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Database: UniProt
Entry: A0A0M2PRC1_9BACI
LinkDB: A0A0M2PRC1_9BACI
Original site: A0A0M2PRC1_9BACI 
ID   A0A0M2PRC1_9BACI        Unreviewed;       350 AA.
AC   A0A0M2PRC1;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Methylthioribose-1-phosphate isomerase {ECO:0000256|HAMAP-Rule:MF_01678};
DE            Short=M1Pi {ECO:0000256|HAMAP-Rule:MF_01678};
DE            Short=MTR-1-P isomerase {ECO:0000256|HAMAP-Rule:MF_01678};
DE            EC=5.3.1.23 {ECO:0000256|HAMAP-Rule:MF_01678};
DE   AltName: Full=S-methyl-5-thioribose-1-phosphate isomerase {ECO:0000256|HAMAP-Rule:MF_01678};
GN   Name=mtnA {ECO:0000256|HAMAP-Rule:MF_01678,
GN   ECO:0000313|EMBL:KKI93932.1};
GN   ORFNames=WQ54_02495 {ECO:0000313|EMBL:KKI93932.1};
OS   Bacillus sp. SA1-12.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1455638 {ECO:0000313|EMBL:KKI93932.1, ECO:0000313|Proteomes:UP000034887};
RN   [1] {ECO:0000313|EMBL:KKI93932.1, ECO:0000313|Proteomes:UP000034887}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SA1-12 {ECO:0000313|EMBL:KKI93932.1,
RC   ECO:0000313|Proteomes:UP000034887};
RA   Kumar A., Mathan Kumar R., Kaur N., Kumar N., Singh N.K., Kaur G.,
RA   Mayilraj S.;
RT   "Taxonomic description and genome sequence of Bacillus tuticoriensis sp.
RT   nov., a novel member of the genus Bacillus isolated from solar saltern.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the interconversion of methylthioribose-1-phosphate
CC       (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
CC       {ECO:0000256|HAMAP-Rule:MF_01678}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-
CC         D-ribulose 1-phosphate; Xref=Rhea:RHEA:19989, ChEBI:CHEBI:58533,
CC         ChEBI:CHEBI:58548; EC=5.3.1.23; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01678};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via salvage
CC       pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate:
CC       step 1/6. {ECO:0000256|HAMAP-Rule:MF_01678}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC       Rule:MF_01678}.
CC   -!- SIMILARITY: Belongs to the EIF-2B alpha/beta/delta subunits family.
CC       MtnA subfamily. {ECO:0000256|HAMAP-Rule:MF_01678}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKI93932.1}.
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DR   EMBL; LATZ01000002; KKI93932.1; -; Genomic_DNA.
DR   RefSeq; WP_046511594.1; NZ_LATZ01000002.1.
DR   AlphaFoldDB; A0A0M2PRC1; -.
DR   PATRIC; fig|1455638.3.peg.541; -.
DR   OrthoDB; 9803436at2; -.
DR   UniPathway; UPA00904; UER00874.
DR   Proteomes; UP000034887; Unassembled WGS sequence.
DR   GO; GO:0046523; F:S-methyl-5-thioribose-1-phosphate isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019284; P:L-methionine salvage from S-adenosylmethionine; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.120.420; translation initiation factor eif-2b, domain 1; 1.
DR   HAMAP; MF_01678; Salvage_MtnA; 1.
DR   InterPro; IPR000649; IF-2B-related.
DR   InterPro; IPR005251; IF-M1Pi.
DR   InterPro; IPR042529; IF_2B-like_C.
DR   InterPro; IPR011559; Initiation_fac_2B_a/b/d.
DR   InterPro; IPR027363; M1Pi_N.
DR   InterPro; IPR037171; NagB/RpiA_transferase-like.
DR   NCBIfam; TIGR00524; eIF-2B_rel; 1.
DR   NCBIfam; TIGR00512; salvage_mtnA; 1.
DR   PANTHER; PTHR43475; METHYLTHIORIBOSE-1-PHOSPHATE ISOMERASE; 1.
DR   PANTHER; PTHR43475:SF4; METHYLTHIORIBOSE-1-PHOSPHATE ISOMERASE; 1.
DR   Pfam; PF01008; IF-2B; 1.
DR   SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01678};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01678};
KW   Methionine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01678};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034887}.
FT   ACT_SITE        241
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT   BINDING         52..54
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT   BINDING         95
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT   BINDING         200
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT   BINDING         251..252
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT   SITE            161
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
SQ   SEQUENCE   350 AA;  38254 MW;  272414A3E6541318 CRC64;
     MAIKEFTIPR SVIWKDSSIS LLNQQKIPHV TEYLELTTVD EVWDAIQTLK VRGAPAIGIT
     AAYGLALAAL QDSSKTIEEF QAAIKKKRDY LASSRPTAVN LFWALDRLVA TVANVKSINE
     AKTRIVHEAI QIQIEDEEVC RLIGEHALSV FNNGDRIMTI CNAGSIATAK YGTALAPFYL
     AKEQNKELKV FACETRPVLQ GSRLTTWELM QAGVDVTLIT DNMAAHTIKS KNITAIIVGA
     DRIAANGDTA NKIGTFNLAL LAKAFNIPFY VAAPLSTFDP SIANGEQIPI EERNPKEVTE
     LNGVQIAPEG VNVFNPAFDV TPNELIAGII TEKGILEGNY QEEILQLFNS
//
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