ID   MTNB_ESOLU              Reviewed;         257 AA.
AC   C1BYA3;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   07-SEP-2016, entry version 32.
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};
OS   Esox lucius (Northern pike).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii;
OC   Esociformes; Esocidae; Esox.
OX   NCBI_TaxID=8010;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RX   PubMed=20433749; DOI=10.1186/1471-2164-11-279;
RA   Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A.,
RA   Messmer A.M., Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J.,
RA   Davidson W.S., Koop B.F.;
RT   "Salmo salar and Esox lucius full-length cDNA sequences reveal changes
RT   in evolutionary pressures on a post-tetraploidization genome.";
RL   BMC Genomics 11:279-279(2010).
CC   -!- FUNCTION: Catalyzes the dehydration of methylthioribulose-1-
CC       phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-
CC       phosphate (DK-MTP-1-P). Functions in the methionine salvage
CC       pathway. May play a role in apoptosis. {ECO:0000255|HAMAP-
CC       Rule:MF_03116}.
CC   -!- CATALYTIC ACTIVITY: S-methyl-5-thio-D-ribulose 1-phosphate = 5-
CC       (methylthio)-2,3-dioxopentyl phosphate + H(2)O.
CC       {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-
CC       Rule:MF_03116};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via
CC       salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose
CC       1-phosphate: 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
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_03116}.
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DR   EMBL; BT079582; ACO14006.1; -; mRNA.
DR   ProteinModelPortal; C1BYA3; -.
DR   UniPathway; UPA00904; UER00875.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 biosynthetic process from methylthioadenosine; ISS:UniProtKB.
DR   GO; GO:0019284; P:L-methionine biosynthetic process from S-adenosylmethionine; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.225.10; -; 1.
DR   HAMAP; MF_03116; Salvage_MtnB_euk; 1.
DR   InterPro; IPR001303; Aldolase_II/adducin_N.
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; Zinc.
FT   CHAIN         1    257       Methylthioribulose-1-phosphate
FT                                dehydratase.
FT                                /FTId=PRO_0000393773.
FT   ACT_SITE    149    149       Proton donor/acceptor.
FT                                {ECO:0000255|HAMAP-Rule:MF_03116}.
FT   METAL       125    125       Zinc; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_03116}.
FT   METAL       127    127       Zinc; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_03116}.
FT   METAL       205    205       Zinc; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_03116}.
FT   BINDING     107    107       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03116}.
SQ   SEQUENCE   257 AA;  29383 MW;  B98A2114037151DF CRC64;
     MVSSQEKMAS ISDIIQKDED SGSEKTESQD KEHPRVLIPE LCRLFYKLGW VTGTGGGISL
     RHGDQIYIAP SGVQKERLQP EDMFVCDVEE RDICVPPAWK NLKKGQCTPL FMNAYTMRAA
     QAVIHTHSKA AVMATLFYPG KEFRITHQEM IKGIRKCTSG TNYRYDETLV VPIIENTPEE
     QDLKERMALA MEQYPESCAV LVRRHGVYVW GESWEKAKTM CECYDYLFDI AVKMKQCGLD
     PSAQPVEENL YYYVQQA
//