Top Level Name

  ⌊ Superfamily (core) Radical SAM

    ⌊ Subgroup F420, menaquinone cofactor biosynthesis

  ⌊ menaquinone synthsis involved

     ⌊ Family aminofutalosine synthase (mqnE-like)

  ⌊ FunctionalDomain aminofutalosine synthase (ID 413420)

Superfamily Assignment Evidence Code(s) FSM PubMed:24083939
Family Assignment Evidence Code CFM PubMed:24083939
This entry was last updated onJune 10, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Thermus thermophilus Taxon ID: 274 499486258 WP_011172898.1 (RefSeq)
Thermus thermophilus HB8 Taxon ID: 300852 55980773 YP_144070.1 (RefSeq) URP
Thermus thermophilus HB27 Taxon ID: 262724 46196383 AAS80800.1 (Genbank) URP
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Uniprot

Protein NameAccessionEC Number Identifier
Aminodeoxyfutalosine synthase {ECO:0000255|HAMAP-Rule:MF_00993} Q5SK48 MQNE_THET8 (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 372 | Length of Functional Domain: 368

1       10        20        30        40        50        60

MRGIRDPRLIPIAEKVMEGKRLSFEDGLVLYQTKDLPTLMRLANLVRERKHGHKTYFVHS
IRVSQTNICYVGCTFCAFQRRFGEEGAWDWDVDEVVAWVKERYQPGLTEIHLTAGHHPKR
PFAYYLDLVRALKENFPGVQVKAWTAAEIHHFSKIARLPYREVLKALKEAGLDAMPGGGA
EIFAERVRRKIARAKVSAEGWLEIHRTAHELGIPTNATMLYGHIETLEERLDHMDRLRRL
QDETGGFMSFIPLAFQPDGNQLARELGKKEFTTGLDDLRNLAVARLYLDNFPHIKGYWAT
LTPELAQVSLDWGVTDVDGTLIEERIVHMAGSPTPQGLTKRELARIILMAGRIPVERDAL
YREVRVWDRVEA
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
69 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
73 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
76 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
69 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
73 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
76 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
Family CAR This EFD conserves 3/3 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
69 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
73 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA
76 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IEA

Catalyzed Reaction

aminodeoxyfutalosine synthase

+ + + + +
3-[(1-carboxylatovinyl)oxy]benzoate(2-)
76981		 S-adenosyl-L-methionine zwitterion
59789		 water
15377		 aminodeoxyfutalosinate
64286		 L-methionine zwitterion
57844		 hydrogencarbonate
17544		 hydron
15378

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

Curation History
Time Change Annotation Old Value New Value
May 14, 2014, 3:03 a.m. update curation agent holliday setDomainBoundaries.py
update domain end position 367 368
update domain start position 5 1
Oct. 15, 2016, 6:14 a.m. update curation agent setDomainBoundaries.py holliday
update curation agent holliday setDomainBoundaries.py
update subgroup F420, menaquinone cofactor biosynthesis menaquinone synthsis involved
EC number assigned by UniProtKB accession ID.