A4J246 (LIPB_DESRM) 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:	Dred_0609

Organism

Desulfotomaculum reducens (strain MI-1) [Complete proteome] [HAMAP]

Taxonomic identifier

349161 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Clostridia › Clostridiales › Peptococcaceae › Desulfotomaculum › Desulfotomaculum reducens

Protein attributes

Sequence length	228 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 – 228	228	Octanoyltransferase HAMAP-Rule MF_00013		PRO_1000070956
Regions
	Region	75 – 82	8	Substrate binding By similarity
	Region	143 – 145	3	Substrate binding By similarity
	Region	156 – 158	3	Substrate binding By similarity
Sites
	Active site	174	1	Acyl-thioester intermediate By similarity
	Site	140	1	Lowers pKa of active site Cys By similarity

Sequences

	Sequence		Length	Mass (Da)
	A4J246 [UniParc]. Last modified May 1, 2007. Version 1. Checksum: 2E65798A52008055	FASTA	228	26,239
	10 20 30 40 50 60 MKLFVAKLGE IDYQDALTMQ EKLLLLRQQN KVEDIMLLLQ HPPTLTLGTR ENRYNILVPE 70 80 90 100 110 120 VELKRQGVNI FKSNRGGDVT YHGPGQIVGY PIVDLNGHGK SIREYVHKIE ETFIQLLKEE 130 140 150 160 170 180 YDLTASRESK YHGVWLGNEK ITAIGCAVKR WVTMHGFAFN VNTNLSHFNL INPCGITDRG 190 200 210 220 VTSLQKIFGQ PQDMEKVYKQ VITYFSRVFD FEPEIIDDKK LNEIVGRE

References

[1]

"Complete sequence of Desulfotomaculum reducens MI-1." US DOE Joint Genome Institute Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F. , Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P. Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MI-1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000612 Genomic DNA. Translation: ABO49149.1.
RefSeq	YP_001111974.1. NC_009253.1.
3D structure databases
ProteinModelPortal	A4J246.
ModBase	Search...
Protein-protein interaction databases
STRING	349161.Dred_0609.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABO49149; ABO49149; Dred_0609.
GeneID	4958319.
KEGG	drm:Dred_0609.
PATRIC	21727169. VBIDesRed82656_0672.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0321.
HOGENOM	HOG000194322.
KO	K03801.
OMA	HYSGIVP.
ProtClustDB	CLSK853423.
Enzyme and pathway databases
BioCyc	DRED349161:GHP6-708-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_DESRM

Accession

Primary (citable) accession number: A4J246

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 26, 2008
Last sequence update:	May 1, 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