B7IMZ7 (LIPA_BACC2) 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:	BCG9842_B0124

Organism

Bacillus cereus (strain G9842) [Complete proteome] [HAMAP]

Taxonomic identifier

405531 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group › Bacillus cereus

Protein attributes

Sequence length	298 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]. 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 – 298	298	Lipoyl synthase HAMAP-Rule MF_00206		PRO_1000191447
Sites
	Metal binding	40	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	45	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	51	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	67	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	71	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	74	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

	Sequence		Length	Mass (Da)
	B7IMZ7 [UniParc]. Last modified February 10, 2009. Version 1. Checksum: 38CF8DE012794114	FASTA	298	33,715
	10 20 30 40 50 60 MTKQTEYKRK PEWLKIKLNT NENYTGLKKM MRSKNLHTVC EEAKCPNIHE CWAVRKTATF 70 80 90 100 110 120 MILGAVCTRA CRFCAVKTGL PTELDLQEPE RVADSVVQMG LKHVVITAVA RDDLKDGGAA 130 140 150 160 170 180 VFAETVRAVR RKNPFTSIEV LPSDMAGVEE NLKMLMDAKP DILNHNIETV RRLSNRVRAR 190 200 210 220 230 240 AKYDRSLEFL RRAKEMQPDI PTKSSIMVGL GETREDLIEA MDDLRANNVD ILTLGQYLQP 250 260 270 280 290 SKKHLPVIKY YPPAEFAELK EIALSKGFSH CEAGPLVRSS YHADEQVRSA KEKTAEAK

References

[1]	"Genome sequence of Bacillus cereus G9842." Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A., Ravel J., Sutton G. Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: G9842.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001186 Genomic DNA. Translation: ACK93698.1.
RefSeq	YP_002448540.1. NC_011772.1.
3D structure databases
ProteinModelPortal	B7IMZ7.
ModBase	Search...
Protein-protein interaction databases
STRING	405531.BCG9842_B0124.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ACK93698; ACK93698; BCG9842_B0124.
GeneID	7181452.
KEGG	bcg:BCG9842_B0124.
PATRIC	18905760. VBIBacCer50903_5003.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0320.
HOGENOM	HOG000235998.
KO	K03644.
OMA	DPHEPQR.
ProtClustDB	PRK05481.
Enzyme and pathway databases
BioCyc	BCER405531:GI5L-1106-MONOMER.
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_BACC2

Accession

Primary (citable) accession number: B7IMZ7

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	February 10, 2009
Last modified:	May 1, 2013
This is version 36 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program