Top Level Name

  ⌊ Superfamily (core) Radical SAM

    ⌊ Subgroup anaerobic coproporphyrinogen-III oxidase like

  ⌊ FunctionalDomain uncharacterized anaerobic coproporphyrinogen-III oxidase-like sequence (ID 431279)

Superfamily Assignment Evidence Code(s) IEA
This entry was last updated onJune 10, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Salmonella enterica subsp. enterica serovar Hvittingfoss str. A4-620 Taxon ID: 913073 353584167 EHC44351.1 (Genbank) URP

Sequence

Length of Enzyme (full-length): 226 | Length of Functional Domain: 225

1       10        20        30        40        50        60

MSEQQIDWDLALIQKYNYSGPRYTSYPTALEFSEDFEDAAFLQAVARYPERPLSLYVHIP
FCHKLCYFCGCNKIVTRQQHKADQYLDALEQEIRHRAPLFADRHVSQLHWGGGTPTYLNK
MQISRLMTLLRENFHFNTDAEISIEVDPREIELDVLDHLRAEGFNRLSMGVQDFNKEVQR
LVNREQDEEFIFALLNHARDIGFTSTNIDLIYGLPKQTPESFAFTL
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
62 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
66 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
69 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
62 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
66 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
69 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
1OLT Coproporphyrinogen Iii Oxidase (Hemn) From Escherichia Coli Is A Radical Sam Enzyme. Oxygen-Independent Coproporphyrinogen Iii Oxidase 131 2.07 S-Adenosylmethionine • Iron/Sulfur Cluster CSA • PDB • PDBSum
Percent identity and alignment length from the BLAST match of the Functional Domain sequence to the PDB sequence.
"Yes" indicates that a GI associated with this Functional Domain was mapped to the PDB ID via UniProtKB.

Curation History
Time Change Annotation Old Value New Value
Oct. 16, 2014, 7:03 a.m. update curation agent holliday setDomainBoundaries.py
June 12, 2015, 7:17 p.m. update curation agent setDomainBoundaries.py holliday
update curation agent holliday setDomainBoundaries.py
remove family assignment evidence code IEA -
remove family oxygen-independent coproporphyrinogen-III oxidase 1 (HemN-like) -
update name Oxygen-independent coproporphyrinogen-III oxidase 1 (HemN) uncharacterized anaerobic coproporphyrinogen-III oxidase-like sequence
update domain start position 1 2
EC number assigned by UniProtKB accession ID.