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Protein

Lipoyl synthase

Gene

lipA

Organism
Histophilus somni (strain 129Pt) (Haemophilus somnus)
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 bindingi67 – 671Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi72 – 721Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi78 – 781Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi93 – 931Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi97 – 971Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi100 – 1001Iron-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

BioCyciHSOM205914:GJ7V-329-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:HS_0315
OrganismiHistophilus somni (strain 129Pt) (Haemophilus somnus)
Taxonomic identifieri205914 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHistophilus
ProteomesiUP000001970 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 – 320320Lipoyl synthasePRO_0000325261Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi205914.HS_0315.

Structurei

3D structure databases

ProteinModelPortaliQ0I1H8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0320.
HOGENOMiHOG000235997.
KOiK03644.
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.

Q0I1H8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTPFKMERG VKYRDAAKTS IIPVKNIDPN QELLKKPEWM KIKLPANSAK
60 70 80 90 100
INSIKNGMRR HGLHSVCEEA SCPNLHECFN HGTATFMILG AICTRRCPFC
110 120 130 140 150
DVAHGKPLPP DPDEPKKLAE TIQDMKLRYV VITSVDRDDL PDRGAGHFAE
160 170 180 190 200
CVKEIRKLNP GIKIEILVPD FRGRIEQALE KLKDNPPDVF NHNLENVPRL
210 220 230 240 250
YREIRPGADY NWSLKLLKEF KTIFPHIPTK SGIMVGLGET NEEILQVMQD
260 270 280 290 300
LRDNGVTMLT LGQYLQPSRH HLPVARYVPP EEFDDFRDKA EKMGFEHAAC
310 320
GPFVRSSYHA DLQASGGLVK
Length:320
Mass (Da):36,285
Last modified:March 18, 2008 - v2
Checksum:iD026E1797515E174
GO

Sequence cautioni

The sequence ABI24593.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000436 Genomic DNA. Translation: ABI24593.1. Different initiation.
RefSeqiYP_718523.1. NC_008309.1.

Genome annotation databases

EnsemblBacteriaiABI24593; ABI24593; HS_0315.
KEGGihso:HS_0315.
PATRICi20280561. VBIHaeSom53361_0331.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000436 Genomic DNA. Translation: ABI24593.1. Different initiation.
RefSeqiYP_718523.1. NC_008309.1.

3D structure databases

ProteinModelPortaliQ0I1H8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi205914.HS_0315.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABI24593; ABI24593; HS_0315.
KEGGihso:HS_0315.
PATRICi20280561. VBIHaeSom53361_0331.

Phylogenomic databases

eggNOGiCOG0320.
HOGENOMiHOG000235997.
KOiK03644.
OrthoDBiEOG6038ZS.

Enzyme and pathway databases

UniPathwayiUPA00538; UER00593.
BioCyciHSOM205914:GJ7V-329-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. "Complete genome sequence of Haemophilus somnus (Histophilus somni) strain 129Pt and comparison to Haemophilus ducreyi 35000HP and Haemophilus influenzae Rd."
    Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O., Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N., Xie G., Inzana T.J.
    J. Bacteriol. 189:1890-1898(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 129Pt.

Entry informationi

Entry nameiLIPA_HISS1
AccessioniPrimary (citable) accession number: Q0I1H8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 18, 2008
Last modified: April 1, 2015
This is version 65 of the entry and version 2 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.