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Q46H10 (LIPB_PROMT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:PMN2A_1736
OrganismProchlorococcus marinus (strain NATL2A) [Complete proteome] [HAMAP]
Taxonomic identifier59920 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length239 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. HAMAP-Rule MF_00013

Sequence similarities

Belongs to the LipB family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 239239Octanoyltransferase HAMAP-Rule MF_00013
PRO_0000242743

Regions

Region101 – 1088Substrate binding By similarity
Region168 – 1703Substrate binding By similarity
Region181 – 1833Substrate binding By similarity

Sites

Active site1991Acyl-thioester intermediate By similarity
Site1651Lowers pKa of active site Cys By similarity

Sequences

Sequence LengthMass (Da)Tools
Q46H10 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: C3229908C779544C

FASTA23927,078
        10         20         30         40         50         60 
MDKKLHFVSP ETGPNSNLDL TPQLAQSSSA FLFEPKNIVP FETALGWQKN FQKNLIEQPF 

        70         80         90        100        110        120 
SPQAVWLLEH FSCFTMGRGS DKKNLLFEEN NSPLPVFSIE RGGEVTHHMP GQIVGYLVLN 

       130        140        150        160        170        180 
LSLHKKDLSW YLRELEQVLI DVLDLLGMEG KRVDGLTGVW CEDKKVGSIG IGCKRWVTQH 

       190        200        210        220        230 
GFSLNVDCDL IGFEKIIPCG LDKVKVGKLS DWIPGIKVCD VTPLLRESVK RRFKLNWEK 

« 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000095 Genomic DNA. Translation: AAZ59224.1.
RefSeqYP_292927.1. NC_007335.2.

3D structure databases

ProteinModelPortalQ46H10.
ModBaseSearch...

Protein-protein interaction databases

STRING59920.PMN2A_1736.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ59224; AAZ59224; PMN2A_1736.
GeneID3607146.
KEGGpmn:PMN2A_1736.
PATRIC23022997. VBIProMar14922_0445.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0321.
HOGENOMHOG000194322.
KOK03801.
OMATHHLPGQ.
ProtClustDBPRK14344.

Enzyme and pathway databases

BioCycPMAR59920:GI1O-1780-MONOMER.
UniPathwayUPA00538; UER00592.

Family and domain databases

HAMAPMF_00013. LipB.
InterProIPR004143. BPL_LipA_LipB.
IPR000544. Octanoyltransferase.
IPR020605. Octanoyltransferase_CS.
[Graphical view]
PANTHERPTHR10993:SF0. PTHR10993:SF0. 1 hit.
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_PROMT
AccessionPrimary (citable) accession number: Q46H10
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: September 13, 2005
Last modified: May 1, 2013
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families