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MTND_SORC5
ID   MTND_SORC5              Reviewed;         180 AA.
AC   A9FCY0;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Acireductone dioxygenase {ECO:0000255|HAMAP-Rule:MF_01682};
DE   AltName: Full=1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase {ECO:0000255|HAMAP-Rule:MF_01682};
DE            Short=DHK-MTPene dioxygenase {ECO:0000255|HAMAP-Rule:MF_01682};
DE   AltName: Full=Acireductone dioxygenase (Fe(2+)-requiring) {ECO:0000255|HAMAP-Rule:MF_01682};
DE            Short=ARD' {ECO:0000255|HAMAP-Rule:MF_01682};
DE            Short=Fe-ARD {ECO:0000255|HAMAP-Rule:MF_01682};
DE            EC=1.13.11.54 {ECO:0000255|HAMAP-Rule:MF_01682};
DE   AltName: Full=Acireductone dioxygenase (Ni(2+)-requiring) {ECO:0000255|HAMAP-Rule:MF_01682};
DE            Short=ARD {ECO:0000255|HAMAP-Rule:MF_01682};
DE            Short=Ni-ARD {ECO:0000255|HAMAP-Rule:MF_01682};
DE            EC=1.13.11.53 {ECO:0000255|HAMAP-Rule:MF_01682};
GN   Name=mtnD {ECO:0000255|HAMAP-Rule:MF_01682}; OrderedLocusNames=sce1550;
OS   Sorangium cellulosum (strain So ce56) (Polyangium cellulosum (strain So
OS   ce56)).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; Sorangiineae;
OC   Polyangiaceae; Sorangium.
OX   NCBI_TaxID=448385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=So ce56;
RX   PubMed=17965706; DOI=10.1038/nbt1354;
RA   Schneiker S., Perlova O., Kaiser O., Gerth K., Alici A., Altmeyer M.O.,
RA   Bartels D., Bekel T., Beyer S., Bode E., Bode H.B., Bolten C.J.,
RA   Choudhuri J.V., Doss S., Elnakady Y.A., Frank B., Gaigalat L., Goesmann A.,
RA   Groeger C., Gross F., Jelsbak L., Jelsbak L., Kalinowski J., Kegler C.,
RA   Knauber T., Konietzny S., Kopp M., Krause L., Krug D., Linke B., Mahmud T.,
RA   Martinez-Arias R., McHardy A.C., Merai M., Meyer F., Mormann S.,
RA   Munoz-Dorado J., Perez J., Pradella S., Rachid S., Raddatz G., Rosenau F.,
RA   Rueckert C., Sasse F., Scharfe M., Schuster S.C., Suen G.,
RA   Treuner-Lange A., Velicer G.J., Vorholter F.-J., Weissman K.J., Welch R.D.,
RA   Wenzel S.C., Whitworth D.E., Wilhelm S., Wittmann C., Bloecker H.,
RA   Puehler A., Mueller R.;
RT   "Complete genome sequence of the myxobacterium Sorangium cellulosum.";
RL   Nat. Biotechnol. 25:1281-1289(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.
CC       {ECO:0000255|HAMAP-Rule:MF_01682}.
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_01682};
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_01682};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01682};
CC       Note=Binds 1 Fe(2+) cation per monomer. {ECO:0000255|HAMAP-
CC       Rule:MF_01682};
CC   -!- COFACTOR:
CC       Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01682};
CC       Note=Binds 1 nickel ion per monomer. {ECO:0000255|HAMAP-Rule:MF_01682};
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_01682}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01682}.
CC   -!- SIMILARITY: Belongs to the acireductone dioxygenase (ARD) family.
CC       {ECO:0000255|HAMAP-Rule:MF_01682}.
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DR   EMBL; AM746676; CAN91708.1; -; Genomic_DNA.
DR   RefSeq; WP_012234185.1; NC_010162.1.
DR   AlphaFoldDB; A9FCY0; -.
DR   SMR; A9FCY0; -.
DR   STRING; 448385.sce1550; -.
DR   EnsemblBacteria; CAN91708; CAN91708; sce1550.
DR   KEGG; scl:sce1550; -.
DR   eggNOG; COG1791; Bacteria.
DR   HOGENOM; CLU_125400_0_0_7; -.
DR   OMA; TTHWFDM; -.
DR   OrthoDB; 1964262at2; -.
DR   BioCyc; SCEL448385:SCE_RS07995-MON; -.
DR   UniPathway; UPA00904; UER00878.
DR   Proteomes; UP000002139; Chromosome.
DR   GO; GO:0010308; F:acireductone dioxygenase (Ni2+-requiring) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0010309; F:acireductone dioxygenase [iron(II)-requiring] activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016151; F:nickel cation 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   CDD; cd02232; cupin_ARD; 1.
DR   Gene3D; 2.60.120.10; -; 1.
DR   HAMAP; MF_01682; Salvage_MtnD; 1.
DR   InterPro; IPR004313; ARD.
DR   InterPro; IPR023956; ARD_bac.
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; Dioxygenase; Iron; Metal-binding;
KW   Methionine biosynthesis; Nickel; Oxidoreductase; Reference proteome.
FT   CHAIN           1..180
FT                   /note="Acireductone dioxygenase"
FT                   /id="PRO_0000359231"
FT   BINDING         96
FT                   /ligand="Fe(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29033"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01682"
FT   BINDING         96
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01682"
FT   BINDING         98
FT                   /ligand="Fe(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29033"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01682"
FT   BINDING         98
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01682"
FT   BINDING         102
FT                   /ligand="Fe(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29033"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01682"
FT   BINDING         102
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01682"
FT   BINDING         140
FT                   /ligand="Fe(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29033"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01682"
FT   BINDING         140
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01682"
FT   SITE            95
FT                   /note="May play a role in metal incorporation in vivo"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01682"
FT   SITE            101
FT                   /note="May play a role in transmitting local conformational
FT                   changes"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01682"
FT   SITE            104
FT                   /note="Important to generate the dianion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01682"
SQ   SEQUENCE   180 AA;  20351 MW;  6B31D768ACECB3A8 CRC64;
     MSRLRVYRES DPTRADEYTT LEDIARVAAE AQIRFERWSA ERPLPPGAAQ EQVLEAYAGP
     VKQLSEACGF VTADVVSVSP GTPNHPELRR KFLDEHIHTE DEARFFVEGR GLFCIHHGER
     VLSFLVEKGD LISVPAGTRH WFDMGPEPSF TCIRWFSDPK GWVAEHTGSD IASRFPRLEA
 
 
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