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Q31F42 (LIPA_THICR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lipoyl synthase

EC=2.8.1.8
Alternative name(s):
Lip-syn
Short name=LS
Lipoate synthase
Lipoic acid synthase
Sulfur insertion protein LipA
Gene names
Name:lipA
Ordered Locus Names:Tcr_1639
OrganismThiomicrospira crunogena (strain XCL-2) [Complete proteome] [HAMAP]
Taxonomic identifier317025 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaThiotrichalesPiscirickettsiaceaeThiomicrospira

Protein attributes

Sequence length316 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 By similarity. HAMAP-Rule MF_00206

Catalytic activity

Protein N(6)-(octanoyl)lysine + 2 sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine = protein N(6)-(lipoyl)lysine + 2 (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine. HAMAP-Rule MF_00206

Cofactor

Binds 2 4Fe-4S clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine By similarity.

Pathway

Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 2/2. HAMAP-Rule MF_00206

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_00206.

Sequence similarities

Belongs to the radical SAM superfamily. Lipoyl synthase family.

Sequence caution

The sequence ABB42231.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCytoplasm
   Ligand4Fe-4S
Iron
Iron-sulfur
Metal-binding
S-adenosyl-L-methionine
   Molecular functionTransferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processprotein lipoylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function4 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

lipoate synthase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 316316Lipoyl synthase HAMAP-Rule MF_00206
PRO_0000325319

Sites

Metal binding641Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding691Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding751Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding901Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding941Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding971Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q31F42 [UniParc].

Last modified March 18, 2008. Version 2.
Checksum: 2025EABFFB8E7A8E

FASTA31635,700
        10         20         30         40         50         60 
MKARNESMSK GEYKTKSLKN RPDPTQPKLK KPSWIKAKLP SAKHIGRVKE LKQVLREQGL 

        70         80         90        100        110        120 
NSVCEEASCP NLGECFGHGT ATFMIMGHIC TRKCPFCDVT HGRPNPLNQD EPRHLAKTIH 

       130        140        150        160        170        180 
AMNLNYVVIT SVDRDDLRDG GATHFKNCTQ AIRDKMPDIQ IETLVPDFRG RLTVALDILA 

       190        200        210        220        230        240 
QQAPDVLNHN LETVPRLYEE ARPGADYQAS LDLLKRFKQM VPETKTKSGL MVGLGETFDE 

       250        260        270        280        290        300 
ILQVMRDLRA HDVEMLTVGQ YLQPSDFHLA VQRYWTPEEF KQLEQAGMEM GFTHVASGPM 

       310 
VRSSYHADLQ AQGQFS 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000109 Genomic DNA. Translation: ABB42231.1. Different initiation.
RefSeqYP_391905.1. NC_007520.2.

3D structure databases

ProteinModelPortalQ31F42.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING317025.Tcr_1639.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB42231; ABB42231; Tcr_1639.
GeneID3761936.
KEGGtcx:Tcr_1639.
PATRIC23975352. VBIThiCru83387_1712.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0320.
HOGENOMHOG000235997.
KOK03644.
OrthoDBEOG6038ZS.
ProtClustDBPRK05481.

Enzyme and pathway databases

BioCycTCRU317025:GHE8-1682-MONOMER.
UniPathwayUPA00538; UER00593.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00206. Lipoyl_synth.
InterProIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
[Graphical view]
PANTHERPTHR10949. PTHR10949. 1 hit.
PfamPF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFPIRSF005963. Lipoyl_synth. 1 hit.
SMARTSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsTIGR00510. lipA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameLIPA_THICR
AccessionPrimary (citable) accession number: Q31F42
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 18, 2008
Last modified: February 19, 2014
This is version 61 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways