(data stored in ACNUC7421 zone)

HOGENOM: CLOBJ_1_PE1313

ID   CLOBJ_1_PE1313                       STANDARD;      PRT;   349 AA.
AC   CLOBJ_1_PE1313; C1FKZ3;
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; (CLOBJ_1.PE1313).
GN   Name=mtnA; OrderedLocusNames=CLM_1427;
OS   CLOSTRIDIUM BOTULINUM A2 STR. KYOTO.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=536232;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CLOBJ_1.PE1313.
CC       Clostridium botulinum A2 str. Kyoto, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:MTNA_CLOBJ
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; C1FKZ3; -.
DR   EMBL; CP001581; ACO86021.1; -; Genomic_DNA.
DR   RefSeq; YP_002803626.1; NC_012563.1.
DR   ProteinModelPortal; C1FKZ3; -.
DR   STRING; C1FKZ3; -.
DR   GeneID; 7767322; -.
DR   GenomeReviews; CP001581_GR; CLM_1427.
DR   KEGG; cby:CLM_1427; -.
DR   OMA; RPRNQGA; -.
DR   ProtClustDB; PRK05720; -.
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; CLOBJ_1.PE1313; -.
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 EDNFENFFKY LKEKSSYLDS SRPTAVNLSW ALKVMESKAL ENKDKDVKEI
     KSILREEAKR IHEEDIEICK AIGENLITLL KDGVGILTHC NAGQLATSKY GTATSPMYLA
     KEKGWNFKVY SDETRPRLQG STLTALELYE AGIDVTTITD NMAAMVMSQG KIDAVIVGCD
     RIAANGDTAN KIGTMGVSIL AKYFGIPMYI AAPTPSIDMN TKTGKDIPIE ERNSEEITSR
     FGVWTAPKGV KVYNPGFDVT PHENITAIVT EKGIVYPPFK ENLKKLFEK
//

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