C1AQD3 (LIPA_MYCBT) 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:	JTY_2228

Organism

Mycobacterium bovis (strain BCG / Tokyo 172 / ATCC 35737 / TMC 1019) [Complete proteome] [HAMAP]

Taxonomic identifier

561275 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex › Mycobacterium bovis › Mycobacterium bovis BCG

Protein attributes

Sequence length	311 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 – 311	311	Lipoyl synthase HAMAP-Rule MF_00206		PRO_1000124641
Sites
	Metal binding	55	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	60	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	66	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	81	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	85	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	88	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

	Sequence		Length	Mass (Da)
	C1AQD3 [UniParc]. Last modified May 26, 2009. Version 1. Checksum: 0594BBC9AB4A547A	FASTA	311	34,719
	10 20 30 40 50 60 MSVAAEGRRL LRLEVRNAQT PIERKPPWIK TRARIGPEYT ELKNLVRREG LHTVCEEAGC 70 80 90 100 110 120 PNIFECWEDR EATFLIGGDQ CTRRCDFCQI DTGKPAELDR DEPRRVADSV RTMGLRYATV 130 140 150 160 170 180 TGVARDDLPD GGAWLYAATV RAIKELNPST GVELLIPDFN GEPTRLAEVF ESGPEVLAHN 190 200 210 220 230 240 VETVPRIFKR IRPAFTYRRS LGVLTAARDA GLVTKSNLIL GLGETSDEVR TALGDLRDAG 250 260 270 280 290 300 CDIVTITQYL RPSARHHPVE RWVKPEEFVQ FARFAEGLGF AGVLAGPLVR SSYRAGRLYE 310 QARNSRALAS R

References

[1]

"Whole genome sequence analysis of Mycobacterium bovis bacillus Calmette-Guerin (BCG) Tokyo 172: a comparative study of BCG vaccine substrains." Seki M., Honda I., Fujita I., Yano I., Yamamoto S., Koyama A. Vaccine 27:1710-1716(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: BCG / Tokyo 172 / ATCC 35737 / TMC 1019.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP010918 Genomic DNA. Translation: BAH26512.1.
RefSeq	YP_002645280.1. NC_012207.1.
3D structure databases
ProteinModelPortal	C1AQD3.
ModBase	Search...
Protein-protein interaction databases
STRING	561275.JTY_2228.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAH26512; BAH26512; JTY_2228.
GeneID	7562830.
KEGG	mbt:JTY_2228.
PATRIC	18024116. VBIMycBov85238_2436.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0320.
HOGENOM	HOG000235997.
KO	K03644.
OMA	EEYVTPE.
ProtClustDB	PRK05481.
Enzyme and pathway databases
BioCyc	MBOV561275:GHDN-3044-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. 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_MYCBT

Accession

Primary (citable) accession number: C1AQD3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 28, 2009
Last sequence update:	May 26, 2009
Last modified:	May 1, 2013
This is version 33 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program