Reviewed, UniProtKB/Swiss-Prot P44464 (LIPB_HAEIN)

Names and origin

Protein names

Recommended name:
    Octanoyltransferase
    EC=2.3.1.181
Alternative name(s):
    Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase
    Lipoyl/octanoyl transferase
    Lipoate-protein ligase B

Gene names

Name:	lipB
Ordered Locus Names:	HI0027

Organism

Haemophilus influenzae [Complete proteome] [HAMAP]

Taxonomic identifier

727 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

Protein attributes

Sequence length	212 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Catalytic activity	Octanoyl-[acyl-carrier-protein] + protein = protein N(6)-(octanoyl)lysine + [acyl-carrier-protein]. HAMAP MF_00013
Pathway	Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2. HAMAP MF_00013
Subcellular location	Cytoplasm By similarity.
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 component	Cytoplasm
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	lipoate biosynthetic process Inferred from electronic annotation. Source: InterPro protein modification 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 – 212	212	Octanoyltransferase HAMAP MF_00013		PRO_0000062841
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)
	P44464-1 [UniParc]. Last modified December 8, 2000. Version 2. Checksum: 06A56778EA6A6F0C	FASTA	212	24,058
	10 20 30 40 50 60 MNNSLIVRQL GLQDYQEIWH KMQDFTDTRN AETQDEIWLV QHYPVFTQGQ AGKPEHLLQR 70 80 90 100 110 120 SEIPVVQSVR GGQITYHAPG QQVMYVLIDI KRHKNLNVRQ LVTALEQTVV KTLAEYGIES 130 140 150 160 170 180 YPKPDAPGVY VDGKKICSLG LRIRRGCSFH GLALNINMDL NPFHYINPCG YAGLEMCQLA 190 200 210 DFVNQDKADC DNVSAKLIKH FANLLGYNIT TL

References

[1]

"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C. Science 269:496-512(1995) [PubMed: 7542800] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L42023 Genomic DNA. Translation: AAC21705.1.
PIR	H64043.
RefSeq	NP_438200.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	950925.
GenomeReviews	Gene locus HI0027 in contig L42023_GR.
KEGG	hin:HI0027.
NMPDR	fig|71421.1.peg.26.
TIGR	HI0027.
Phylogenomic databases
HOGENOM	P44464.
OMA	SGVWLPA
Enzyme and pathway databases
BioCyc	HINF71421:HI_0027-MON.
BRENDA	2.3.1.181. 109.
Family and domain databases
HAMAP	MF_00013. [Tree]
InterPro	IPR004143. BPL_LipA_LipB. IPR000544. Octanoyltransferase. IPR020605. Octanoyltransferase_CS. [Graphical view]
Pfam	PF03099. BPL_LipA_LipB. 1 hit. [Graphical view]
TIGRFAMs	TIGR00214. lipB. 1 hit.
PROSITE	PS01313. LIPB. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LIPB_HAEIN

Accession

Primary (citable) accession number: P44464

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	December 8, 2000
Last modified:	November 24, 2009
This is version 65 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)