(data stored in ACNUC7421 zone)

HOGENOM: BACCN_2_PE2588

ID   BACCN_2_PE2588                       STANDARD;      PRT;   349 AA.
AC   BACCN_2_PE2588; A7GS56;
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; (BACCN_2.PE2588).
GN   Name=mtnA; OrderedLocusNames=Bcer98_2731;
OS   BACILLUS CYTOTOXICUS NVH 391-98.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus; Bacillus cereus
OC   group.
OX   NCBI_TaxID=315749;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS BACCN_2.PE2588.
CC       Bacillus cereus subsp. cytotoxis NVH 391-98, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:MTNA_BACCN
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; A7GS56; -.
DR   EMBL; CP000764; ABS22964.1; -; Genomic_DNA.
DR   RefSeq; YP_001375959.1; NC_009674.1.
DR   ProteinModelPortal; A7GS56; -.
DR   SMR; A7GS56; 1-348.
DR   STRING; A7GS56; -.
DR   EnsemblBacteria; EBBACT00000038752; EBBACP00000037803; EBBACG00000038743.
DR   GeneID; 5345762; -.
DR   GenomeReviews; CP000764_GR; Bcer98_2731.
DR   KEGG; bcy:Bcer98_2731; -.
DR   eggNOG; COG0182; -.
DR   GeneTree; EBGT00050000000839; -.
DR   OMA; EDGWKVI; -.
DR   ProtClustDB; PRK05720; -.
DR   BioCyc; BCER315749:BCER98_2731-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; BACCN_2.PE2588; -.
KW   Amino-acid biosynthesis; Complete proteome; Isomerase;
KW   Methionine biosynthesis.
SQ   SEQUENCE   349 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MNTTVAVPRA IIWKGDSITI LNQTKLPHVA EYKTLTSIED VWKSIVMLEV RGAPAIGIAA
     AFGLALAAQK YEAINIVEFK TKFNRDCNYL GTSRPTAVNL FWAIDRMRAA IEEVSTIKIA
     REILEEEALQ IQQEDEQVCR SLGEHALTCF QDGDRILTIC NAGSIATARY GTALAPFYIG
     KEKGIHLHAY ACETRPVLQG ARLTTWELRE AGVDVTLITD NMAAHTIRTK NISAIIVGAD
     RIVANGDTAN KVGTLNLAIL AKHYQIPFYV AAPLSTFDTK KKTGNEIIIE ERDETEVTKI
     NGQQIAPAGI HIYNPAFDIT PHEFISGIIT EKGILQGDYT KEIASLFEK
//

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