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Protein

Lipoyl synthase

Gene

lipA

Organism
Treponema denticola (strain ATCC 35405 / CIP 103919 / DSM 14222)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.UniRule annotation

Catalytic activityi

Protein N(6)-(octanoyl)lysine + 2 sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + 2 reduced [2Fe-2S] ferredoxin = protein N(6)-(lipoyl)lysine + 2 (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine + 2 oxidized [2Fe-2S] ferredoxin.UniRule annotation

Cofactori

[4Fe-4S] clusterUniRule annotationNote: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi44 – 441Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi49 – 491Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi55 – 551Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi70 – 701Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi74 – 741Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi77 – 771Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-HAMAP
  2. lipoate synthase activity Source: UniProtKB-HAMAP
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. protein lipoylation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciTDEN243275:GJ7G-1601-MONOMER.
UniPathwayiUPA00538; UER00593.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipoyl synthaseUniRule annotation (EC:2.8.1.8UniRule annotation)
Alternative name(s):
Lip-synUniRule annotation
Short name:
LSUniRule annotation
Lipoate synthaseUniRule annotation
Lipoic acid synthaseUniRule annotation
Sulfur insertion protein LipAUniRule annotation
Gene namesi
Name:lipAUniRule annotation
Ordered Locus Names:TDE_1575
OrganismiTreponema denticola (strain ATCC 35405 / CIP 103919 / DSM 14222)
Taxonomic identifieri243275 [NCBI]
Taxonomic lineageiBacteriaSpirochaetesSpirochaetalesSpirochaetaceaeTreponema
ProteomesiUP000008212 Componenti: Chromosome

Subcellular locationi

  1. Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 290290Lipoyl synthasePRO_0000102374Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi243275.TDE1575.

Structurei

3D structure databases

ProteinModelPortaliP61199.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the radical SAM superfamily. Lipoyl synthase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0320.
KOiK03644.
OMAiEEYVTPE.
OrthoDBiEOG6038ZS.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00206. Lipoyl_synth.
InterProiIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
[Graphical view]
PANTHERiPTHR10949. PTHR10949. 1 hit.
PfamiPF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFiPIRSF005963. Lipoyl_synth. 1 hit.
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00510. lipA. 1 hit.

Sequencei

Sequence statusi: Complete.

P61199-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNFKAGFMTC NQRKPDWLKI KLPTGELSQE VSNTIKIHKL NTICTSGKCP
60 70 80 90 100
NQGECWRCGT ATFMICGNIC TRACKFCNVP TGCPLPLNPN EPMEIAQSVE
110 120 130 140 150
ALKLKHVVLT SVDRDDIKDF GASHWVKVIR AVKQKTPNVT MEVLIPDFQG
160 170 180 190 200
HEDLVSMIIE AKPEVISHNL ETVRRLSPHV RSRATYDTSL KVLKQIADSG
210 220 230 240 250
LVCKSGIMLG LGETRAEILE TMDDLRKINC KVMTIGQYLR PSIKNIEVKE
260 270 280 290
YVRPEVFEEY KQIGLEKGFS FVESGPLVRS SYHAEKHVLS
Length:290
Mass (Da):32,592
Last modified:May 10, 2004 - v1
Checksum:i5FF6BFA727192040
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017226 Genomic DNA. Translation: AAS12092.1.
RefSeqiNP_972181.1. NC_002967.9.
WP_010957001.1. NC_002967.9.

Genome annotation databases

EnsemblBacteriaiAAS12092; AAS12092; TDE_1575.
GeneIDi2739325.
KEGGitde:TDE1575.
PATRICi20525312. VBITreDen445_1504.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017226 Genomic DNA. Translation: AAS12092.1.
RefSeqiNP_972181.1. NC_002967.9.
WP_010957001.1. NC_002967.9.

3D structure databases

ProteinModelPortaliP61199.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243275.TDE1575.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAS12092; AAS12092; TDE_1575.
GeneIDi2739325.
KEGGitde:TDE1575.
PATRICi20525312. VBITreDen445_1504.

Phylogenomic databases

eggNOGiCOG0320.
KOiK03644.
OMAiEEYVTPE.
OrthoDBiEOG6038ZS.

Enzyme and pathway databases

UniPathwayiUPA00538; UER00593.
BioCyciTDEN243275:GJ7G-1601-MONOMER.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00206. Lipoyl_synth.
InterProiIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
[Graphical view]
PANTHERiPTHR10949. PTHR10949. 1 hit.
PfamiPF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFiPIRSF005963. Lipoyl_synth. 1 hit.
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00510. lipA. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 35405 / CIP 103919 / DSM 14222.

Entry informationi

Entry nameiLIPA_TREDE
AccessioniPrimary (citable) accession number: P61199
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 10, 2004
Last modified: April 29, 2015
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.