位置:首页 > 蛋白库 > MTNB_ASPTN
MTNB_ASPTN
ID   MTNB_ASPTN              Reviewed;         241 AA.
AC   Q0CT19;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 71.
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};
GN   Name=mde1 {ECO:0000255|HAMAP-Rule:MF_03116}; ORFNames=ATEG_03165;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) 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       {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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CH476597; EAU36439.1; -; Genomic_DNA.
DR   RefSeq; XP_001212343.1; XM_001212343.1.
DR   AlphaFoldDB; Q0CT19; -.
DR   SMR; Q0CT19; -.
DR   STRING; 341663.Q0CT19; -.
DR   EnsemblFungi; EAU36439; EAU36439; ATEG_03165.
DR   GeneID; 4317587; -.
DR   VEuPathDB; FungiDB:ATEG_03165; -.
DR   eggNOG; KOG2631; Eukaryota.
DR   HOGENOM; CLU_006033_4_0_1; -.
DR   OMA; IRGHGLY; -.
DR   OrthoDB; 1062330at2759; -.
DR   UniPathway; UPA00904; UER00875.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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: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   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   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cytoplasm; Lyase; Metal-binding;
KW   Methionine biosynthesis; Reference proteome; Zinc.
FT   CHAIN           1..241
FT                   /note="Methylthioribulose-1-phosphate dehydratase"
FT                   /id="PRO_0000393811"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        147
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03116"
FT   BINDING         101
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03116"
FT   BINDING         118
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03116"
FT   BINDING         120
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03116"
FT   BINDING         203
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03116"
SQ   SEQUENCE   241 AA;  27123 MW;  5F4395561A1F0887 CRC64;
     MSQEITQKDN NDHLVQSSDP DHPANMIPDL CRKFYNWGWV TGTGGGTSIR RGDHIFIAPS
     GVQKELMQPH NIFVLEFPTP KYPPSDRKYI RKPLDLKPSA CTPLFLAAFE RGAGCCIHTH
     SQWAVLVTLL VEREKGPGGY FEISNIEQIK GIPRGKGKGM MGFHDTLRIP IIENTAFEED
     LTGSLEKAME ENPDTYAVLV KRHGIYVWGD DVAKAKTQCE SLDYLFQLAV EMHKLGLPWV
     K
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024