ID A0A0X8CTX0_9BRAD Unreviewed; 368 AA.
AC A0A0X8CTX0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
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 ORFNames=BCCGELA001_34870 {ECO:0000313|EMBL:AMA60877.1};
OS Bradyrhizobium sp. CCGE-LA001.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1223566 {ECO:0000313|EMBL:AMA60877.1, ECO:0000313|Proteomes:UP000019052};
RN [1] {ECO:0000313|EMBL:AMA60877.1, ECO:0000313|Proteomes:UP000019052}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCGE-LA001 {ECO:0000313|EMBL:AMA60877.1,
RC ECO:0000313|Proteomes:UP000019052};
RX PubMed=24952318; DOI=10.1016/j.ympev.2014.06.006;
RA Servin-Garciduenas L.E., Zayas-Del Moral A., Ormeno-Orrillo E., Rogel M.A.,
RA Delgado-Salinas A., Sanchez F., Martinez-Romero E.;
RT "Symbiont shift towards Rhizobium nodulation in a group of phylogenetically
RT related Phaseolus species.";
RL Mol. Phylogenet. Evol. 79:1-11(2014).
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 -!- SIMILARITY: Belongs to the EIF-2B alpha/beta/delta subunits family.
CC MtnA subfamily. {ECO:0000256|HAMAP-Rule:MF_01678}.
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DR EMBL; CP013949; AMA60877.1; -; Genomic_DNA.
DR RefSeq; WP_008540604.1; NZ_CP013949.1.
DR AlphaFoldDB; A0A0X8CTX0; -.
DR STRING; 1223566.BCCGELA001_34870; -.
DR KEGG; brc:BCCGELA001_34870; -.
DR UniPathway; UPA00904; UER00874.
DR Proteomes; UP000019052; Chromosome.
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:SF1; 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}.
FT ACT_SITE 243
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT BINDING 53..55
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT BINDING 202
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT BINDING 253..254
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT SITE 163
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
SQ SEQUENCE 368 AA; 39805 MW; B36860C84C063D64 CRC64;
MKVDGKHFRS IWRERDGWSV GAIDQRRLPH EFIVAKLTSC EDAAVAIRDM LVRGAPLIGA
TAAYGMALAM REDASDAGLK RAYERLVVAR PTAINLKWAL DEMRATLAPI DPAERAEAAY
ARADEIAEQD VEINRGIADN GLKLIEAVAA KKPGETVNVL THCNAGWLAT VDWGTATAPI
YLAHERGIKI HVWVDETRPR NQGASLTAWE LGHHGVPHTV IPDNTGGHLM QHGMVDLAIV
GTDRVAANGD VCNKIGTYLK ALAAHDNHVP FYVALPSPTI DFAVHDGIRD IPIEQRSGTE
VTDMTGRTAD GRLETVRIVP ENSPVANYAF DVTPARLVTG LITERGVLKP DRAALAAAFP
ERIAAAAE
//
