Q97U63 (LIPA_SULSO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable 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:	SSO3158

Organism

Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) [Reference proteome] [HAMAP]

Taxonomic identifier

273057 [NCBI]

Taxonomic lineage

cellular organisms › Archaea › Crenarchaeota › Thermoprotei › Sulfolobales › Sulfolobaceae › Sulfolobus › Sulfolobus solfataricus

Protein attributes

Sequence length	285 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 Reference 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 – 285	285	Probable lipoyl synthase HAMAP-Rule MF_00206		PRO_0000102394
Sites
	Metal binding	31	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	36	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	42	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	57	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	61	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	64	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q97U63 [UniParc]. Last modified October 1, 2001. Version 1. Checksum: B48A93B5C7FE13EC	FASTA	285	32,111
	10 20 30 40 50 60 MEKKVQIAVY ENENFKRVAE IVKKKSIATV CEEALCPNIM ECWGSGTATF MIMGSICTRG 70 80 90 100 110 120 CRFCYVLKGK PSPLDDEEPK RVAEAVKEME LDYVVITSVD RDDLSDGGAQ HFANVVKTVK 130 140 150 160 170 180 ELNPGIIVEV LTPDFRGNID AVKKVIDAGV DVFAHNVETV RRLTPIVRDP RASYEQSLNV 190 200 210 220 230 240 LKYAENVIKK SSILLGLGET WDEIVETMRD LRSVGVSILV LSQYMRPSRK QLEVKKRYTL 250 260 270 280 EEFKELEEIA YSMGFSAVIS LPLARTSYKA KEAYFRAIEN AKNHS

References

[1]

"The complete genome of the crenarchaeon Sulfolobus solfataricus P2." She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J., Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G., Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J., Medina N., Peng X. , Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C., Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T., Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J. Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE006641 Genomic DNA. Translation: AAK43259.1.
PIR	D90500.
RefSeq	NP_344469.1. NC_002754.1.
3D structure databases
ProteinModelPortal	Q97U63.
ModBase	Search...
Protein-protein interaction databases
STRING	273057.SSO3158.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAK43259; AAK43259; SSO3158.
GeneID	1453178.
KEGG	sso:SSO3158.
Phylogenomic databases
eggNOG	COG0320.
HOGENOM	HOG000235998.
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_SULSO

Accession

Primary (citable) accession number: Q97U63

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 26, 2002
Last sequence update:	October 1, 2001
Last modified:	May 1, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program