MTNB_AQUAE
ID MTNB_AQUAE Reviewed; 208 AA.
AC O67788;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Methylthioribulose-1-phosphate dehydratase {ECO:0000255|HAMAP-Rule:MF_01677};
DE Short=MTRu-1-P dehydratase {ECO:0000255|HAMAP-Rule:MF_01677};
DE EC=4.2.1.109 {ECO:0000255|HAMAP-Rule:MF_01677};
GN Name=mtnB {ECO:0000255|HAMAP-Rule:MF_01677}; OrderedLocusNames=aq_1979;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RG RIKEN structural genomics initiative (RSGI);
RT "Crystal structure of the L-fuculose-1-phosphate aldolase (aq_1979) from
RT Aquifex aeolicus VF5.";
RL Submitted (DEC-2007) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the dehydration of methylthioribulose-1-phosphate
CC (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P).
CC {ECO:0000255|HAMAP-Rule:MF_01677}.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_01677};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01677};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01677};
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. {ECO:0000255|HAMAP-Rule:MF_01677}.
CC -!- SIMILARITY: Belongs to the aldolase class II family. MtnB subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01677}.
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DR EMBL; AE000657; AAC07751.1; -; Genomic_DNA.
DR PIR; H70469; H70469.
DR RefSeq; NP_214357.1; NC_000918.1.
DR RefSeq; WP_010881293.1; NC_000918.1.
DR PDB; 2IRP; X-ray; 2.40 A; A/B=1-208.
DR PDBsum; 2IRP; -.
DR AlphaFoldDB; O67788; -.
DR SMR; O67788; -.
DR STRING; 224324.aq_1979; -.
DR EnsemblBacteria; AAC07751; AAC07751; aq_1979.
DR KEGG; aae:aq_1979; -.
DR PATRIC; fig|224324.8.peg.1528; -.
DR eggNOG; COG0235; Bacteria.
DR HOGENOM; CLU_006033_4_1_0; -.
DR InParanoid; O67788; -.
DR OMA; IRGHGLY; -.
DR OrthoDB; 599627at2; -.
DR UniPathway; UPA00904; UER00875.
DR EvolutionaryTrace; O67788; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0046570; F:methylthioribulose 1-phosphate dehydratase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IBA:GO_Central.
DR GO; GO:0019284; P:L-methionine salvage from S-adenosylmethionine; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.225.10; -; 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; IPR017714; MethylthioRu-1-P_deHdtase_MtnB.
DR Pfam; PF00596; Aldolase_II; 1.
DR SMART; SM01007; Aldolase_II; 1.
DR SUPFAM; SSF53639; SSF53639; 1.
DR TIGRFAMs; TIGR03328; salvage_mtnB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Lyase; Metal-binding;
KW Methionine biosynthesis; Reference proteome; Zinc.
FT CHAIN 1..208
FT /note="Methylthioribulose-1-phosphate dehydratase"
FT /id="PRO_0000162933"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01677"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01677"
FT HELIX 5..25
FT /evidence="ECO:0007829|PDB:2IRP"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:2IRP"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:2IRP"
FT STRAND 41..48
FT /evidence="ECO:0007829|PDB:2IRP"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:2IRP"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:2IRP"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:2IRP"
FT HELIX 79..90
FT /evidence="ECO:0007829|PDB:2IRP"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:2IRP"
FT HELIX 103..111
FT /evidence="ECO:0007829|PDB:2IRP"
FT STRAND 114..118
FT /evidence="ECO:0007829|PDB:2IRP"
FT HELIX 122..125
FT /evidence="ECO:0007829|PDB:2IRP"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:2IRP"
FT HELIX 149..162
FT /evidence="ECO:0007829|PDB:2IRP"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:2IRP"
FT TURN 172..174
FT /evidence="ECO:0007829|PDB:2IRP"
FT STRAND 175..182
FT /evidence="ECO:0007829|PDB:2IRP"
FT HELIX 183..203
FT /evidence="ECO:0007829|PDB:2IRP"
SQ SEQUENCE 208 AA; 23550 MW; 3295652C5ED17344 CRC64;
MNVELFKKFS EKVEEIIEAG RILHSRGWVP ATSGNISAKV SEEYIAITAS GKHKGKLTPE
DILLIDYEGR PVGGGKPSAE TLLHTTVYKL FPEVNAVVHT HSPNATVISI VEKKDFVELE
DYELLKAFPD IHTHEVKIKI PIFPNEQNIP LLAKEVENYF KTSEDKYGFL IRGHGLYTWG
RSMEEALIHT EALEFIFECE LKLLSFHS
