A4VQZ7 (LIPB_PSEU5) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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:	PST_3775

Organism

Pseudomonas stutzeri (strain A1501) [Complete proteome] [HAMAP]

Taxonomic identifier

379731 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas › Pseudomonas stutzeri group › Pseudomonas stutzeri subgroup › Pseudomonas stutzeri

Protein attributes

Sequence length	219 AA.
Sequence status	Complete.
Protein existence	Inferred 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

Keywords
Cellular component	Cytoplasm
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	cellular protein modification process Inferred from electronic annotation. Source: InterPro lipoate biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	lipoyl(octanoyl) transferase activity Inferred from electronic annotation. Source: EC octanoyltransferase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 219	219	Octanoyltransferase HAMAP-Rule MF_00013		PRO_0000321661
Regions
	Region	71 – 78	8	Substrate binding By similarity
	Region	138 – 140	3	Substrate binding By similarity
	Region	151 – 153	3	Substrate binding By similarity
Sites
	Active site	169	1	Acyl-thioester intermediate By similarity
	Site	135	1	Lowers pKa of active site Cys By similarity

Sequences

	Sequence		Length	Mass (Da)
	A4VQZ7 [UniParc]. Last modified May 29, 2007. Version 1. Checksum: D6641B45E5F723C3	FASTA	219	24,117
	10 20 30 40 50 60 MMTHDVGVRE LGLIEYRAAW QAMQHFTNTR DADSGDEIWL LQHPPVFTQG QAGKAEHLLF 70 80 90 100 110 120 PGEIPVVQVD RGGQVTYHGP GQLVGYLLLD VRRLGIGVRE LVSRIERSLI DLLAGYDVEA 130 140 150 160 170 180 VAKPDAPGVY VGGAKIASLG LRIRNGRSFH GLALNVDMDL EPFRRINPCG YAGLPMTQLR 190 200 210 DLIGPIDISE VADRLRDHLV RQLGYAQQKT LAGGIEAYE

References

[1]

"Complete genome sequence of the metabolically versatile and root-associated nitrogen-fixing bacterium Pseudomonas stutzeri A1501." Yan Y., Yang J., Dou Y., Ping S., Chen M., Yao Z., Li H., Lu W., Zhang W., Peng J., Liu W., He S., Geng L., Zhang X., Yang F., Li D., Lin Z., Wang Y. , Elmerich C., Lin M., Jin Q. Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: A1501.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000304 Genomic DNA. Translation: ABP81398.1.
RefSeq	YP_001174240.1. NC_009434.1.
3D structure databases
ProteinModelPortal	A4VQZ7.
ModBase	Search...
Protein-protein interaction databases
STRING	379731.PST_3775.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABP81398; ABP81398; PST_3775.
GeneID	5096736.
KEGG	psa:PST_3775.
PATRIC	19968050. VBIPseStu31643_3754.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0321.
HOGENOM	HOG000194321.
KO	K03801.
OMA	KEYVYRI.
ProtClustDB	PRK14342.
Enzyme and pathway databases
BioCyc	PSTU379731:GJER-3770-MONOMER.
UniPathway	UPA00538; UER00592.
Family and domain databases
HAMAP	MF_00013. LipB.
InterPro	IPR004143. BPL_LipA_LipB. IPR000544. Octanoyltransferase. IPR020605. Octanoyltransferase_CS. [Graphical view]
PANTHER	PTHR10993:SF0. PTHR10993:SF0. 1 hit.
Pfam	PF03099. BPL_LplA_LipB. 1 hit. [Graphical view]
PIRSF	PIRSF016262. LPLase. 1 hit.
TIGRFAMs	TIGR00214. lipB. 1 hit.
PROSITE	PS01313. LIPB. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LIPB_PSEU5

Accession

Primary (citable) accession number: A4VQZ7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 26, 2008
Last sequence update:	May 29, 2007
Last modified:	May 1, 2013
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program