ID   MTNAB_NOCFA             Reviewed;         552 AA.
AC   Q5YQZ6;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Probable bifunctional methylthioribose-1-phosphate isomerase/methylthioribulose-1-phosphate dehydratase;
DE   Includes:
DE     RecName: Full=Methylthioribose-1-phosphate isomerase;
DE              Short=M1Pi;
DE              Short=MTR-1-P isomerase;
DE              EC=5.3.1.23;
DE     AltName: Full=S-methyl-5-thioribose-1-phosphate isomerase;
DE   Includes:
DE     RecName: Full=Methylthioribulose-1-phosphate dehydratase;
DE              Short=MTRu-1-P dehydratase;
DE              EC=4.2.1.109;
GN   Name=mtnAB; OrderedLocusNames=NFA_45440;
OS   Nocardia farcinica (strain IFM 10152).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Nocardia.
OX   NCBI_TaxID=247156;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFM 10152;
RX   PubMed=15466710; DOI=10.1073/pnas.0406410101;
RA   Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K.,
RA   Shiba T., Hattori M.;
RT   "The complete genomic sequence of Nocardia farcinica IFM 10152.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(2004).
CC   -!- FUNCTION: Bifunctional protein that catalyzes the interconversion of
CC       methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-
CC       phosphate (MTRu-1-P), and the dehydration of methylthioribulose-1-
CC       phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate
CC       (DK-MTP-1-P). {ECO:0000250}.
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;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-methyl-5-thio-D-ribulose 1-phosphate = 5-methylsulfanyl-2,3-
CC         dioxopentyl phosphate + H2O; Xref=Rhea:RHEA:15549, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:58548, ChEBI:CHEBI:58828; EC=4.2.1.109;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
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.
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 2/6.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the eIF-2B
CC       alpha/beta/delta subunits family. MtnA subfamily. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the aldolase class II
CC       family. MtnB subfamily. {ECO:0000305}.
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DR   EMBL; AP006618; BAD59395.1; -; Genomic_DNA.
DR   RefSeq; WP_011211079.1; NC_006361.1.
DR   AlphaFoldDB; Q5YQZ6; -.
DR   SMR; Q5YQZ6; -.
DR   STRING; 247156.NFA_45440; -.
DR   EnsemblBacteria; BAD59395; BAD59395; NFA_45440.
DR   GeneID; 61135151; -.
DR   KEGG; nfa:NFA_45440; -.
DR   eggNOG; COG0182; Bacteria.
DR   eggNOG; COG0235; Bacteria.
DR   HOGENOM; CLU_036388_0_0_11; -.
DR   OMA; HTAVYRA; -.
DR   BioCyc; NFAR247156:NFA_RS22535-MON; -.
DR   UniPathway; UPA00904; UER00874.
DR   UniPathway; UPA00904; UER00875.
DR   Proteomes; UP000006820; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0046570; F:methylthioribulose 1-phosphate dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046523; F:S-methyl-5-thioribose-1-phosphate isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; 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; -; 1.
DR   Gene3D; 3.40.225.10; -; 1.
DR   Gene3D; 3.40.50.10470; -; 1.
DR   HAMAP; MF_01678; Salvage_MtnA; 1.
DR   HAMAP; MF_01677; Salvage_MtnB; 1.
DR   InterPro; IPR001303; Aldolase_II/adducin_N.
DR   InterPro; IPR036409; Aldolase_II/adducin_N_sf.
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; IPR017714; MethylthioRu-1-P_deHdtase_MtnB.
DR   InterPro; IPR037171; NagB/RpiA_transferase-like.
DR   Pfam; PF00596; Aldolase_II; 1.
DR   Pfam; PF01008; IF-2B; 1.
DR   SMART; SM01007; Aldolase_II; 1.
DR   SUPFAM; SSF100950; SSF100950; 1.
DR   SUPFAM; SSF53639; SSF53639; 1.
DR   TIGRFAMs; TIGR00524; eIF-2B_rel; 1.
DR   TIGRFAMs; TIGR00512; salvage_mtnA; 1.
DR   TIGRFAMs; TIGR03328; salvage_mtnB; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Isomerase; Lyase; Metal-binding;
KW   Methionine biosynthesis; Multifunctional enzyme; Reference proteome; Zinc.
FT   CHAIN           1..552
FT                   /note="Probable bifunctional methylthioribose-1-phosphate
FT                   isomerase/methylthioribulose-1-phosphate dehydratase"
FT                   /id="PRO_0000357211"
FT   REGION          1..333
FT                   /note="Methylthioribose-1-phosphate isomerase activity"
FT   REGION          334..535
FT                   /note="Methylthioribulose-1-phosphate dehydratase activity"
FT   ACT_SITE        236
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         49..51
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         91
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         195
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         246..247
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         427
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         429
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   SITE            156
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   552 AA;  57853 MW;  ECCDBF65489570CD CRC64;
     MRPIDDSSLT WDDGALVTVD QRGLPHEARP LRLRTADQII DAIKTLAIRG APAIGIAGAF
     AVVLATRAHT RDGIVDVAAV RAEADRIAAA RPTAVNLAWA VDRVRPRIAE GADAVLAETL
     DMLAEDGRVN RAAATHAADL VQRLCGPRPL RVLTHCNTGR LATSAFGTAI GALRVLAERG
     AVEEVLVDET RPLLQGARLT TWELAEAGIP HRLTIDSAAA WAMATGLVDC VLVGADRVTA
     RGDVANKIGT YAVALAAHRH GIPFVVVAPE STRDPATASW RDIVVEERAA EEVTAFAGSA
     TAPVGTAAFN PAFDVTPADL VTAVVTEHGV VHGTVAAEPG ARIAATAREL YARGWMPGTA
     GNLSVRTGDT AVVTASGLAK GELSATDMVR VAIADSTPLP GQDRRPSAET TIHTAVYRAT
     GAAAVVHVHS PFATALATRA GAADEVRVLR ITDYELIKGL GGSDPTAIDL AIFPNWRDVP
     RIAADIERRL AEHPGAPPVL CIAGHGITTW GENLTQARDR AECLEAVCEL VLRTGREHAF
     APQTHVLEMG PT