MTNB_CAEEL
ID MTNB_CAEEL Reviewed; 263 AA.
AC Q23261;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Probable methylthioribulose-1-phosphate dehydratase {ECO:0000255|HAMAP-Rule:MF_03116};
DE Short=MTRu-1-P dehydratase {ECO:0000255|HAMAP-Rule:MF_03116};
DE EC=4.2.1.109 {ECO:0000255|HAMAP-Rule:MF_03116};
GN ORFNames=ZC373.5;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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_03116}.
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_03116};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03116};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03116};
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_03116}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03116}.
CC -!- SIMILARITY: Belongs to the aldolase class II family. MtnB subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03116}.
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DR EMBL; Z49131; CAA88977.2; -; Genomic_DNA.
DR PIR; T27523; T27523.
DR RefSeq; NP_509690.2; NM_077289.4.
DR AlphaFoldDB; Q23261; -.
DR SMR; Q23261; -.
DR IntAct; Q23261; 1.
DR STRING; 6239.ZC373.5; -.
DR EPD; Q23261; -.
DR PaxDb; Q23261; -.
DR PeptideAtlas; Q23261; -.
DR EnsemblMetazoa; ZC373.5.1; ZC373.5.1; WBGene00013870.
DR GeneID; 181218; -.
DR KEGG; cel:CELE_ZC373.5; -.
DR UCSC; ZC373.5; c. elegans.
DR CTD; 181218; -.
DR WormBase; ZC373.5; CE37460; WBGene00013870; -.
DR eggNOG; KOG2631; Eukaryota.
DR GeneTree; ENSGT00390000001680; -.
DR HOGENOM; CLU_006033_4_0_1; -.
DR InParanoid; Q23261; -.
DR OMA; IRGHGLY; -.
DR OrthoDB; 1062330at2759; -.
DR PhylomeDB; Q23261; -.
DR UniPathway; UPA00904; UER00875.
DR PRO; PR:Q23261; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00013870; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0046570; F:methylthioribulose 1-phosphate dehydratase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
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_03116; Salvage_MtnB_euk; 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 InterPro; IPR027514; Salvage_MtnB_euk.
DR PANTHER; PTHR10640; PTHR10640; 1.
DR Pfam; PF00596; Aldolase_II; 1.
DR SMART; SM01007; Aldolase_II; 1.
DR SUPFAM; SSF53639; SSF53639; 1.
DR TIGRFAMs; TIGR03328; salvage_mtnB; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Cytoplasm; Lyase; Metal-binding;
KW Methionine biosynthesis; Reference proteome; Zinc.
FT CHAIN 1..263
FT /note="Probable methylthioribulose-1-phosphate dehydratase"
FT /id="PRO_0000393794"
FT ACT_SITE 144
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03116"
FT BINDING 102
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03116"
FT BINDING 120
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03116"
FT BINDING 122
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03116"
FT BINDING 200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03116"
SQ SEQUENCE 263 AA; 30005 MW; 89D00AEB6A60C261 CRC64;
MVEFVNDPNF KDLVVDTTID NRNDEEPMTI RNFTELMIQF YKLGWMRGSG GAMGCISGSE
LMISPSALQK ERIREQDVFV YNMKDKTEVQ RPPNKRITVS SCSVLFSLIM KETGSECVIH
THSKCANLIT QLIKSNVFEI SHQEYIKGIY DPFSGKALKY SDTLTIPIID NMPSESQLLE
PIRGVLENYP QAIAVLVRNH GLFVWGPTWE STKIMTECID YLLELSIEML KNNIPLVNEE
AFEKEDNLSD KMRTLMFGDM APV
