ID I8RJB7_9FIRM Unreviewed; 350 AA.
AC I8RJB7;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 38.
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=FB4_3429 {ECO:0000313|EMBL:EIW18255.1};
OS Pelosinus fermentans B4.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Pelosinus.
OX NCBI_TaxID=1149862 {ECO:0000313|EMBL:EIW18255.1, ECO:0000313|Proteomes:UP000004324};
RN [1] {ECO:0000313|EMBL:EIW18255.1, ECO:0000313|Proteomes:UP000004324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4 {ECO:0000313|EMBL:EIW18255.1,
RC ECO:0000313|Proteomes:UP000004324};
RX PubMed=22933770; DOI=10.1128/JB.01174-12;
RA Brown S.D., Podar M., Klingeman D.M., Johnson C.M., Yang Z.K.,
RA Utturkar S.M., Land M.L., Mosher J.J., Hurt R.A.Jr., Phelps T.J.,
RA Palumbo A.V., Arkin A.P., Hazen T.C., Elias D.A.;
RT "Draft Genome Sequences for Two Metal-Reducing Pelosinus fermentans Strains
RT Isolated from a Cr(VI)-Contaminated Site and for Type Strain R7.";
RL J. Bacteriol. 194:5147-5148(2012).
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:EIW18255.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AKVJ01000027; EIW18255.1; -; Genomic_DNA.
DR RefSeq; WP_007934358.1; NZ_AKVJ01000027.1.
DR AlphaFoldDB; I8RJB7; -.
DR PATRIC; fig|1149862.3.peg.2395; -.
DR OrthoDB; 9803436at2; -.
DR UniPathway; UPA00904; UER00874.
DR Proteomes; UP000004324; Unassembled WGS sequence.
DR GO; GO:0046523; F:S-methyl-5-thioribose-1-phosphate isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
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 Initiation factor {ECO:0000313|EMBL:EIW18255.1};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01678};
KW Methionine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01678};
KW Protein biosynthesis {ECO:0000313|EMBL:EIW18255.1}.
FT ACT_SITE 235
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT BINDING 45..47
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT BINDING 245..246
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT SITE 155
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
SQ SEQUENCE 350 AA; 38417 MW; 36E9CE7BF74AAE43 CRC64;
MLQTIEWKNS TLWLLDQTLL PNRIEFIECH SFQRVAQAIK RLEVRGAPAI GAAAAFGLVL
GAKELCNDSD FGTNIERVAE ELRQTRPTAV NLFWAIERMM SIIHKANCDK DIIDLVKDLE
KEAISIASED CAINHKISQY GAQLFNEPVS VLTHCNAGAL ATAGFGTALG VIRQAFSEGK
ITRVFADETR PLLQGARLTA WELMQENIPV TLITDNMAGW VMKKNMVQAV IVGADRITLN
GDVANKIGTY SVAVLAKEHK IPFYVAAPVS TFDFTMESGL NIPIEERHAD EVAQFAGVLT
APKGVEVFNP AFDVTPNSLI SAIITEYGVL EQPYHEAIIA LQQKKIKGVL
//