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Q7V6S0 (LIPA2_PROMM) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 75. 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 2

EC=2.8.1.8
Alternative name(s):
Lip-syn 2
Lipoate synthase 2
Lipoic acid synthase 2
Sulfur insertion protein lipA2
Gene names
Name:lipA2
Synonyms:lipA
Ordered Locus Names:PMT_1076
OrganismProchlorococcus marinus (strain MIT 9313) [Complete proteome] [HAMAP]
Taxonomic identifier74547 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length306 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 – 306306Lipoyl synthase 2 HAMAP-Rule MF_00206
PRO_0000102339

Sites

Metal binding491Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding541Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding601Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding751Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding791Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding821Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7V6S0 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: BD8D731A6BCBF94C

FASTA30634,003
        10         20         30         40         50         60 
MSSTHRPTQY SSILPAERLP EWLRRPIGSV SQLEQMQQLV KGNHLHTICE EGRCPNRGEC 

        70         80         90        100        110        120 
YAAGTATFLL GGSICTRSCA FCQVMKGQSP QAIDPLEAER VADAVQQMGL RYVVLTSVAR 

       130        140        150        160        170        180 
DDLPDHGVSI FTETMAAIRQ RNPLIEIEVL TPDFWGGVAD LAKALEAQRE RLTQLLMAAP 

       190        200        210        220        230        240 
VCFNHNLETV ERLQSKVRRG ATYHHSLSLL AAARELAPNI PTKSGLMLGL GEEQEEVVQT 

       250        260        270        280        290        300 
LEDLRSVDCQ RVTLGQYLRP SLAHIPVHRY WHPEDFKNLA EVACKLGFAQ VRSGPLVRSS 


YHAGEE 

« Hide

References

[1]"Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche differentiation."
Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L., Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C. expand/collapse author list , Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R., Chisholm S.W.
Nature 424:1042-1047(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MIT 9313.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX548175 Genomic DNA. Translation: CAE21251.1.
RefSeqNP_894907.1. NC_005071.1.

3D structure databases

ProteinModelPortalQ7V6S0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING74547.PMT1076.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE21251; CAE21251; PMT_1076.
GeneID1729074.
KEGGpmt:PMT1076.
PATRIC23010517. VBIProMar135351_1408.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0320.
KOK03644.
OMAEWLRRPI.
OrthoDBEOG6038ZS.

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 nameLIPA2_PROMM
AccessionPrimary (citable) accession number: Q7V6S0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: October 1, 2003
Last modified: May 14, 2014
This is version 75 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