ID G1U1X1_RABIT Unreviewed; 242 AA.
AC G1U1X1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 74.
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:ENSOCUP00000023363.1};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000023363.1, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000023363.1, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000023363.1,
RC ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000023363.1}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000023363.1};
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, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
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; AAGW02037611; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02037612; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02037613; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_008267886.1; XM_008269664.2.
DR AlphaFoldDB; G1U1X1; -.
DR SMR; G1U1X1; -.
DR STRING; 9986.ENSOCUP00000023363; -.
DR PaxDb; 9986-ENSOCUP00000023363; -.
DR Ensembl; ENSOCUT00000025282.3; ENSOCUP00000023363.1; ENSOCUG00000021141.3.
DR GeneID; 100349561; -.
DR KEGG; ocu:100349561; -.
DR CTD; 51074; -.
DR eggNOG; KOG2631; Eukaryota.
DR GeneTree; ENSGT00390000001680; -.
DR HOGENOM; CLU_006033_4_0_1; -.
DR InParanoid; G1U1X1; -.
DR OMA; HGLYTWG; -.
DR OrthoDB; 275419at2759; -.
DR TreeFam; TF105632; -.
DR UniPathway; UPA00904; UER00875.
DR Proteomes; UP000001811; Chromosome 1.
DR Bgee; ENSOCUG00000021141; Expressed in skeletal muscle tissue and 15 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; 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:UP000001811};
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; 27117 MW; 73C008C7E9CF7A9E CRC64;
MSGRLAPEGD CCSRRCGAQD KEHPRYLIPE LCKQFYHLGW VTGTGGGISL KHGNEIYIAP
SGVQKERIQP EDMFVCDLNE QDISGPPPSK KLKKSQCTPL FMNAYTMRGA GAVIHTHSKA
AVMATLLFPG REFKITHQEM IKGIKKCTSG GYYRYDDMLV VPIIENTPEE KDLKERMAQA
MNEYPDSCAV LVRRHGVYVW GETWEKAKTM CECYDYLFDI AVSMKKVGLD PTQLPAGENG
IV
//
