Q57390 (LIPA_PELCD) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lipoyl synthase
EC=2.8.1.8

Alternative name(s):
Lip-syn
Short name=LS
Lipoate synthase
Lipoic acid synthase
Sulfur insertion protein LipA

Gene names

Name:	lipA
Synonyms:	acoS
Ordered Locus Names:	Pcar_0346

Organism

Pelobacter carbinolicus (strain DSM 2380 / Gra Bd 1) [Complete proteome] [HAMAP]

Taxonomic identifier

338963 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › delta/epsilon subdivisions › Deltaproteobacteria › Desulfuromonadales › Pelobacteraceae › Pelobacter › Pelobacter carbinolicus

Protein attributes

Sequence length	309 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives By similarity. HAMAP-Rule MF_00206
Catalytic activity	Protein N(6)-(octanoyl)lysine + 2 sulfur + 2 S-adenosyl-L-methionine = protein N(6)-(lipoyl)lysine + 2 L-methionine + 2 5'-deoxyadenosine. HAMAP-Rule MF_00206
Cofactor	Binds 2 4Fe-4S clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine By similarity.
Pathway	Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 2/2. HAMAP-Rule MF_00206
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the radical SAM superfamily. Lipoyl synthase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding S-adenosyl-L-methionine
Molecular function	Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	protein lipoylation Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: HAMAP lipoate synthase activity Inferred from electronic annotation. Source: HAMAP metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 309	309	Lipoyl synthase HAMAP-Rule MF_00206		PRO_0000102333
Sites
	Metal binding	56	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	61	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	67	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	82	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	86	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	89	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Experimental info
	Sequence conflict	149 – 151	3	EGV → RRVY in AAA91878. Ref.1
	Sequence conflict	149 – 151	3	EGV → RRVY in AAA18918. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q57390 [UniParc]. Last modified December 20, 2005. Version 2. Checksum: 9EA24FB6E17AFAC7	FASTA	309	34,154
	10 20 30 40 50 60 MDVGQKKRGA DKTALATTDE QGALSKPTWI RAKAPISPEV GRLTGILRDL HLHTVCEEAS 70 80 90 100 110 120 CPNLGECFKR GTATFMIMGD VCTRRCPFCD VAHGRPAALD TEEPGHLADA IGAMKLKYVV 130 140 150 160 170 180 ITSVTRDDLE DGGAAHFAQC IESIRKKTEG VKVEILVPDF RGHVDAALKN LGNCLPDVFN 190 200 210 220 230 240 HNLETVPRLY AESRPGARYH ESLRLLQRFK ETYPGIPTKS GLMLGLGETD EEILEVMRDL 250 260 270 280 290 300 RVHGCDMLTI GQYLRPSRHH LPVQRYVTPE QFEAFRVAGL KMGFSQVASG PLVRSSYHAD LQAKEVLHT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification and molecular characterization of the aco genes encoding the Pelobacter carbinolicus acetoin dehydrogenase enzyme system." Oppermann F.B., Steinbuechel A. J. Bacteriol. 176:469-485(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete sequence of Pelobacter carbinolicus DSM 2380." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chertkov O., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P. Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 2380 / Gra Bd 1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L24124 Genomic DNA. Translation: AAA91878.1. U01100 Unassigned DNA. Translation: AAA18918.1. CP000142 Genomic DNA. Translation: ABA87606.1.
PIR	E36953.
RefSeq	YP_006716018.1. NC_007498.2.
3D structure databases
ProteinModelPortal	Q57390.
ModBase	Search...
Protein-protein interaction databases
STRING	338963.Pcar_0346.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABA87606; ABA87606; Pcar_0346.
GeneID	3723479.
KEGG	pca:Pcar_0346.
PATRIC	22886614. VBIPelCar86875_0384.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0320.
HOGENOM	HOG000235997.
KO	K03644.
OMA	EEYVTPE.
ProtClustDB	PRK05481.
Enzyme and pathway databases
UniPathway	UPA00538; UER00593.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
HAMAP	MF_00206. Lipoyl_synth.
InterPro	IPR013785. Aldolase_TIM. IPR006638. Elp3/MiaB/NifB. IPR003698. Lipoyl_synth. IPR007197. rSAM. [Graphical view]
PANTHER	PTHR10949. PTHR10949. 1 hit.
Pfam	PF04055. Radical_SAM. 1 hit. [Graphical view]
PIRSF	PIRSF005963. Lipoyl_synth. 1 hit.
SMART	SM00729. Elp3. 1 hit. [Graphical view]
TIGRFAMs	TIGR00510. lipA. 1 hit.
ProtoNet	Search...

Entry information

Entry name

LIPA_PELCD

Accession

Primary (citable) accession number: Q57390
Secondary accession number(s): Q3A7N8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	December 20, 2005
Last modified:	May 1, 2013
This is version 97 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program