(data stored in ACNUC7421 zone)

HOGENOM: DESHD_1_PE3711

ID   DESHD_1_PE3711                       STANDARD;      PRT;   345 AA.
AC   DESHD_1_PE3711; B8FRM1;
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; (DESHD_1.PE3711).
GN   Name=mtnA; OrderedLocusNames=Dhaf_3765;
OS   DESULFITOBACTERIUM HAFNIENSE DCB-2.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfitobacterium.
OX   NCBI_TaxID=272564;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS DESHD_1.PE3711.
CC       Desulfitobacterium hafniense DCB-2, complete genome.
CC       complete genome.
CC   -!- ANNOTATIONS ORIGIN:MTNA_DESHD
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; B8FRM1; -.
DR   EMBL; CP001336; ACL21781.1; -; Genomic_DNA.
DR   RefSeq; YP_002460217.1; NC_011830.1.
DR   ProteinModelPortal; B8FRM1; -.
DR   STRING; B8FRM1; -.
DR   GeneID; 7260786; -.
DR   GenomeReviews; CP001336_GR; Dhaf_3765.
DR   KEGG; dhd:Dhaf_3765; -.
DR   OMA; RPRNQGA; -.
DR   ProtClustDB; CLSK2466347; -.
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; DESHD_1.PE3711; -.
KW   Amino-acid biosynthesis; Complete proteome; Isomerase;
KW   Methionine biosynthesis.
SQ   SEQUENCE   345 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MKALEWMGDS LKILDQTRLP VEIKYRMAAT YEEVAEAIEK MEVRGAPAIG AAAAYGYALG
     AIGYSGELAD LPAHMEKVQH RLAETRPTAV NLFWALRRME DRLRDQHEAK ELAEIRQALV
     AEAENIAEDD RRVNRLIGEH GNAIVTAEAN ILTHCNAGAL ATVEYGTALG VIRAAQQAGK
     KVHVYAGETR PFLQGARLTA LELMNDHIPV TLIADNMAGF LMQQGNIDLV IVGADRIAAN
     GDTANKIGTY SLAVLAHAHG IPFYVAAPTS TIDLKVPSGQ DIPIEERNPK ELREVFGVQV
     APPEVPVYNP AFDVTPAKLI TGIITEKGIV TSPYSVNLLK MMVRS
//

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