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P44463 (LIPA_HAEIN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:HI_0026
OrganismHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) [Reference proteome] [HAMAP]
Taxonomic identifier71421 [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 By similarity 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
Reference 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_0000102320

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
P44463 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 7D4C4136925450C6

FASTA32036,197
        10         20         30         40         50         60 
MSTPFKMERG VKYRDAAKTS IIPVKNIDPN QDLLKKPEWM KIKLPASSAK IESIKNGMRR 

        70         80         90        100        110        120 
HGLHSVCEEA SCPNLHECFN HGTATFMILG AICTRRCPFC DVAHGKPLPP DPEEPQKLAE 

       130        140        150        160        170        180 
TIQDMKLKYV VITSVDRDDL PDRGAGHFSE CVKAVRELNP NIKIEILVPD FRGRITQALE 

       190        200        210        220        230        240 
KLKDNPPDVF NHNLENVPRL YKEIRPGADY EWSLKLLREF KEIFPNIPTK SGLMVGLGET 

       250        260        270        280        290        300 
NEEILQVMQD LRDNGVTMLT LGQYLQPSRH HLPVARYVPP TEFDEFRDKA NEMGFEHAAC 

       310        320 
GPFVRSSYHA DLQASGGLVK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L42023 Genomic DNA. Translation: AAC21704.1.
PIRG64043.
RefSeqNP_438199.1. NC_000907.1.

3D structure databases

ProteinModelPortalP44463.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING71421.HI0026.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC21704; AAC21704; HI_0026.
GeneID950923.
KEGGhin:HI0026.
PATRIC20188503. VBIHaeInf48452_0026.

Phylogenomic databases

eggNOGCOG0320.
KOK03644.
OMAEEYVTPE.
OrthoDBEOG6038ZS.
ProtClustDBPRK05481.

Enzyme and pathway databases

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_HAEIN
AccessionPrimary (citable) accession number: P44463
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: February 19, 2014
This is version 103 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

Haemophilus influenzae

Haemophilus influenzae (strain Rd): entries and gene names