ID A0A1I4NW18_9BACL Unreviewed; 363 AA.
AC A0A1I4NW18;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=SAMN03159341_1209 {ECO:0000313|EMBL:SFM19510.1};
OS Paenibacillus sp. 1_12.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1566278 {ECO:0000313|EMBL:SFM19510.1, ECO:0000313|Proteomes:UP000198699};
RN [1] {ECO:0000313|EMBL:SFM19510.1, ECO:0000313|Proteomes:UP000198699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1_12 {ECO:0000313|EMBL:SFM19510.1,
RC ECO:0000313|Proteomes:UP000198699};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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 -!- 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; FOTE01000020; SFM19510.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4NW18; -.
DR STRING; 1566278.SAMN03159341_1209; -.
DR OrthoDB; 9803436at2; -.
DR UniPathway; UPA00904; UER00874.
DR Proteomes; UP000198699; 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}.
FT ACT_SITE 254
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT BINDING 62..64
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT BINDING 104
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT BINDING 213
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT BINDING 264..265
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT SITE 174
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
SQ SEQUENCE 363 AA; 39432 MW; 64109CF2377B59E1 CRC64;
MSVNEKQEEK NEAADWLQSV RWNSATQSLD LLDQRLLPDE IVYLELTTAE QVWDAIKQLA
VRGAPAIGIA AAYGVYLGMR GTSGGLEHLL AETAKQCDYL ATSRPTAVNL FWALERMKQR
ATELASAGGE PEAMKQALLD EAKLIQSEDE ETCRLIGVHA LDLFEDGMGV LTHCNAGGLA
TARYGTALAP MYLAQERGMN LKVFADETRP VLQGARLTAF ELQQAGVDVT LICDNMAGVV
MSKGWVQAVI VGTDRVAANG DVANKIGTYS VAVLAKAHGI PFYVACPMST IDLNTANGAD
IPIEERHEDE ITQGFGKRTA PKGVKVFNPA FDITPNEYVT AIITEKGVIR APYQENLKKL
FQE
//
