(data stored in ACNUC7421 zone)

HOGENOM: CLOBL_1_PE1248

ID   CLOBL_1_PE1248                       STANDARD;      PRT;   349 AA.
AC   CLOBL_1_PE1248; A7GCV8;
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; (CLOBL_1.PE1248).
GN   Name=mtnA; OrderedLocusNames=CLI_1353;
OS   CLOSTRIDIUM BOTULINUM F STR. LANGELAND.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=441772;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CLOBL_1.PE1248.
CC       Clostridium botulinum F str. Langeland, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:MTNA_CLOBL
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; A7GCV8; -.
DR   EMBL; CP000728; ABS42520.1; -; Genomic_DNA.
DR   RefSeq; YP_001390618.1; NC_009699.1.
DR   ProteinModelPortal; A7GCV8; -.
DR   SMR; A7GCV8; 3-348.
DR   STRING; A7GCV8; -.
DR   GeneID; 5403822; -.
DR   GenomeReviews; CP000728_GR; CLI_1353.
DR   KEGG; cbf:CLI_1353; -.
DR   eggNOG; COG0182; -.
DR   OMA; RPRNQGA; -.
DR   ProtClustDB; PRK05720; -.
DR   BioCyc; CBOT441772:CLI_1353-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; CLOBL_1.PE1248; -.
KW   Amino-acid biosynthesis; Complete proteome; Isomerase;
KW   Methionine biosynthesis.
SQ   SEQUENCE   349 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MAELLAIKWD DNRDKLILLD QTILPNKIEY IEYDTAEGVY DSIKDMIVRG APAIGVTAAY
     GLYFAAKVAP EDKFEGFFKY LKEKSAYLDS SRPTAVNLSW ALKVMESKAL ENKDKDVKEI
     KSILREEAKR IHEEDIEICK TIGENLITLL KDGVGILTHC NAGQLATSKY GTATSPMYLA
     KEKGWNFKVY SDETRPRLQG STLTALELYE AGIDVTTITD NMAAMVMSQG KIDAVIVGCD
     RIAANGDTAN KIGTMGVSIL AKYFGIPMYI AAPTPSIDIN TKTGEDIPIE ERNSEEVTSR
     FGVWTAPKGV KVYNPGFDVT PHENITAIVT EKGIVYPPFK ENLKKLFEK
//

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