Top Level Name

  ⌊ Superfamily (core) Radical SAM

    ⌊ Subgroup lipoyl synthase like

     ⌊ Family lipoyl synthase

  ⌊ FunctionalDomain Lipoyl synthase (ID 280037)

Superfamily Assignment Evidence Code(s) FSM PubMed:11106496 PubMed:14700636 PubMed:15157071 PubMed:21370834 PubMed:18307109 PubMed:15362861 PubMed:15740115 PubMed:15112987 PubMed:22773649
Family Assignment Evidence Code CFM PubMed:11106496 PubMed:14700636 PubMed:15157071
This entry was last updated onJune 10, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Escherichia coli O157:H7 str. Sakai Taxon ID: 386585 15829920 NP_308693.1 (RefSeq)
Escherichia coli str. K-12 substr. MG1655 Taxon ID: 511145 16128611 NP_415161.1 (RefSeq) URP
Shigella flexneri 2a str. 301 Taxon ID: 198214 24112072 NP_706582.1 (RefSeq)
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Uniprot

Protein NameAccessionEC Number Identifier
Lipoyl synthase {ECO:0000255|HAMAP-Rule:MF_00206} A7ZJ15 LIPA_ECO24 (Swiss-Prot)
Lipoyl synthase {ECO:0000255|HAMAP-Rule:MF_00206} B7UKR9 LIPA_ECO27 (Swiss-Prot)
Lipoyl synthase {ECO:0000255|HAMAP-Rule:MF_00206} B7MFQ1 LIPA_ECO45 (Swiss-Prot)
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Sequence

Length of Enzyme (full-length): 321 | Length of Functional Domain: 297

1       10        20        30        40        50        60

MSKPIVMERGVKYRDADKMALIPVKNVATEREALLRKPEWMKIKLPADSTRIQGIKAAMR
KNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPVAPDANEPVKLA
QTIADMALRYVVITSVDRDDLRDGGAQHFADCITAIREKSPQIKIETLVPDFRGRMDRAL
DILTATPPDVFNHNLENVPRIYRQVRPGADYNWSLKLLERFKEAHPEIPTKSGLMVGLGE
TNEEIIEVMRDLRRHGVTMLTLGQYLQPSRHHLPVQRYVSPDEFDEMKAEALAMGFTHAA
CGPFVRSSYHADLQAKGMEVK
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
94 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
98 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
101 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding ISS
Subgroup CAR This EFD conserves 6/6 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
68 Cys (C) side chain Binds [4Fe-4S] cluster cofactor binding -- binding IDA PubMed:15362861
73 Cys (C) side chain Binds [4Fe-4S] cluster cofactor binding -- binding IDA PubMed:15362861
79 Cys (C) side chain Binds [4Fe-4S] cluster cofactor binding -- binding IDA PubMed:15362861
94 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IDA PubMed:15362861
98 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IDA PubMed:15362861
101 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IDA PubMed:15362861
Family CAR This EFD conserves 6/6 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
68 Cys (C) side chain Binds [4Fe-4S] cluster cofactor binding -- binding IDA PubMed:15362861
73 Cys (C) side chain Binds [4Fe-4S] cluster cofactor binding -- binding IDA PubMed:15362861
79 Cys (C) side chain Binds [4Fe-4S] cluster cofactor binding -- binding IDA PubMed:15362861
94 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IDA PubMed:15362861
98 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IDA PubMed:15362861
101 Cys (C) side chain Binds [4Fe-4S]-AdoMet cluster cofactor binding -- binding IDA PubMed:15362861

Catalyzed Reaction

lipoyl synthase

+ 2 + + 2 2 + 2 + + 2 + 2
thiol group
29917		 S-adenosyl-L-methionine zwitterion
59789		 N(6)-octanoyl-L-lysine residue
78809		 di-mu-sulfido-diiron(1+)
33738		 H group
64428		 5'-deoxyadenosine
17319		 N(6)-[(R)-lipoyl]-L-lysine residue
83099		 L-methionine zwitterion
57844		 di-mu-sulfido-diiron(2+)
33737

EC: 2.8.1.8 | IntEnz: 2.8.1.8 | Kegg: 2.8.1.8 | BioCyc: 2.8.1.8 | BRENDA: 2.8.1.8

Curation History
Time Change Annotation Old Value New Value
May 14, 2014, 3 a.m. update curation agent mischel setDomainBoundaries.py
update domain start position 1 3
July 15, 2014, 3:58 a.m. update domain end position 321 320
update domain start position 3 25
May 11, 2015, 8:43 a.m. update curation agent setDomainBoundaries.py holliday
update curation agent holliday setDomainBoundaries.py
update family assignment evidence code CFM,IES CFM
Oct. 15, 2016, 3:51 a.m. update domain start position 25 24
EC number assigned by UniProtKB accession ID.