(data stored in ACNUC7421 zone)

HOGENOM: BACC1_1_PE4064

ID   BACC1_1_PE4064                       STANDARD;      PRT;   351 AA.
AC   BACC1_1_PE4064; Q731R7;
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; (BACC1_1.PE4064).
GN   Name=mtnA; OrderedLocusNames=BCE_4098;
OS   BACILLUS CEREUS ATCC 10987.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus; Bacillus cereus
OC   group.
OX   NCBI_TaxID=222523;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS BACC1_1.PE4064.
CC       Bacillus cereus ATCC 10987, complete genome.
CC       genome.
CC   -!- ANNOTATIONS ORIGIN:MTNA_BACC1
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; Q731R7; -.
DR   EMBL; AE017194; AAS43000.1; -; Genomic_DNA.
DR   RefSeq; NP_980392.1; NC_003909.8.
DR   HSSP; Q06489; 1W2W.
DR   ProteinModelPortal; Q731R7; -.
DR   SMR; Q731R7; 9-348.
DR   STRING; Q731R7; -.
DR   EnsemblBacteria; EBBACT00000025570; EBBACP00000024920; EBBACG00000025561.
DR   GeneID; 2752414; -.
DR   GenomeReviews; AE017194_GR; BCE_4098.
DR   KEGG; bca:BCE_4098; -.
DR   NMPDR; fig|222523.1.peg.4064; -.
DR   TIGR; BCE_4098; -.
DR   eggNOG; COG0182; -.
DR   GeneTree; EBGT00050000000839; -.
DR   OMA; EDGWKVI; -.
DR   ProtClustDB; PRK05720; -.
DR   BioCyc; BCER405917:BCE_4098-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; BACC1_1.PE4064; -.
KW   Amino-acid biosynthesis; Complete proteome; Isomerase;
KW   Methionine biosynthesis.
SQ   SEQUENCE   351 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSTIVTIPRS VSWKGDAIAV LNQTKLPHST EYKTLTTIEE VWKSIVMLEV RGAPAIGIVA
     AFGLALVAKK YTTLHIEEFQ KKFNRDCNYL GTSRPTAVNL FWAIDRMRES IQEITTIKEA
     QKILEEEALL IQQEDEAVCR SIGEHALSCF QDGDNILTIC NAGSIATAKY GTALAPFYIG
     KEKGVHLHAY ACETRPVLQG GRLTTWELKQ AGIDVTLITD NTAAHAIQTK EINAIIVGAD
     RIVANGDTAN KIGTMNLAIL AKYFGIPFYV AAPLSTFDIT KQTGAEIVIE ERDETEVTKI
     FGKQVTPVGT TVYNPAFDVT PNELITGIIT ERGIIRGDYK REIASLFEKT S
//

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