B9KSE2 (LIPA_RHOSK) 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:	RSKD131_1089

Organism

Rhodobacter sphaeroides (strain KD131 / KCTC 12085) [Complete proteome] [HAMAP]

Taxonomic identifier

557760 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Rhodobacter › Rhodobacter sphaeroides

Protein attributes

Sequence length	320 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 – 320	320	Lipoyl synthase HAMAP-Rule MF_00206		PRO_1000124643
Sites
	Metal binding	60	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	65	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	71	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	86	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	90	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	93	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

	Sequence		Length	Mass (Da)
	B9KSE2 [UniParc]. Last modified March 24, 2009. Version 1. Checksum: 0BF64485962BE698	FASTA	320	35,492
	10 20 30 40 50 60 MIGKLVRDLK IPDQRHPEKA HRPDNVQPKK PSWIRVKAPT SEGYKETRDI IRGQKLATVC 70 80 90 100 110 120 EEAGCPNVGE CWSQGHATMM IMGEICTRGC SFCNVATGRP QALDAFEPGR VAHAVSQLGL 130 140 150 160 170 180 KHVVVTSVDR DDLEDGGAEH FAQTIRAIRH RAPATTIEVL VPDFLKCGPS ALETVVAARP 190 200 210 220 230 240 DVFNHNLETV PGLYPEVRPG ARYFHSLRLL QRAKELDPSI FTKSGIMVGL GEDRQGVLQV 250 260 270 280 290 300 MDDMRSAEVD FLTIGQYLQP TPKHHRVDRF VTPEEFAGYE KAAYGKGFLM VSATPLTRSS 310 320 YHAGDDFARL RDARQKRLGA

References

[1]	"Complete genome sequence of Rhodobacter sphaeroides KD131." Lim S.-K., Kim S.J., Cha S.H., Oh Y.-K., Rhee H.-J., Kim M.-S., Lee J.K. J. Bacteriol. 191:1118-1119(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: KD131 / KCTC 12085.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001150 Genomic DNA. Translation: ACM00949.1.
RefSeq	YP_002525450.1. NC_011963.1.
3D structure databases
ProteinModelPortal	B9KSE2.
ModBase	Search...
Protein-protein interaction databases
STRING	557760.RSKD131_1089.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ACM00949; ACM00949; RSKD131_1089.
GeneID	7360504.
KEGG	rsk:RSKD131_1089.
PATRIC	23181277. VBIRhoSph125910_2502.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0320.
HOGENOM	HOG000235997.
KO	K03644.
OMA	EEYVTPE.
ProtClustDB	PRK05481.
Enzyme and pathway databases
BioCyc	RSPH557760:GH1P-1099-MONOMER.
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. [Graphical view]
PANTHER	PTHR10949. PTHR10949. 1 hit.
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_RHOSK

Accession

Primary (citable) accession number: B9KSE2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 28, 2009
Last sequence update:	March 24, 2009
Last modified:	May 29, 2013
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program