Top Level Name

  ⌊ Superfamily (core) Radical SAM

    ⌊ Subgroup 7-carboxy-7-deazaguanine synthase like

     ⌊ Family 7-carboxy-7-deazaguanine synthase, Cx14CxxC type

  ⌊ FunctionalDomain 7-carboxy-7-deazaguanine synthase, CX14CX2C type (ID 436568)

Superfamily Assignment Evidence Code(s) ISS PubMed:24362703
Family Assignment Evidence Code CFM PubMed:24362703
This entry was last updated onJune 10, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Burkholderia multivorans Taxon ID: 87883 501170460 WP_012214363.1 (RefSeq) URP
Burkholderia multivorans ATCC 17616 Taxon ID: 395019 160343713 ABX16799.1 (Genbank) URP
Burkholderia multivorans ATCC 17616 Taxon ID: 395019 189333024 URP

Uniprot

Protein NameAccessionEC Number Identifier
7-carboxy-7-deazaguanine synthase {ECO:0000255|HAMAP-Rule:MF_00917, ECO:0000303|PubMed:24362703} A0A0H3KB22 QUEE_BURM1 (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 210 | Length of Functional Domain: 210

1       10        20        30        40        50        60

MTYAVKEIFYTLQGEGANAGRPAVFCRFAGCNLWSGREEDRAQAVCRFCDTDFVGTDGEN
GGKFKDADALVATIAGLWPAGEAHRFVVCTGGEPMLQLDQPLVDALHAAGFGIAIETNGS
LPVLESIDWICVSPKADAPLVVTKGNELKVVIPQDNQRLADYAKLDFEYFLVQPMDGPSR
DLNTKLAIDWCKRHPQWRLSMQTHKYLNIP
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 2/3 Superfamily-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
46 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
49 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
Subgroup CAR This EFD conserves 5/5 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
31 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
46 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
49 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
50 Asp (D) side chain Activates Mg(II) binding residue activation -- spectator IEA
51 Thr (T) side chain Binds Mg(II) ion metal ligand -- binding IEA
Family CAR This EFD conserves 8/8 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
25 Phe (F) side chain Binds substrate substrate binding -- binding ICS PubMed:24362703
31 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ICS PubMed:24362703
46 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ICS PubMed:24362703
49 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ICS PubMed:24362703
50 Asp (D) side chain Activates metal binding Thr activation -- spectator ICS PubMed:24362703
51 Thr (T) side chain Binds Mg(II) ion metal ligand -- binding ICS PubMed:24362703
116 Glu (E) side chain General acid/base proton relay -- reactant ICS PubMed:24362703
204 His (H) side chain Binds substrate substrate binding -- binding ICS PubMed:24362703

Catalyzed Reaction

7-carboxy-7-deazaguanine synthase

+ +
5,6,7,8-tetrahydropterin-6-carboxylate
61032		 hydron
15378		 7-carboxylato-7-deazaguanine
61036		 ammonium
28938

EC: 4.3.99.3 | IntEnz: 4.3.99.3 | Kegg: 4.3.99.3 | BioCyc: 4.3.99.3 | BRENDA: 4.3.99.3

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
4NJK Crystal Structure Of Quee From Burkholderia Multivorans In Complex With Adomet, 7-Carboxy-7-Deazaguanine, And Mg2+ 7-Carboxy-7-Deazaguanine Synthase 14 1.91 Iron/Sulfur Cluster
(5 more ⇓) 		CSA • PDB • PDBSum
4NJJ Crystal Structure Of Quee From Burkholderia Multivorans In Complex With Adomet, 6-Carboxy-5,6,7,8-Tetrahydropterin, And Manganese(Ii) 7-Carboxy-7-Deazaguanine Synthase 14 2.7 Iron/Sulfur Cluster
(3 more ⇓) 		CSA • PDB • PDBSum
4NJI Crystal Structure Of Quee From Burkholderia Multivorans In Complex With Adomet, 6-Carboxy-5,6,7,8-Tetrahydropterin, And Mg2+ 7-Carboxy-7-Deazaguanine Synthase 14 2.2 Iron/Sulfur Cluster
(5 more ⇓) 		CSA • PDB • PDBSum
4NJH Crystal Structure Of Quee From Burkholderia Multivorans In Complex With Adomet And 6-Carboxy-5,6,7,8-Tetrahydropterin 7-Carboxy-7-Deazaguanine Synthase 14 1.9 Iron/Sulfur Cluster
(4 more ⇓) 		CSA • PDB • PDBSum
4NJG Crystal Structure Of Quee From Burkholderia Multivorans In Complex With Adomet And 6-Carboxypterin 7-Carboxy-7-Deazaguanine Synthase 14 2.6 Iron/Sulfur Cluster
(2 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
Oct. 16, 2014, 7:13 a.m. update curation agent holliday setDomainBoundaries.py
EC number assigned by UniProtKB accession ID.