MTNB_BOVIN
ID MTNB_BOVIN Reviewed; 242 AA.
AC Q0VCJ2;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
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 {ECO:0000255|HAMAP-Rule:MF_03116};
GN Name=APIP {ECO:0000255|HAMAP-Rule:MF_03116};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) 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, which plays a key role in
CC cancer, apoptosis, microbial proliferation and inflammation. May
CC inhibit the CASP1-related inflammatory response (pyroptosis), the
CC CASP9-dependent apoptotic pathway and the cytochrome c-dependent and
CC APAF1-mediated cell death. {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 -!- SUBUNIT: Homotetramer. Interacts with APAF1. May interact with CASP1.
CC {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; BC120140; AAI20141.1; -; mRNA.
DR RefSeq; NP_001068820.1; NM_001075352.2.
DR AlphaFoldDB; Q0VCJ2; -.
DR SMR; Q0VCJ2; -.
DR STRING; 9913.ENSBTAP00000024300; -.
DR PaxDb; Q0VCJ2; -.
DR Ensembl; ENSBTAT00000024300; ENSBTAP00000024300; ENSBTAG00000018257.
DR GeneID; 508345; -.
DR KEGG; bta:508345; -.
DR CTD; 51074; -.
DR VEuPathDB; HostDB:ENSBTAG00000018257; -.
DR VGNC; VGNC:26016; APIP.
DR eggNOG; KOG2631; Eukaryota.
DR GeneTree; ENSGT00390000001680; -.
DR HOGENOM; CLU_006033_4_0_1; -.
DR InParanoid; Q0VCJ2; -.
DR OMA; IRGHGLY; -.
DR OrthoDB; 1062330at2759; -.
DR TreeFam; TF105632; -.
DR UniPathway; UPA00904; UER00875.
DR Proteomes; UP000009136; Chromosome 15.
DR Bgee; ENSBTAG00000018257; Expressed in oocyte and 103 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
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 GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR GO; GO:0070269; P:pyroptosis; ISS:UniProtKB.
DR GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
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..242
FT /note="Methylthioribulose-1-phosphate dehydratase"
FT /id="PRO_0000393742"
FT ACT_SITE 139
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03116"
FT BINDING 97
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03116"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03116"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03116"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03116"
SQ SEQUENCE 242 AA; 27095 MW; 0B4B819140858F14 CRC64;
MSGSHAPEGD CCLRQCRAQD KEHPRYLIPE LCKQFYHLGW VTGTGGGISL KHGNEIYIAP
SGVQKERIQP EDMFVCDINE KDISGPPPSK NLKKSQCTPL FMNAYTMREA GAVIHTHSKA
AVMATLVFPG KEFKITHQEM IKGIKKCTSG GYYRYDDMLV VPIIENTPEE KDLKERMARA
VNDYPDSCAV LVRRHGVYVW GETWEKAKTM CECYDYLFDV AVSMKQAGLD PAQLPAGENG
IV
