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B8F679 (LIPA_HAEPS) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 37. 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:HAPS_1235
OrganismHaemophilus parasuis serovar 5 (strain SH0165) [Complete proteome] [HAMAP]
Taxonomic identifier557723 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

Protein attributes

Sequence length320 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.

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 – 320320Lipoyl synthase HAMAP-Rule MF_00206
PRO_1000124634

Sites

Metal binding671Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding721Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding781Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding931Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding971Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1001Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
B8F679 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: EAA6B7722F2B6997

FASTA32036,193
        10         20         30         40         50         60 
MGTPFKMERG VKYRDAAKTS IIPVKNIDPN QELLKKPEWM KIKLPANSAK IESIKNGMRR 

        70         80         90        100        110        120 
HGLHSVCEEA SCPNLHECFN HGTATFMIMG AICTRRCPFC DVAHGKPLPL DKDEPKKLAE 

       130        140        150        160        170        180 
TIQDMKLKYV VITSVDRDDL PDRGAGHFAE CVKEIRALNP GIKIEILVPD FRGRVEQAIE 

       190        200        210        220        230        240 
ILKENPPDVF NHNLENVPRL YKEIRPGADY EWSLKLLKEF KAVFPDIPTK SGIMVGLGET 

       250        260        270        280        290        300 
NEEILQVMQD LRDHGVTMLT LGQYLQPSRH HLPVARYVHP TEFDMFREKA NEMGFEHAAC 

       310        320 
GPFVRSSYHA DLQASGGLVK 

« Hide

References

[1]"Complete genome sequence of Haemophilus parasuis SH0165."
Yue M., Yang F., Yang J., Bei W., Cai X., Chen L., Dong J., Zhou R., Jin M., Jin Q., Chen H.
J. Bacteriol. 191:1359-1360(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SH0165.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001321 Genomic DNA. Translation: ACL32831.1.
RefSeqYP_002475779.1. NC_011852.1.

3D structure databases

ProteinModelPortalB8F679.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING557723.HAPS_1235.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACL32831; ACL32831; HAPS_1235.
GeneID7278960.
KEGGhap:HAPS_1235.
PATRIC20194749. VBIHaePar127548_1221.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0320.
HOGENOMHOG000235997.
KOK03644.
OMAEEYVTPE.
OrthoDBEOG6038ZS.
ProtClustDBPRK05481.

Enzyme and pathway databases

BioCycHPAR557723:GH24-1235-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_HAEPS
AccessionPrimary (citable) accession number: B8F679
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: February 19, 2014
This is version 37 of the entry and version 1 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