Top Level Name

  ⌊ Superfamily (core) Radical SAM

    ⌊ Subgroup organic radical-activating enzymes

     ⌊ Family 4-hydroxyphenylacetate decarboxylase activase

  ⌊ FunctionalDomain 4-hydroxyphenylacetate decarboxylase activating enzyme (ID 380987)

Superfamily Assignment Evidence Code(s) ISS
Family Assignment Evidence Code CFM PubMed:16878993 PubMed:15153112
This entry was last updated onJune 10, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Clostridium difficile Taxon ID: 1496 75392923 URP
Clostridium difficile ATCC 9689 Taxon ID: 1121308 28300943 URP

Uniprot

Protein NameAccessionEC Number Identifier
4-hydroxyphenylacetate decarboxylase activating enzyme {ECO:0000303|PubMed:16878993} Q84F14 1.97.1.- HPDA_CLODI (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 316 | Length of Functional Domain: 316

1       10        20        30        40        50        60

MSSQKQLEGMIFDVQSFSVHDGPGCRTTVFLNGCPLSCKWCANPESWTVRPHMMFSELSC
QYENGCTVCHGKCKNGALSFNLDNKPVIDWNICKDCESFECVNSCYYNAFKLCAKPYTVD
ELVQVIKRDSNNWRSNGGVTFSGGEPLLQHEFLHEVLLKCHEVNVHTAIETSACVSNEVF
NKIFNDIDFAFIDIKHMDREKHKEQTGVYNDLILENISNLANSDWNGRLVLRVPVISGFN
DSDENISDIISFMHKNNLVEINLLPFHRLGESKWTQLGKEYEYSDKGDVDEGHLEELQDI
FLDNGIACYVGHVTAF
This shows the full-length sequence of the enzyme. The region of the functional domain is highlighted in black letters, while the residual residues are shown in grey. The Superfamily domain, when present, is shown using underlining. In many cases the functional domain is the full-length sequence.
Conserved catalytic residues (as determined by automated alignment to family, subgroup, or superfamily HMMs) are shown with teal highlighting . Conserved catalytic residues which do not matched the Conserved Alignment Residue are shown with maroon highlighting . Information regarding their function can be found in the Conserved Residues section below.
FASTA formatted full-length sequence.
BLAST this sequence against SFLD.
Scan SFLD-HMMs with this sequence.

Conserved Residues
Superfamily CAR This EFD conserves 3/3 Superfamily-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
34 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
38 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
41 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
Subgroup CAR This EFD conserves 3/3 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
34 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
38 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
41 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
Family CAR This EFD conserves 3/3 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
34 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
38 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
41 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS

Catalyzed Reaction

[4-hydroxyphenylacetate decarboxylase]-activating enzyme

+ + + + +
S-adenosyl-L-methioninate
67040		 [4-hydroxyphenylacetate decarboxylase]-glycine residue
29947		 1,5-dihydroflavin
62787		 L-methionine zwitterion
57844		 5'-deoxyadenosine
17319		 semiquinone
15817		 [4-hydroxyphenylacetate decarboxylase]-glycine radical
10175

EC: 1.97.1.- | IntEnz: 1.97.1.- | Kegg: 1.97.1.- | BioCyc: 1.97.1.- | BRENDA: 1.97.1.- |

Curation History
Time Change Annotation Old Value New Value
Oct. 16, 2014, 5:18 a.m. update curation agent holliday setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.