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Protein

Lipoyl synthase

Gene

lipA

Organism
Chlamydophila felis (strain Fe/C-56)
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 bindingi51 – 511Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi56 – 561Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi62 – 621Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi77 – 771Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi81 – 811Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi84 – 841Iron-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

BioCyciCFEL264202:GJCG-82-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:CF0080
OrganismiChlamydophila felis (strain Fe/C-56)
Taxonomic identifieri264202 [NCBI]
Taxonomic lineageiBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydophila
ProteomesiUP000001260: Chromosome

Subcellular locationi

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 – 312312Lipoyl synthasePRO_1000012207Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi264202.CF0080.

Structurei

3D structure databases

ProteinModelPortaliQ256D6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0320.
HOGENOMiHOG000235998.
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.

Q256D6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNEAPAEKQK PQQGKRFSER LPQWLRQVLP RGSVFTHTDA TLKRTGLATV
60 70 80 90 100
CEEALCPNRT HCWSRKTATY LALGDTCSRR CGFCNIDFSK NPLPPDPEEP
110 120 130 140 150
QKIAESAKAL QLKHIVLTMV ARDDLEDGGA SYLARIIHTL HQELPESTIE
160 170 180 190 200
VLASDFQGNV DALHVLLDSG LTIYNHNVET VERLTPVVRH KATYRRSLFM
210 220 230 240 250
LEQAAVYLPN LKIKSGIMVG LGEQESEVKQ TLKDLADHGV RIVTIGQYLR
260 270 280 290 300
PSRLHIPVKN YVTPETFDYY RSVGESLGLF VYAGPFVRSS FNADMVLHNL
310
QDKQSEIAKV PR
Length:312
Mass (Da):35,120
Last modified:April 18, 2006 - v1
Checksum:i03D605F8411B658D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP006861 Genomic DNA. Translation: BAE80852.1.
RefSeqiWP_011457637.1. NC_007899.1.
YP_514997.1. NC_007899.1.

Genome annotation databases

GeneIDi3958435.
KEGGicfe:CF0080.
PATRICi20203708. VBIChlFel51660_0084.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP006861 Genomic DNA. Translation: BAE80852.1.
RefSeqiWP_011457637.1. NC_007899.1.
YP_514997.1. NC_007899.1.

3D structure databases

ProteinModelPortaliQ256D6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi264202.CF0080.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi3958435.
KEGGicfe:CF0080.
PATRICi20203708. VBIChlFel51660_0084.

Phylogenomic databases

eggNOGiCOG0320.
HOGENOMiHOG000235998.
KOiK03644.
OMAiEEYVTPE.
OrthoDBiEOG6038ZS.

Enzyme and pathway databases

UniPathwayiUPA00538; UER00593.
BioCyciCFEL264202:GJCG-82-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: Fe/C-56.

Entry informationi

Entry nameiLIPA_CHLFF
AccessioniPrimary (citable) accession number: Q256D6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: April 18, 2006
Last modified: March 4, 2015
This is version 64 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

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.