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A8LYF4 (LIPB_SALAI) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 45. 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:
Octanoyltransferase

EC=2.3.1.181
Alternative name(s):
Lipoate-protein ligase B
Lipoyl/octanoyl transferase
Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase
Gene names
Name:lipB
Ordered Locus Names:Sare_3560
OrganismSalinispora arenicola (strain CNS-205) [Complete proteome] [HAMAP]
Taxonomic identifier391037 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicromonosporineaeMicromonosporaceaeSalinispora

Protein attributes

Sequence length213 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate By similarity. HAMAP-Rule MF_00013

Catalytic activity

Octanoyl-[acyl-carrier-protein] + protein = protein N(6)-(octanoyl)lysine + [acyl-carrier-protein]. HAMAP-Rule MF_00013

Pathway

Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2. HAMAP-Rule MF_00013

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_00013.

Miscellaneous

In the reaction, the free carboxyl group of octanoic acid is attached via an amide linkage to the epsilon-amino group of a specific lysine residue of lipoyl domains of lipoate-dependent enzymes By similarity.

Sequence similarities

Belongs to the LipB family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processcellular protein modification process

Inferred from electronic annotation. Source: InterPro

lipoate biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionlipoyl(octanoyl) transferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

octanoyltransferase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 213213Octanoyltransferase HAMAP-Rule MF_00013
PRO_1000074012

Regions

Region73 – 808Substrate binding By similarity
Region145 – 1473Substrate binding By similarity
Region158 – 1603Substrate binding By similarity

Sites

Active site1761Acyl-thioester intermediate By similarity
Site1421Lowers pKa of active site Cys By similarity

Sequences

Sequence LengthMass (Da)Tools
A8LYF4 [UniParc].

Last modified December 4, 2007. Version 1.
Checksum: 18FDF8D654137190

FASTA21323,142
        10         20         30         40         50         60 
MTTTTSDLTV LRAGTLDYEA AWEEQRRLHE SVVTDKHGDA VLLLEHPSVY TAGKRTEPWD 

        70         80         90        100        110        120 
RPMDGTPVID VDRGGKITWH GPGQLVGYPI LRLPDPVDVV AYVRRVEQML IDVCAEFGLV 

       130        140        150        160        170        180 
AGRIEGRSGV WVPADDRGPA RKVAAIGIRV ARGVTLHGFS LNCDCDLTYY DRIVPCGIRD 

       190        200        210 
AGVTSLAAEL GRPVTVADAL PVVERHLPTL VGA 

« Hide

References

[1]"Complete sequence of Salinispora arenicola CNS-205."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Foster B., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Jensen P.R., Moore B.S., Penn K. expand/collapse author list , Jenkins C., Udwary D., Xiang L., Gontang E., Richardson P.
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CNS-205.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000850 Genomic DNA. Translation: ABV99362.1.
RefSeqYP_001538353.1. NC_009953.1.

3D structure databases

ProteinModelPortalA8LYF4.
SMRA8LYF4. Positions 6-196.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING391037.Sare_3560.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV99362; ABV99362; Sare_3560.
GeneID5705053.
KEGGsaq:Sare_3560.
PATRIC23435655. VBISalAre38676_3588.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0321.
HOGENOMHOG000194322.
KOK03801.
OMAVAYFLIN.
OrthoDBEOG6XM7G6.
ProtClustDBPRK14345.

Enzyme and pathway databases

BioCycSARE391037:GH66-3597-MONOMER.
UniPathwayUPA00538; UER00592.

Family and domain databases

HAMAPMF_00013. LipB.
InterProIPR004143. BPL_LipA_LipB.
IPR000544. Octanoyltransferase.
IPR020605. Octanoyltransferase_CS.
[Graphical view]
PfamPF03099. BPL_LplA_LipB. 1 hit.
[Graphical view]
PIRSFPIRSF016262. LPLase. 1 hit.
TIGRFAMsTIGR00214. lipB. 1 hit.
PROSITEPS01313. LIPB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLIPB_SALAI
AccessionPrimary (citable) accession number: A8LYF4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: December 4, 2007
Last modified: February 19, 2014
This is version 45 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