位置:首页 > 蛋白库 > MTND_MACMU
MTND_MACMU
ID   MTND_MACMU              Reviewed;         179 AA.
AC   F6QS54;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Acireductone dioxygenase {ECO:0000255|HAMAP-Rule:MF_03154};
DE   AltName: Full=Acireductone dioxygenase (Fe(2+)-requiring) {ECO:0000255|HAMAP-Rule:MF_03154};
DE            Short=ARD' {ECO:0000255|HAMAP-Rule:MF_03154};
DE            Short=Fe-ARD {ECO:0000255|HAMAP-Rule:MF_03154};
DE            EC=1.13.11.54 {ECO:0000255|HAMAP-Rule:MF_03154};
DE   AltName: Full=Acireductone dioxygenase (Ni(2+)-requiring) {ECO:0000255|HAMAP-Rule:MF_03154};
DE            Short=ARD {ECO:0000255|HAMAP-Rule:MF_03154};
DE            Short=Ni-ARD {ECO:0000255|HAMAP-Rule:MF_03154};
DE            EC=1.13.11.53 {ECO:0000255|HAMAP-Rule:MF_03154};
DE   AltName: Full=Membrane-type 1 matrix metalloproteinase cytoplasmic tail-binding protein 1 {ECO:0000255|HAMAP-Rule:MF_03154};
DE            Short=MTCBP-1 {ECO:0000255|HAMAP-Rule:MF_03154};
GN   Name=ADI1 {ECO:0000255|HAMAP-Rule:MF_03154};
GN   Synonyms=MTCBP1 {ECO:0000255|HAMAP-Rule:MF_03154};
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17573;
RX   PubMed=17431167; DOI=10.1126/science.1139247;
RA   Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
RA   Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K.,
RA   Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C.,
RA   Makova K.D., Miller W., Milosavljevic A., Palermo R.E., Siepel A.,
RA   Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
RA   Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H.,
RA   Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J.,
RA   Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N.,
RA   Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S.,
RA   Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V.,
RA   Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C.,
RA   Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J.,
RA   Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R.,
RA   Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L.,
RA   Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X.,
RA   Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P.,
RA   Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L.,
RA   Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H.,
RA   Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
RA   Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
RA   Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
RA   Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
RA   Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A.,
RA   Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A.,
RA   Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D.,
RA   Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y.,
RA   Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N.,
RA   Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E.,
RA   Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P.,
RA   Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D.,
RA   Kuhn R.M., Smith K.E., Zwieg A.S.;
RT   "Evolutionary and biomedical insights from the rhesus macaque genome.";
RL   Science 316:222-234(2007).
CC   -!- FUNCTION: Catalyzes 2 different reactions between oxygen and the
CC       acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene)
CC       depending upon the metal bound in the active site. Fe-containing
CC       acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4-
CC       methylthiobutyrate (KMTB), the alpha-ketoacid precursor of methionine
CC       in the methionine recycle pathway. Ni-containing acireductone
CC       dioxygenase (Ni-ARD) produces methylthiopropionate, carbon monoxide and
CC       formate, and does not lie on the methionine recycle pathway. Also down-
CC       regulates cell migration mediated by MMP14. {ECO:0000255|HAMAP-
CC       Rule:MF_03154}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2 = 4-
CC         methylsulfanyl-2-oxobutanoate + formate + 2 H(+);
CC         Xref=Rhea:RHEA:24504, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:15740, ChEBI:CHEBI:16723, ChEBI:CHEBI:49252;
CC         EC=1.13.11.54; Evidence={ECO:0000255|HAMAP-Rule:MF_03154};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2 = 3-
CC         (methylsulfanyl)propanoate + CO + formate + 2 H(+);
CC         Xref=Rhea:RHEA:14161, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:15740, ChEBI:CHEBI:17245, ChEBI:CHEBI:49016,
CC         ChEBI:CHEBI:49252; EC=1.13.11.53; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03154};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03154};
CC       Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03154};
CC       Note=Binds either 1 Fe or Ni cation per monomer. Iron-binding promotes
CC       an acireductone dioxygenase reaction producing 2-keto-4-
CC       methylthiobutyrate, while nickel-binding promotes an acireductone
CC       dioxygenase reaction producing 3-(methylsulfanyl)propanoate.
CC       {ECO:0000255|HAMAP-Rule:MF_03154};
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 5/6. {ECO:0000255|HAMAP-Rule:MF_03154}.
CC   -!- SUBUNIT: Monomer. Interacts with MMP14. {ECO:0000255|HAMAP-
CC       Rule:MF_03154}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03154}.
CC       Nucleus {ECO:0000255|HAMAP-Rule:MF_03154}. Cell membrane
CC       {ECO:0000255|HAMAP-Rule:MF_03154}; Peripheral membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_03154}; Cytoplasmic side {ECO:0000255|HAMAP-
CC       Rule:MF_03154}. Note=Localizes to the plasma membrane when complexed to
CC       MMP14. {ECO:0000255|HAMAP-Rule:MF_03154}.
CC   -!- SIMILARITY: Belongs to the acireductone dioxygenase (ARD) family.
CC       {ECO:0000255|HAMAP-Rule:MF_03154}.
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   RefSeq; XP_014967103.1; XM_015111617.1.
DR   AlphaFoldDB; F6QS54; -.
DR   SMR; F6QS54; -.
DR   STRING; 9544.ENSMMUP00000025585; -.
DR   Ensembl; ENSMMUT00000027353; ENSMMUP00000025585; ENSMMUG00000019471.
DR   Ensembl; ENSMMUT00000043782; ENSMMUP00000036770; ENSMMUG00000019471.
DR   GeneID; 722050; -.
DR   KEGG; mcc:722050; -.
DR   CTD; 55256; -.
DR   VEuPathDB; HostDB:ENSMMUG00000019471; -.
DR   VGNC; VGNC:69738; ADI1.
DR   eggNOG; KOG2107; Eukaryota.
DR   GeneTree; ENSGT00390000008195; -.
DR   HOGENOM; CLU_090154_0_1_1; -.
DR   InParanoid; F6QS54; -.
DR   OMA; RGQEDEW; -.
DR   OrthoDB; 1166094at2759; -.
DR   TreeFam; TF300231; -.
DR   UniPathway; UPA00904; UER00878.
DR   Proteomes; UP000006718; Chromosome 13.
DR   Bgee; ENSMMUG00000019471; Expressed in liver and 21 other tissues.
DR   ExpressionAtlas; F6QS54; baseline.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0010308; F:acireductone dioxygenase (Ni2+-requiring) activity; IEA:RHEA.
DR   GO; GO:0010309; F:acireductone dioxygenase [iron(II)-requiring] activity; IBA:GO_Central.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniRule.
DR   GO; GO:0006555; P:methionine metabolic process; IBA:GO_Central.
DR   CDD; cd02232; cupin_ARD; 1.
DR   Gene3D; 2.60.120.10; -; 1.
DR   HAMAP; MF_03154; Salvage_MtnD_euk; 1.
DR   InterPro; IPR004313; ARD.
DR   InterPro; IPR027496; ARD_euk.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   PANTHER; PTHR23418; PTHR23418; 1.
DR   Pfam; PF03079; ARD; 1.
DR   SUPFAM; SSF51182; SSF51182; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cell membrane; Cytoplasm; Dioxygenase; Iron;
KW   Membrane; Metal-binding; Methionine biosynthesis; Nickel; Nucleus;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..179
FT                   /note="Acireductone dioxygenase"
FT                   /id="PRO_0000414328"
FT   BINDING         88
FT                   /ligand="Fe(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29033"
FT                   /ligand_note="for iron-dependent acireductone dioxygenase
FT                   activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03154"
FT   BINDING         88
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_note="for nickel-dependent acireductone dioxygenase
FT                   activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03154"
FT   BINDING         90
FT                   /ligand="Fe(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29033"
FT                   /ligand_note="for iron-dependent acireductone dioxygenase
FT                   activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03154"
FT   BINDING         90
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_note="for nickel-dependent acireductone dioxygenase
FT                   activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03154"
FT   BINDING         94
FT                   /ligand="Fe(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29033"
FT                   /ligand_note="for iron-dependent acireductone dioxygenase
FT                   activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03154"
FT   BINDING         94
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_note="for nickel-dependent acireductone dioxygenase
FT                   activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03154"
FT   BINDING         133
FT                   /ligand="Fe(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29033"
FT                   /ligand_note="for iron-dependent acireductone dioxygenase
FT                   activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03154"
FT   BINDING         133
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_note="for nickel-dependent acireductone dioxygenase
FT                   activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03154"
SQ   SEQUENCE   179 AA;  21573 MW;  9A2E339FCB6A6A48 CRC64;
     MVQAWYMDDA PGDPRQPHRP DPDRPVGLEQ LRRLGVLYWK LDADKYENDP ELEKIRRERN
     YSWMDIITIC KDKLPNYEEK IKMFYEEHLH LDDEIRYILD GSGYFDVRDK EDKWIRIFME
     KGDMITLPAG IYHRFTVDEK NYAKAMRLFV GEPVWTAYNR PADHFEARGQ YMKFLAQTA
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024