ID D3PAF0_DEFDS Unreviewed; 329 AA.
AC D3PAF0;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 77.
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 OrderedLocusNames=DEFDS_0061 {ECO:0000313|EMBL:BAI79573.1};
OS Deferribacter desulfuricans (strain DSM 14783 / JCM 11476 / NBRC 101012 /
OS SSM1).
OC Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC Deferribacteraceae; Deferribacter.
OX NCBI_TaxID=639282 {ECO:0000313|EMBL:BAI79573.1, ECO:0000313|Proteomes:UP000001520};
RN [1] {ECO:0000313|EMBL:BAI79573.1, ECO:0000313|Proteomes:UP000001520}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14783 / JCM 11476 / NBRC 101012 / SSM1
RC {ECO:0000313|Proteomes:UP000001520};
RX PubMed=20189949; DOI=10.1093/dnares/dsq005;
RA Takaki Y., Shimamura S., Nakagawa S., Fukuhara Y., Horikawa H., Ankai A.,
RA Harada T., Hosoyama A., Oguchi A., Fukui S., Fujita N., Takami H.,
RA Takai K.;
RT "Bacterial lifestyle in a deep-sea hydrothermal vent chimney revealed by
RT the genome sequence of the thermophilic bacterium Deferribacter
RT desulfuricans SSM1.";
RL DNA Res. 17:123-137(2010).
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; AP011529; BAI79573.1; -; Genomic_DNA.
DR RefSeq; WP_013006821.1; NC_013939.1.
DR AlphaFoldDB; D3PAF0; -.
DR STRING; 639282.DEFDS_0061; -.
DR KEGG; ddf:DEFDS_0061; -.
DR eggNOG; COG0182; Bacteria.
DR HOGENOM; CLU_016218_1_2_0; -.
DR OrthoDB; 9803436at2; -.
DR UniPathway; UPA00904; UER00874.
DR Proteomes; UP000001520; Chromosome.
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:BAI79573.1};
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:BAI79573.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001520}.
FT ACT_SITE 222
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 79
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT BINDING 181
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT BINDING 232..233
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
FT SITE 142
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01678"
SQ SEQUENCE 329 AA; 36214 MW; 42B2A28E61DE6A3C CRC64;
MVEPIIWENG VLKLLDQRIL PHEKRYVECN TAENVANAIK DMVVRGAPAI GVTAAFGVVL
GLKEGKNIDE IYSLLLNTRP TAVNLKWALD KMKAAYEYAE GNIDFVEESA VKLFERDIEY
NRMIGKSGLQ VIKDGDNILT HCNAGALATA GYGTALGVLR AAKEAGLNIH VYVDETRPYL
QGARLTAFEL MEEGISCTLI CDNMPGFLMK QKKIDKIIVG ADRIAKNGDT ANKIGTYQLA
VLAYFHDIPL YIAAPISTFD FSIECGDDIV IEHRNPDEVR KVGDKLIAPE NVNVYNPAFD
VTPANLISGF ITEFGVFNSV DEILNKIND
//
