ID A6P078_9FIRM Unreviewed; 339 AA.
AC A6P078;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 24-JAN-2024, entry version 70.
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:EDM98228.1};
GN ORFNames=BACCAP_03886 {ECO:0000313|EMBL:EDM98228.1};
OS Pseudoflavonifractor capillosus ATCC 29799.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Pseudoflavonifractor.
OX NCBI_TaxID=411467 {ECO:0000313|EMBL:EDM98228.1, ECO:0000313|Proteomes:UP000003639};
RN [1] {ECO:0000313|EMBL:EDM98228.1, ECO:0000313|Proteomes:UP000003639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29799 {ECO:0000313|EMBL:EDM98228.1,
RC ECO:0000313|Proteomes:UP000003639};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDM98228.1, ECO:0000313|Proteomes:UP000003639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29799 {ECO:0000313|EMBL:EDM98228.1,
RC ECO:0000313|Proteomes:UP000003639};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Pseudoflavonifractor capillosus ATCC 29799.";
RL Submitted (JUN-2007) 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:EDM98228.1}.
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DR EMBL; AAXG02000041; EDM98228.1; -; Genomic_DNA.
DR RefSeq; WP_006574374.1; NZ_AAXG02000041.1.
DR AlphaFoldDB; A6P078; -.
DR STRING; 411467.BACCAP_03886; -.
DR eggNOG; COG0182; Bacteria.
DR OrthoDB; 9803436at2; -.
DR UniPathway; UPA00904; UER00874.
DR Proteomes; UP000003639; 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: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};
KW Reference proteome {ECO:0000313|Proteomes:UP000003639}.
FT ACT_SITE 231
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT BINDING 44..46
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT BINDING 85
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT BINDING 190
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT BINDING 241..242
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT SITE 151
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
SQ SEQUENCE 339 AA; 36700 MW; FF650AA2C7C6A7AD CRC64;
MDAIRWEGNT LYLLDQTRLP VQEDWIAYTD FRSVARAITD MVVRGAPAIG ITAAYAYCLA
ALEFRNAPDF AAAMEQAEQV LAASRPTAVN LFWALRRMAD CLKANGSTPE AIDVLIQEAQ
AIHEEDVEMN RTLGDFGAAV VPAHARILTH CNAGSLATGG YGTALGVVRS AFNQGKVDMV
YADETRPLLQ GARLTAYELV HDNIPCTLIT DNMAGFLMAQ GKVDLVILGC DRMAANGDFA
NKIGTYSVAV NARYHGIPFY TALPSSTIDL SIEDGSGIPI EERPGVEVTH LAGVQTAPEQ
VRTWNPAFDV TPHQLLTGII TERGVIYPPF KENLAKLFG
//
