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Protein

Lipoyl synthase, mitochondrial

Gene

SMAC_01256

Organism
Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

Protein N(6)-(octanoyl)lysine + 2 sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + 2 reduced [2Fe-2S] ferredoxin = protein N(6)-(lipoyl)lysine + 2 (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine + 2 oxidized [2Fe-2S] ferredoxin.UniRule annotation

Cofactori

[4Fe-4S] clusterUniRule annotationNote: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.UniRule annotation

Pathway: protein lipoylation via endogenous pathway

This protein is involved in step 2 of the subpathway that synthesizes protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein].UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Lipoyl synthase, mitochondrial (SMAC_01256)
This subpathway is part of the pathway protein lipoylation via endogenous pathway, which is itself part of Protein modification.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein], the pathway protein lipoylation via endogenous pathway and in Protein modification.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi157 – 1571Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi162 – 1621Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi168 – 1681Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi188 – 1881Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi192 – 1921Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi195 – 1951Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

UniPathwayiUPA00538; UER00593.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipoyl synthase, mitochondrialUniRule annotation (EC:2.8.1.8UniRule annotation)
Alternative name(s):
Lipoate synthaseUniRule annotation
Short name:
LSUniRule annotation
Short name:
Lip-synUniRule annotation
Lipoic acid synthaseUniRule annotation
Gene namesi
ORF Names:SMAC_01256
OrganismiSordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell)
Taxonomic identifieri771870 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeSordaria
ProteomesiUP000001881 Componenti: Unassembled WGS sequence

Organism-specific databases

EuPathDBiFungiDB:SMAC_01256.

Subcellular locationi

  • Mitochondrion UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4040MitochondrionUniRule annotationAdd
BLAST
Chaini41 – 445405Lipoyl synthase, mitochondrialPRO_0000398293Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi771870.XP_003352422.1.

Structurei

3D structure databases

ProteinModelPortaliD1Z4I6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the radical SAM superfamily. Lipoyl synthase family.UniRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

InParanoidiD1Z4I6.
KOiK03644.
OrthoDBiEOG79KPR7.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00206. Lipoyl_synth.
InterProiIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
[Graphical view]
PANTHERiPTHR10949. PTHR10949. 1 hit.
PfamiPF04055. Radical_SAM. 1 hit.
[Graphical view]
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00510. lipA. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

D1Z4I6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRPGSWRVIT HYGFTGPIQR LQAPLRRSLA RAAALSTRSY ATIPSAPSSQ
60 70 80 90 100
PTSQESSPAA SASASASAPA TKPRPTYFKD TTLASLDDFI ANQSSAAPLA
110 120 130 140 150
PSEAYTLRTA QVGPAGKKRT ITRLPEWLKT PIPSAGANPE FAKIKADLRG
160 170 180 190 200
LNLHTVCEEA RCPNIGECWG GSNKAAATAT IMLMGDTCTR GCRFCSVKTS
210 220 230 240 250
RKPPPLDPHE PENTAEALAR WGLGYVVLTS VDRDDLADGG ARHFAETIRR
260 270 280 290 300
IKQKKPTLLV EALTGDFMGD LDMVKIVADS GLDVYAHNVE TVENLTPYVR
310 320 330 340 350
DRRATFRQSL KVLEHVKNVR GKEGIITKTS IMLGLGETEE ELWDALRELR
360 370 380 390 400
KVDVDVVTFG QYMRPTKRHL AVEKYITPDE FELWRQRALD MGFLYCASGP
410 420 430 440
LVRSSYKAGE AFIENVLKKR ASERVVSEAL GQAVAAEEAT SAKSA
Length:445
Mass (Da):48,591
Last modified:February 9, 2010 - v1
Checksum:iCC87656ED8D9D672
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CABT02000004 Genomic DNA. Translation: CCC07689.1.
RefSeqiXP_003352422.1. XM_003352374.1.

Genome annotation databases

GeneIDi10810058.
KEGGismp:SMAC_01256.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CABT02000004 Genomic DNA. Translation: CCC07689.1.
RefSeqiXP_003352422.1. XM_003352374.1.

3D structure databases

ProteinModelPortaliD1Z4I6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi771870.XP_003352422.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi10810058.
KEGGismp:SMAC_01256.

Organism-specific databases

EuPathDBiFungiDB:SMAC_01256.

Phylogenomic databases

InParanoidiD1Z4I6.
KOiK03644.
OrthoDBiEOG79KPR7.

Enzyme and pathway databases

UniPathwayiUPA00538; UER00593.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00206. Lipoyl_synth.
InterProiIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
[Graphical view]
PANTHERiPTHR10949. PTHR10949. 1 hit.
PfamiPF04055. Radical_SAM. 1 hit.
[Graphical view]
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00510. lipA. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads: Sordaria macrospora, a model organism for fungal morphogenesis."
    Nowrousian M., Stajich J.E., Chu M., Engh I., Espagne E., Halliday K., Kamerewerd J., Kempken F., Knab B., Kuo H.-C., Osiewacz H.D., Poeggeler S., Read N.D., Seiler S., Smith K.M., Zickler D., Kueck U., Freitag M.
    PLoS Genet. 6:E1000891-E1000891(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC MYA-333 / DSM 997 / K(L3346) / K-hell.

Entry informationi

Entry nameiLIPA_SORMK
AccessioniPrimary (citable) accession number: D1Z4I6
Secondary accession number(s): F7VQA7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: February 9, 2010
Last modified: June 24, 2015
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.