ID G8UC78_BACCE Unreviewed; 351 AA.
AC G8UC78;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 03-APR-2013, entry version 12.
DE RecName: Full=Methylthioribose-1-phosphate isomerase;
DE Short=M1Pi;
DE Short=MTR-1-P isomerase;
DE EC=5.3.1.23;
DE AltName: Full=S-methyl-5-thioribose-1-phosphate isomerase;
GN Name=mtnA; ORFNames=bcf_20055;
OS Bacillus cereus F837/76.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=347495;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=F837/76;
RX PubMed=22374959; DOI=10.1128/JB.06719-11;
RA Auger S., Galleron N., Segurens B., Dossat C., Bolotin A., Wincker P.,
RA Sorokin A.;
RT "Complete Genome Sequence of the Highly Hemolytic Strain Bacillus
RT cereus F837/76.";
RL J. Bacteriol. 194:1630-1630(2012).
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 (By similarity).
CC -!- SIMILARITY: Belongs to the EIF-2B alpha/beta/delta subunits
CC family. MtnA subfamily.
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DR EMBL; CP003187; AEW57132.1; -; Genomic_DNA.
DR RefSeq; YP_005120645.1; NC_016779.1.
DR EnsemblBacteria; AEW57132; AEW57132; bcf_20055.
DR GeneID; 11679704; -.
DR KEGG; bcf:bcf_20055; -.
DR KO; K08963; -.
DR UniPathway; UPA00904; UER00874.
DR GO; GO:0046523; F:S-methyl-5-thioribose-1-phosphate isomerase activity; IEA:HAMAP.
DR GO; GO:0019284; P:L-methionine biosynthetic process from S-adenosylmethionine; IEA:HAMAP.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniPathway.
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; PTHR10233; 1.
DR PANTHER; PTHR10233:SF6; PTHR10233:SF6; 1.
DR Pfam; PF01008; IF-2B; 1.
DR TIGRFAMs; TIGR00524; eIF-2B_rel; 1.
DR TIGRFAMs; TIGR00512; salvage_mtnA; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Isomerase; Methionine biosynthesis.
FT REGION 51 53 Substrate binding (By similarity).
FT REGION 250 251 Substrate binding (By similarity).
FT ACT_SITE 240 240 Proton donor (By similarity).
FT BINDING 94 94 Substrate (By similarity).
FT BINDING 199 199 Substrate (By similarity).
FT SITE 160 160 Transition state stabilizer (By
FT similarity).
SQ SEQUENCE 351 AA; 38634 MW; DB8F19D48AC7481D CRC64;
MSTVVTIPRS VSWKGDAIAV LKQTKLPHST EYKTLTTIEE VWKSIVMLEV RGAPAIGIVA
AFGLALASKK YTTLYIEEFQ KKFNRDCNYL GTSRPTAVNL FWAIDRMRES IQEITTIKEA
QKILEEEALR IQQEDEAVCR SIGEHALTCF KDGDNILTIC NAGSIATARY GTALAPFYIG
KEKGVRLHAY ACETRPVLQG GRLTTWELKQ AGIDVTLITD NTAAHAIQTK EINAIIVGAD
RIVANGDTAN KIGTMNLAIL AKYFDIPFYV AAPLSTFDIT KQTGAEIVIE ERDETEVTKI
FGKQVAPVGT TVYNPAFDVT PNKLITGIIT EKGIICGDYK REIASLFEKT S
//
