ID A0A2I3GH41_NOMLE Unreviewed; 242 AA.
AC A0A2I3GH41;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Methylthioribulose-1-phosphate dehydratase {ECO:0000256|HAMAP-Rule:MF_03116};
DE Short=MTRu-1-P dehydratase {ECO:0000256|HAMAP-Rule:MF_03116};
DE EC=4.2.1.109 {ECO:0000256|HAMAP-Rule:MF_03116};
DE AltName: Full=APAF1-interacting protein {ECO:0000256|HAMAP-Rule:MF_03116};
GN Name=APIP {ECO:0000256|HAMAP-Rule:MF_03116,
GN ECO:0000313|Ensembl:ENSNLEP00000030645.1};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000030645.1, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000030645.1, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000030645.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|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:0000256|HAMAP-Rule:MF_03116};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03116};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|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:0000256|HAMAP-Rule:MF_03116}.
CC -!- SUBUNIT: Homotetramer. Interacts with APAF1. May interact with CASP1.
CC {ECO:0000256|HAMAP-Rule:MF_03116}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03116}.
CC -!- SIMILARITY: Belongs to the aldolase class II family. Adducin subfamily.
CC {ECO:0000256|ARBA:ARBA00006274}.
CC -!- SIMILARITY: Belongs to the aldolase class II family. MtnB subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03116}.
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DR EMBL; ADFV01113403; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01113404; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01113405; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01113406; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003254457.1; XM_003254409.2.
DR AlphaFoldDB; A0A2I3GH41; -.
DR SMR; A0A2I3GH41; -.
DR STRING; 61853.ENSNLEP00000030645; -.
DR Ensembl; ENSNLET00000047042.1; ENSNLEP00000030645.1; ENSNLEG00000028265.1.
DR GeneID; 100587323; -.
DR KEGG; nle:100587323; -.
DR CTD; 51074; -.
DR GeneTree; ENSGT00390000001680; -.
DR InParanoid; A0A2I3GH41; -.
DR OMA; HGLYTWG; -.
DR OrthoDB; 275419at2759; -.
DR UniPathway; UPA00904; UER00875.
DR Proteomes; UP000001073; Chromosome 15.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0046570; F:methylthioribulose 1-phosphate dehydratase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniPathway.
DR GO; GO:0019284; P:L-methionine salvage from S-adenosylmethionine; IEA:UniProtKB-UniRule.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0051289; P:protein homotetramerization; IEA:Ensembl.
DR GO; GO:0070269; P:pyroptosis; IEA:Ensembl.
DR GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR Gene3D; 3.40.225.10; Class II aldolase/adducin N-terminal domain; 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 NCBIfam; TIGR03328; salvage_mtnB; 1.
DR PANTHER; PTHR10640; METHYLTHIORIBULOSE-1-PHOSPHATE DEHYDRATASE; 1.
DR PANTHER; PTHR10640:SF7; METHYLTHIORIBULOSE-1-PHOSPHATE DEHYDRATASE; 1.
DR Pfam; PF00596; Aldolase_II; 1.
DR SMART; SM01007; Aldolase_II; 1.
DR SUPFAM; SSF53639; AraD/HMP-PK domain-like; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_03116};
KW Apoptosis {ECO:0000256|ARBA:ARBA00022703, ECO:0000256|HAMAP-Rule:MF_03116};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03116};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_03116};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03116};
KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167, ECO:0000256|HAMAP-
KW Rule:MF_03116}; Reference proteome {ECO:0000313|Proteomes:UP000001073};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_03116}.
FT DOMAIN 26..222
FT /note="Class II aldolase/adducin N-terminal"
FT /evidence="ECO:0000259|SMART:SM01007"
FT ACT_SITE 139
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03116"
FT BINDING 97
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03116"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03116"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03116"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03116"
SQ SEQUENCE 242 AA; 27125 MW; 9B8D5D1435D6775A CRC64;
MSGCDAREGD CCSRRCGAQD KEHPRYLIPE LCKQFYHLGW VTGTGGGISL KHGDEIYIAP
SGVQKERIQP EDMFVCDINE KDISGPSPSK KLKKSQCTPL FMNAYTMRGA GAVIHTHSKA
AVMATLLFPG REFKITHQEM IKGIKKCTSG GYYRYDDMLV VPIIENTPEE KDLKDRMAHA
MNEYPDSCAV LVRRHGVYVW GETWEKAKTM CECYDYLFDI AVSMKKVGLD PSQLPVGENG
IV
//
