Top Level Name

  ⌊ Superfamily (core) Radical SAM

    ⌊ Subgroup spore photoproduct lyase like

     ⌊ Family spore photoproduct lyase 1

  ⌊ FunctionalDomain Spore Photoproduct Lyase (ID 407121)

Superfamily Assignment Evidence Code(s) FSM PubMed:22761404
Family Assignment Evidence Code CFM PubMed:22761404
This entry was last updated onJune 10, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Geobacillus thermodenitrificans Taxon ID: 33940 500217645 WP_011887788.1 (RefSeq)
Geobacillus thermodenitrificans NG80-2 Taxon ID: 420246 134267500 ABO67695.1 (Genbank) URP

Uniprot

Protein NameAccessionEC Number Identifier
n/a A4IQU1 A4IQU1_GEOTN (TrEMBL)

Sequence

Length of Enzyme (full-length): 341 | Length of Functional Domain: 341

1       10        20        30        40        50        60

MKPFVPKLVYFEPEALSYPLGKELYEKFTQMGIKIRETTSHNQVRGIPGETELARYRNAK
STLVVGVRRTLKFDSSKPSAEYAIPLATGCMGHCHYCYLQTTLGSKPYIRVYVNLDDIFA
QAQKYINERAPEITRFEAACTSDIVGIDHLTHSLKKAIEFIGATDYGRLRFVTKYEHVDH
LLDARHNGKTRFRFSINSRYVINHFEPGTSSFDGRLAAARKVAGAGYKLGFVVAPIYRHE
GWERGYFELFQELARQLEGMDLSDLTFELIQHRFTKPAKRVIEQRYPKTRLDLDETKRKY
KWGRYGIGKYVYRDEEAKELEDTMRRYIEQFFPGAYVQYFT
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
90 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
94 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
97 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
Subgroup CAR This EFD conserves 4/4 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
90 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
94 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
97 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
98 Tyr (Y) side chain Hydrogen radical shuttle hydrogen relay -- reactant IEA
Family CAR This EFD conserves 5/5 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
90 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS PubMed:22761404
94 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS PubMed:22761404
97 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS PubMed:22761404
98 Tyr (Y) side chain Hydrogen radical shuttle hydrogen relay -- reactant ISS PubMed:22761404
140 Cys (C) side chain Hydrogen radical shuttle hydrogen relay -- reactant ISS PubMed:22761404

Catalyzed Reaction

spore photoproduct lyase

(5R)-5,6-dihydro-5-(thymidin-7-yl)thymidine (in double-helical DNA)
85625
Two thymine residues (in DNA)
81146

EC: 4.1.99.14 | IntEnz: 4.1.99.14 | Kegg: 4.1.99.14 | BioCyc: 4.1.99.14 | BRENDA: 4.1.99.14

Structures

PDB ID Title Molecule Name Number of
EFDs
Resolution (Å) Mutant? Het group Links
4FHD Spore Photoproduct Lyase Complexed With Dinucleoside Spore Photoproduct Spore Photoproduct Lyase 5 2.0 Iron/Sulfur Cluster
(4 more ⇓)
CSA • PDB • PDBSum
4FHC Spore Photoproduct Lyase Spore Photoproduct Lyase 5 2.2 Iron/Sulfur Cluster
(3 more ⇓)
CSA • PDB • PDBSum
4FHF Spore Photoproduct Lyase C140A Mutant With Dinucleoside Spore Photoproduct Spore Photoproduct Lyase 5 2.3 Yes Iron/Sulfur Cluster
(4 more ⇓)
CSA • PDB • PDBSum
4FHE Spore Photoproduct Lyase C140A Mutant Spore Photoproduct Lyase 5 2.0 Iron/Sulfur Cluster
(3 more ⇓)
CSA • PDB • PDBSum
4FHG Spore Photoproduct Lyase C140S Mutant Spore Photoproduct Lyase 5 2.0 Yes Iron/Sulfur Cluster
(3 more ⇓)
CSA • PDB • PDBSum
4K9R Spore Photoproduct Lyase Y98F Mutant Spore Photoproduct Lyase 5 2.3 Yes Iron/Sulfur Cluster
(2 more ⇓)
CSA • PDB • PDBSum
4RH1 Spore Photoproduct Lyase C140A/S76C Mutant With Bound Adomet And Dinucleoside Spore Photoproduct Spore Photoproduct Lyase 5 2.6 Yes Iron/Sulfur Cluster
(3 more ⇓)
CSA • PDB • PDBSum
4RH0 Spore Photoproduct Lyase C140A/S76C Mutant With Bound Adomet Spore Photoproduct Lyase 5 2.1 Yes [(3S)-3-Amino-4-Hydroxy-4-Oxo-Butyl]-[[(2S,3S,4R,5R)-5-(6-Aminopurin-9-Yl)-3,4-Dihydroxy-Oxolan-2-Yl]Methyl]-Methyl-Selanium
(3 more ⇓)
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
July 15, 2014, 5:55 a.m. update name uncharacterized Radical SAM superfamily sequence Spore Photoproduct Lyase
update superfamily assignment evidence code ISS FSM
Oct. 16, 2014, 6:12 a.m. update curation agent holliday setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.