MTNB_LITCT
ID MTNB_LITCT Reviewed; 239 AA.
AC C1C4M8;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 43.
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 Lithobates catesbeianus (American bullfrog) (Rana catesbeiana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX NCBI_TaxID=8400;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Helbing C.C., Veldhoen N., Leong J., Koop B.F.;
RT "Rana catesbeiana ESTs and full-length cDNAs.";
RL Submitted (APR-2009) 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; BT081807; ACO51938.1; -; mRNA.
DR AlphaFoldDB; C1C4M8; -.
DR SMR; C1C4M8; -.
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 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; Zinc.
FT CHAIN 1..239
FT /note="Methylthioribulose-1-phosphate dehydratase"
FT /id="PRO_0000393776"
FT ACT_SITE 136
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03116"
FT BINDING 94
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03116"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
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 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03116"
SQ SEQUENCE 239 AA; 27031 MW; 7467C957734AA621 CRC64;
MYYCNGENCN QTDSAKEKGH PRHLIPELCR QFYNLGWVTG TGGGISMKHG EEIYIAPSGV
QKERIQPDDL FVCDIDERDI SCPPPYKNLK KSQCTPLFMN AYTLRGAGAV IHTHSKSAVL
ATLLFPGKEF RITHQEMIKG IKKGSSGDYY RYDDLLVVPI VENTPEEKDL KDRMARAMTE
YPDSCAVLVR RHGVYVWGDT WEKAKTMCEC YDYLFDIAVQ MKQLGLDPAA HPAEEKGIV
