ID   A0A7K7C626_APHCE        Unreviewed;       223 AA.
AC   A0A7K7C626;
DT   07-APR-2021, integrated into UniProtKB/TrEMBL.
DT   07-APR-2021, sequence version 1.
DT   18-JUN-2025, entry version 17.
DE   SubName: Full=MTNB dehydratase {ECO:0000313|EMBL:NWY16224.1};
DE   Flags: Fragment;
GN   Name=Apip {ECO:0000313|EMBL:NWY16224.1};
GN   ORFNames=APHCOE_R08647 {ECO:0000313|EMBL:NWY16224.1};
OS   Aphelocoma coerulescens (Florida scrub-jay) (Corvus coerulescens).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC   Passeriformes; Corvoidea; Corvidae; Aphelocoma.
OX   NCBI_TaxID=39617 {ECO:0000313|EMBL:NWY16224.1, ECO:0000313|Proteomes:UP000575874};
RN   [1] {ECO:0000313|EMBL:NWY16224.1, ECO:0000313|Proteomes:UP000575874}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OUT-0022 {ECO:0000313|EMBL:NWY16224.1};
RC   TISSUE=Blood {ECO:0000313|EMBL:NWY16224.1};
RA   Zhang G.;
RT   "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL   Submitted (SEP-2019) 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:0000256|ARBA:ARBA00060021}.
CC   -!- SIMILARITY: Belongs to the aldolase class II family. Adducin subfamily.
CC       {ECO:0000256|ARBA:ARBA00006274}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:NWY16224.1}.
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DR   EMBL; VZSI01000068; NWY16224.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A7K7C626; -.
DR   Proteomes; UP000575874; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046570; F:methylthioribulose 1-phosphate dehydratase activity; IEA:TreeGrafter.
DR   GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:InterPro.
DR   FunFam; 3.40.225.10:FF:000003; Methylthioribulose-1-phosphate dehydratase; 1.
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};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167};
KW   Reference proteome {ECO:0000313|Proteomes:UP000575874};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          7..203
FT                   /note="Class II aldolase/adducin N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01007"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:NWY16224.1"
FT   NON_TER         223
FT                   /evidence="ECO:0000313|EMBL:NWY16224.1"
SQ   SEQUENCE   223 AA;  25042 MW;  C0F793E3F14C96D1 CRC64;
     DGLHPRNLIP ELCRLFYGLG WVTGTGGGIS LKHGDEIYIA PSGVQKERIQ PEDMFVCDMD
     EQDISGPPLH KKLKKSQCTP LFMNAYTMRG AGAVIHTHSK AAVMATLLYP GSEFSITHQE
     MIKGIQKCTS GGYYRYDDTL VVPIIENTPE EKDLKERMAR AMEKYPDSCA VLVRRHGVYV
     WGETWEKAKT MCECYDYLFD IAVQMKQHGL DPSKHPAGEN GIL
//