ID   MTNB_DANRE              Reviewed;         241 AA.
AC   Q66I75;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=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};
DE   AltName: Full=APAF1-interacting protein homolog {ECO:0000255|HAMAP-Rule:MF_03116};
GN   Name=apip {ECO:0000255|HAMAP-Rule:MF_03116}; ORFNames=zgc:103619;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=AB; TISSUE=Liver;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
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       Functions in the methionine salvage pathway. May play a role in
CC       apoptosis. {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; BC081498; AAH81498.1; -; mRNA.
DR   RefSeq; NP_001004679.1; NM_001004679.1.
DR   AlphaFoldDB; Q66I75; -.
DR   SMR; Q66I75; -.
DR   STRING; 7955.ENSDARP00000027609; -.
DR   PaxDb; Q66I75; -.
DR   DNASU; 447941; -.
DR   GeneID; 447941; -.
DR   KEGG; dre:447941; -.
DR   CTD; 51074; -.
DR   ZFIN; ZDB-GENE-040912-128; apip.
DR   eggNOG; KOG2631; Eukaryota.
DR   InParanoid; Q66I75; -.
DR   OrthoDB; 1062330at2759; -.
DR   PhylomeDB; Q66I75; -.
DR   Reactome; R-DRE-111458; Formation of apoptosome.
DR   Reactome; R-DRE-9627069; Regulation of the apoptosome activity.
DR   UniPathway; UPA00904; UER00875.
DR   PRO; PR:Q66I75; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
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:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   Amino-acid biosynthesis; Apoptosis; Cytoplasm; Lyase; Metal-binding;
KW   Methionine biosynthesis; Reference proteome; Zinc.
FT   CHAIN           1..241
FT                   /note="Methylthioribulose-1-phosphate dehydratase"
FT                   /id="PRO_0000239025"
FT   ACT_SITE        138
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03116"
FT   BINDING         96
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03116"
FT   BINDING         114
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03116"
FT   BINDING         116
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03116"
FT   BINDING         194
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03116"
SQ   SEQUENCE   241 AA;  27231 MW;  584142347F792AE8 CRC64;
     MSSVVNAAYA EYNGKEKGDQ EDPRVLIPQL CRLFYELGWV TGTGGGISLR HGEHIYIAPS
     GVQKERIQPE DLFVCDIDEK DISCPPPQKK LKKSQCTPPF MNAYTMRGAQ AVIHTHSKSA
     VMATLLFPGK EFRITHQEMI KGIRKGNSGT NFRYDDTLVV PIIENTPEEK DLKERMARAM
     DMYPDSCAVL VRRHGVYVWG ETWEKAKTMC ECYDYLFDIA VQMKQSGLDP SAFPTEEKGI
     V