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SHDD_SEDHY
ID   SHDD_SEDHY              Reviewed;          68 AA.
AC   Q4R102;
DT   25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 21.
DE   RecName: Full=Protein ShdD {ECO:0000305|PubMed:24193968};
DE   AltName: Full=Phenolic acid decarboxylase subunit D {ECO:0000303|PubMed:24193968};
DE            Short=PAD {ECO:0000303|PubMed:24193968};
GN   Name=shdD {ECO:0000303|PubMed:15979273};
OS   Sedimentibacter hydroxybenzoicus (Clostridium hydroxybenzoicum).
OC   Bacteria; Firmicutes; Tissierellia; Sedimentibacter.
OX   NCBI_TaxID=29345;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 51151 / DSM 7310 / JW/Z-1 {ECO:0000312|EMBL:AAY67851.1};
RX   PubMed=7744052; DOI=10.1111/j.1432-1033.1995.tb20440.x;
RA   He Z., Wiegel J.;
RT   "Purification and characterization of an oxygen-sensitive reversible 4-
RT   hydroxybenzoate decarboxylase from Clostridium hydroxybenzoicum.";
RL   Eur. J. Biochem. 229:77-82(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 51151 / DSM 7310 / JW/Z-1 {ECO:0000312|EMBL:AAY67851.1};
RX   PubMed=10438791; DOI=10.1128/jb.181.16.5119-5122.1999;
RA   Huang J., He Z., Wiegel J.;
RT   "Cloning, characterization, and expression of a novel gene encoding a
RT   reversible 4-hydroxybenzoate decarboxylase from Clostridium
RT   hydroxybenzoicum.";
RL   J. Bacteriol. 181:5119-5122(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 51151 / DSM 7310 / JW/Z-1 {ECO:0000312|EMBL:AAY67851.1};
RX   PubMed=12054241; DOI=10.1099/00207713-52-3-801;
RA   Breitenstein A., Wiegel J., Haertig C., Weiss N., Andreesen J.R.,
RA   Lechner U.;
RT   "Reclassification of Clostridium hydroxybenzoicum as Sedimentibacter
RT   hydroxybenzoicus gen. nov., comb. nov., and description of Sedimentibacter
RT   saalensis sp. nov..";
RL   Int. J. Syst. Evol. Microbiol. 52:801-807(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 51151 / DSM 7310 / JW/Z-1 {ECO:0000312|EMBL:AAY67851.1};
RX   PubMed=15979273; DOI=10.1016/j.ygeno.2005.05.002;
RA   Lupa B., Lyon D., Gibbs M.D., Reeves R.A., Wiegel J.;
RT   "Distribution of genes encoding the microbial non-oxidative reversible
RT   hydroxyarylic acid decarboxylases/phenol carboxylases.";
RL   Genomics 86:342-351(2005).
RN   [5]
RP   FUNCTION, AND INDUCTION.
RC   STRAIN=ATCC 51151 / DSM 7310 / JW/Z-1;
RX   PubMed=24193968; DOI=10.1007/bf02543871;
RA   Zhang X., Wiegel J.;
RT   "Isolation and partial characterization of a Clostridium species
RT   transforming para-hydroxybenzoate and 3,4-dihydroxybenzoate and producing
RT   phenols as the final transformation products.";
RL   Microb. Ecol. 20:103-121(1990).
CC   -!- FUNCTION: Involved in the non-oxidative decarboxylation and
CC       detoxification of phenolic derivatives under anaerobic conditions,
CC       however the precise biochemical function of ShdD in metabolism of
CC       phenolic acid is unknown. {ECO:0000269|PubMed:15979273,
CC       ECO:0000269|PubMed:24193968}.
CC   -!- INDUCTION: By 4-hydroxybenzoate and 3,4-dihydroxybenzoate.
CC       {ECO:0000305|PubMed:24193968}.
CC   -!- MISCELLANEOUS: It is not known, if phenolic acid decarboxylase forms a
CC       complex composed of ShdB, ShdC and ShdD. The term subunit is often used
CC       in reference to the operon, however there is no experimental evidence
CC       to prove the existence of the complex. {ECO:0000305}.
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DR   EMBL; AF128880; AAY67851.1; -; Genomic_DNA.
DR   PDB; 7AE4; X-ray; 3.31 A; a/b/c/d/e/f=1-68.
DR   PDB; 7AE5; X-ray; 2.19 A; a/b/c/d/e/f=1-68.
DR   PDB; 7AE7; X-ray; 2.66 A; a/b/c/d/e/f=1-58.
DR   PDBsum; 7AE4; -.
DR   PDBsum; 7AE5; -.
DR   PDBsum; 7AE7; -.
DR   AlphaFoldDB; Q4R102; -.
DR   SMR; Q4R102; -.
DR   BRENDA; 4.1.1.61; 5658.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   3D-structure; Aromatic hydrocarbons catabolism; Detoxification.
FT   CHAIN           1..68
FT                   /note="Protein ShdD"
FT                   /id="PRO_0000444038"
FT   TURN            4..6
FT                   /evidence="ECO:0007829|PDB:7AE5"
FT   STRAND          11..16
FT                   /evidence="ECO:0007829|PDB:7AE5"
FT   STRAND          24..28
FT                   /evidence="ECO:0007829|PDB:7AE5"
FT   TURN            29..31
FT                   /evidence="ECO:0007829|PDB:7AE5"
FT   STRAND          34..36
FT                   /evidence="ECO:0007829|PDB:7AE5"
FT   HELIX           45..47
FT                   /evidence="ECO:0007829|PDB:7AE5"
FT   HELIX           51..55
FT                   /evidence="ECO:0007829|PDB:7AE5"
FT   STRAND          59..61
FT                   /evidence="ECO:0007829|PDB:7AE5"
SQ   SEQUENCE   68 AA;  7788 MW;  3FC64FEAD99B8997 CRC64;
     MKCHRCGSDN VRKMVDSPVG DAWEVYVCEK CCYSWRSTEN PVVMEKFKLD DNKIANMGVI
     PPIPPLKK
 
 
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