE487

ID   DEHSB_1_PE487                        STANDARD;      PRT;   332 AA.
AC   DEHSB_1_PE487; A5FRU8;
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; (DEHSB_1.PE487).
GN   Name=mtnA; OrderedLocusNames=DehaBAV1_0494;
OS   DEHALOCOCCOIDES SP. BAV1.
OC   Bacteria; Chloroflexi; Dehalococcoidetes; Dehalococcoides.
OX   NCBI_TaxID=216389;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS DEHSB_1.PE487.
CC       Dehalococcoides sp. BAV1, complete genome.
CC       / IFO 0083) chromosome G, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:MTNA_DEHSB
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   -!- 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; A5FRU8; -.
DR   EMBL; CP000688; ABQ17079.1; -; Genomic_DNA.
DR   RefSeq; YP_001213957.1; NC_009455.1.
DR   ProteinModelPortal; A5FRU8; -.
DR   SMR; A5FRU8; 1-330.
DR   STRING; A5FRU8; -.
DR   GeneID; 5131242; -.
DR   GenomeReviews; CP000688_GR; DehaBAV1_0494.
DR   KEGG; deb:DehaBAV1_0494; -.
DR   eggNOG; COG0182; -.
DR   OMA; RPRNQGA; -.
DR   ProtClustDB; CLSK837455; -.
DR   BioCyc; DSP216389:DEHABAV1_0494-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; DEHSB_1.PE487; -.
KW   translation initiation factor 2B subunit I;
KW   Amino-acid biosynthesis; Complete proteome; Isomerase;
KW   Methionine biosynthesis.
SQ   SEQUENCE   332 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MKAIEWRNNR LIILDQTLLP LEEKYLELND YHAVAEAIKT LRVRGAPSIG VAAAYGIAFG
     ALSIETRYCS EFLPLYQQIS AEIASTRPTA KNLFMAVERM DHVVASGTDV LQVKISLVDE
     AVKIHREEEE ASRKISTFGA DLIQPGWTVL THCNAGPLAT AGYGTALGVI IAAHQQNKGI
     SAFATETRPL LQGARLTALE LKEAGVPFKL ITDSMAGHFM KKGVINAVVV GADRIARNGD
     TANKIGTYSL AVLALAHGIP FYVAAPSSTF DKSIESGNDI VIEERKPEEI TYLRGQRIAP
     ENIDVANPAF DVTPANLIAA FITENGIIRR GE
//

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