ID A0A176L2I7_9ACTN Unreviewed; 379 AA.
AC A0A176L2I7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=A6P39_20645 {ECO:0000313|EMBL:OAA98762.1};
OS Streptomyces sp. FXJ1.172.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=710705 {ECO:0000313|EMBL:OAA98762.1};
RN [1] {ECO:0000313|EMBL:OAA98762.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FXJ1.172 {ECO:0000313|EMBL:OAA98762.1};
RA Liu M., Liu N., Shang F., Huang Y.;
RT "Activation and identification of NC-1, a novel cryptic cyclodepsipeptide
RT from red soil-derived Streptomyces sp. FXJ1.172.";
RL Submitted (APR-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}.
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:OAA98762.1}.
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DR EMBL; LWRP01000104; OAA98762.1; -; Genomic_DNA.
DR RefSeq; WP_067048029.1; NZ_CP119133.1.
DR AlphaFoldDB; A0A176L2I7; -.
DR STRING; 710705.A6P39_20645; -.
DR OrthoDB; 9803436at2; -.
DR UniPathway; UPA00904; UER00874.
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 253
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT BINDING 64..66
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT BINDING 212
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT BINDING 263..264
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT SITE 173
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
SQ SEQUENCE 379 AA; 38899 MW; EF0C5C422D9C9DF8 CRC64;
MADQQARTDG DKRPTGIPVI RWEEPPEGPV LVLLDQTRLP AEEVELVCTD ASALVEAIRS
LAVRGAPLLG IAGAYGVALA AARGFEVAEA AQALESARPT AVNLSVGVRR ARTAHQAALA
KTGDPAAAAA AALAAARTLH REDAEASARM AAHGLALLEE LQPGGGHRVL THCNSGSLVS
GGEGTAFAVA LQAHREGRLR RLWVDETRPL LQGARLTAYE AARSGMAYTL LTDNAAGSLF
AAGEVDAVLI GADRIAADGS VANKVGSYPL AVLARYHHVP FIVVAPVTTI DLDTPDGASI
EVEQRPGFEV TEVTAPQVPV TGAGGGIPVA PLGTQAYNPA FDVTPPELVT AIVTEEGTVS
PVTAEALGAL CASSRQVTI
//
