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Q46IV8 (Q46IV8_PROMT) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 66. Feed History...

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

Names and origin

Protein namesRecommended name:
Lipoyl synthase HAMAP-Rule MF_00206

EC=2.8.1.8 HAMAP-Rule MF_00206
Alternative name(s):
Lip-syn HAMAP-Rule MF_00206
Lipoate synthase HAMAP-Rule MF_00206
Lipoic acid synthase HAMAP-Rule MF_00206
Sulfur insertion protein LipA HAMAP-Rule MF_00206
Gene names
Name:lipA HAMAP-Rule MF_00206
Ordered Locus Names:PMN2A_1080 EMBL AAZ58570.1
OrganismProchlorococcus marinus (strain NATL2A) [Complete proteome] [HAMAP] EMBL AAZ58570.1
Taxonomic identifier59920 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length289 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. HAMAP-Rule MF_00206

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. HAMAP-Rule MF_00206

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Metal binding331Iron-sulfur 1 (4Fe-4S) By similarity HAMAP-Rule MF_00206
Metal binding381Iron-sulfur 1 (4Fe-4S) By similarity HAMAP-Rule MF_00206
Metal binding441Iron-sulfur 1 (4Fe-4S) By similarity HAMAP-Rule MF_00206
Metal binding591Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity HAMAP-Rule MF_00206
Metal binding631Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity HAMAP-Rule MF_00206
Metal binding661Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity HAMAP-Rule MF_00206

Sequences

Sequence LengthMass (Da)Tools
Q46IV8 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 0FE80E83D22D7091

FASTA28932,163
        10         20         30         40         50         60 
MLKPDWLRVK APQQERIGNV ADLLVDLKLN TVCQEASCPN IGECFAGGTA TFLIMGPACT 

        70         80         90        100        110        120 
RKCPYCDISF DNSKRLLDPS EPDRLGEAVY RMGLTHVVIT SVNRDDLEDG GASQFLKCIK 

       130        140        150        160        170        180 
AVQSKSPFTS IEVLIPDLCG NWDALKVILD AAPNVLNHNI ETVPRLYPRV RPQGKYERSL 

       190        200        210        220        230        240 
ELLKRVREGW PRVYTKSGLM AGLGETDDEI LSVLSDLHLN KVDIVTIGQY LSPGPKHLPV 

       250        260        270        280 
NRFVSPSQFD SYRVEGENKL GFLQVISSPL TRSSYHAGEV KKLMMSHPR 

« Hide

References

[1]"Patterns and implications of gene gain and loss in the evolution of Prochlorococcus."
Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., Richardson P., Chisholm S.W.
PLoS Genet. 3:2515-2528(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NATL2A EMBL AAZ58570.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000095 Genomic DNA. Translation: AAZ58570.1.
RefSeqYP_292273.1. NC_007335.2.

3D structure databases

ProteinModelPortalQ46IV8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING59920.PMN2A_1080.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ58570; AAZ58570; PMN2A_1080.
GeneID3606467.
KEGGpmn:PMN2A_1080.
PATRIC23026021. VBIProMar14922_1937.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycPMAR59920:GI1O-1959-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 nameQ46IV8_PROMT
AccessionPrimary (citable) accession number: Q46IV8
Entry history
Integrated into UniProtKB/TrEMBL: September 13, 2005
Last sequence update: September 13, 2005
Last modified: February 19, 2014
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)