A7FKY9 (LIPA_YERP3) 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
Ordered Locus Names:	YpsIP31758_2955

Organism

Yersinia pseudotuberculosis serotype O:1b (strain IP 31758) [Complete proteome] [HAMAP]

Taxonomic identifier

349747 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Yersinia › Yersinia pseudotuberculosis

Protein attributes

Sequence length	321 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 Potential HAMAP-Rule MF_00206.
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 – 321	321	Lipoyl synthase HAMAP-Rule MF_00206		PRO_1000058580
Sites
	Metal binding	68	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	73	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	79	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	94	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	98	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	101	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

	Sequence		Length	Mass (Da)
	A7FKY9 [UniParc]. Last modified September 11, 2007. Version 1. Checksum: ABA14E24EA640399	FASTA	321	36,086
	10 20 30 40 50 60 MSKPIQMERG VKYRDADKMA LIPVKNVVTE RQELLRKPEW LKIKLPTDSS RIQGIKAAMR 70 80 90 100 110 120 KNGLHSVCEE ASCPNLSECF NHGTATFMIL GAICTRRCPF CDVAHGRPVT PDANEPEKLA 130 140 150 160 170 180 QTIQDMGLRY VVITSVDRDD LRDGGAQHFA DCISAIRAKN PTIKIETLVP DFRGRMDRAL 190 200 210 220 230 240 DILTATPPDV FNHNLENVPR VYRQVRPGAN YDWSLKLLER FKEAHPDIPT KSGLMVGLGE 250 260 270 280 290 300 TNAEIVEVMH DLRRHGVTML TLGQYLQPSR HHLPVQRYVS PAEFDEMKAE AMAMGFTHAA 310 320 CGPFVRSSYH ADLQAKGMEV K

References

[1]

"The complete genome sequence of Yersinia pseudotuberculosis IP31758, the causative agent of Far East scarlet-like fever." Eppinger M., Rosovitz M.J., Fricke W.F., Rasko D.A., Kokorina G., Fayolle C., Lindler L.E., Carniel E., Ravel J. PLoS Genet. 3:1508-1523(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: IP 31758.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000720 Genomic DNA. Translation: ABS48859.1.
RefSeq	YP_001401917.1. NC_009708.1.
3D structure databases
ProteinModelPortal	A7FKY9.
ModBase	Search...
Protein-protein interaction databases
STRING	349747.YpsIP31758_2955.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABS48859; ABS48859; YpsIP31758_2955.
GeneID	5386298.
KEGG	ypi:YpsIP31758_2955.
PATRIC	18634993. VBIYerPse15693_3416.
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_YERP3

Accession

Primary (citable) accession number: A7FKY9

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	September 11, 2007
Last modified:	May 1, 2013
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program