B6QSZ4 (LIPA_PENMQ) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lipoyl synthase, mitochondrial
EC=2.8.1.8

Alternative name(s):
Lipoate synthase
Short name=LS
Short name=Lip-syn
Lipoic acid synthase

Gene names

ORF Names:

PMAA_003450

Organism

Penicillium marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333) [Complete proteome]

Taxonomic identifier

441960 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Talaromyces › Penicillium marneffei

Protein attributes

Sequence length	425 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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_03123
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_03123
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_03123
Subcellular location	Mitochondrion Potential HAMAP-Rule MF_03123.
Sequence similarities	Belongs to the radical SAM superfamily. Lipoyl synthase family.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
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	mitochondrion 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
	Transit peptide	1 – 33	33	Mitochondrion Potential
	Chain	34 – 425	392	Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123		PRO_0000398279
Sites
	Metal binding	142	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	147	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	153	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	173	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	177	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	180	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

	Sequence		Length	Mass (Da)
	B6QSZ4 [UniParc]. Last modified December 16, 2008. Version 1. Checksum: E1A082491BFA6990	FASTA	425	46,515
	10 20 30 40 50 60 MAASSTRLRC LYASSSTWKT SPSQSLISLS RRYATTSSAP PTPSDESSST LPKRRKTTTF 70 80 90 100 110 120 KDKLNAGPSF ADFVSGNGDS NNAPLDASEA YALETVMIPG PAGRGKKEHT RLPSWLKTPI 130 140 150 160 170 180 PDSTNYKRIK KDLRGLKLNT VCEEARCPNI SDCWGGSDKS AATATIMLMG DSCTRGCRFC 190 200 210 220 230 240 SVKTLRTPGP LDPHEPENTA EALSRWGLGY VVLTSVDRDD LSDGGAHHFA ETVIKIKQKA 250 260 270 280 290 300 PGILVECLTG DFAGDFDMVA LVAKSGLDVY AHNVETVEAL TPHVRDRRAT FQQSLRVLEA 310 320 330 340 350 360 AKRAKPSLIT KTSMMLGFGE TEDQMWDALR QLRASNVDVV TFGQYMRPTK RHMAVHEYVT 370 380 390 400 410 420 PDKFELWRQR ALEMGFLYVA SGPLVRSSYK AGEAFIENVL KKRRGVGNTP GAEVTTEVPV DALAK

References

[1]

"The genome sequence of Penicillium marneffei strain ATCC 18224." Fedorova N.D., Joardar V.S., Maiti R., Schobel S., Amedeo P., Galens K., Inman J.M., White O.R., Whitty B.R., Wortman J.R., Nierman W.C. Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 18224 / CBS 334.59 / QM 7333.

Cross-references

Sequence databases
EMBL GenBank DDBJ	DS995905 Genomic DNA. Translation: EEA19557.1.
RefSeq	XP_002152494.1. XM_002152458.1.
3D structure databases
ProteinModelPortal	B6QSZ4.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	7029911.
Phylogenomic databases
OrthoDB	EOG4G1QR3.
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_PENMQ

Accession

Primary (citable) accession number: B6QSZ4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 5, 2010
Last sequence update:	December 16, 2008
Last modified:	April 3, 2013
This is version 25 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program