Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Lipoyl synthase, mitochondrial

Gene

ACLA_034510

Organism
Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1)
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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi132 – 1321Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi137 – 1371Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi143 – 1431Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi163 – 1631Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi167 – 1671Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi170 – 1701Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-HAMAP
  2. lipoate synthase activity Source: UniProtKB-HAMAP
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. protein lipoylation Source: UniProtKB-HAMAP
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:ACLA_034510
OrganismiAspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1)
Taxonomic identifieri344612 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006701 Componenti: Unassembled WGS sequence

Subcellular locationi

Mitochondrion UniRule annotation

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3333MitochondrionUniRule annotationAdd
BLAST
Chaini34 – 415382Lipoyl synthase, mitochondrialPRO_0000398251Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi5057.CADACLAP00003729.

Structurei

3D structure databases

ProteinModelPortaliA1CJC4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0320.
HOGENOMiHOG000235998.
KOiK03644.
OMAiCAFCQVE.
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.

A1CJC4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASTSHLRS LCSSTRSLSR SGVIVTPIAC RGYATTDPSP SATTPTPVRR
60 70 80 90 100
RTTFKDKLNA GPSFSDFVSN GNDNAPLDPS EAYALKTALV GPAGRKKEMT
110 120 130 140 150
RLPSWLKTPI PDSKNYQRLK KDLRGLNLHT VCEEARCPNI SDCWGGSDKS
160 170 180 190 200
SATATIMLMG DTCTRGCRFC SVKTSRAPPP LDPHEPENTA EAISRWGLGY
210 220 230 240 250
VVLTSVDRDD LVDGGARHFA ETVIKIKQKA PSILVECLTG DYAGDLDMVK
260 270 280 290 300
LVARSGLDVY AHNVETVEAL TPQVRDRRAN FQQSLRVLDA AKKAQPTLIT
310 320 330 340 350
KTSLMLGLGE TDEQLWDALR QLRAVNVDVV TFGQYMRPTK RHMAVHEYVT
360 370 380 390 400
PDRFELWRQR ALEMGFLYCA SGPLVRSSYK AGEAFIENVL KKRRAASGGA
410
ETIGERPVAV DEASR
Length:415
Mass (Da):45,519
Last modified:January 23, 2007 - v1
Checksum:iDE25AD5BD2982A90
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS027056 Genomic DNA. Translation: EAW09248.1.
RefSeqiXP_001270674.1. XM_001270673.1.

Genome annotation databases

EnsemblFungiiCADACLAT00003809; CADACLAP00003729; CADACLAG00003809.
GeneIDi4702900.
KEGGiact:ACLA_034510.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DS027056 Genomic DNA. Translation: EAW09248.1.
RefSeqiXP_001270674.1. XM_001270673.1.

3D structure databases

ProteinModelPortaliA1CJC4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5057.CADACLAP00003729.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADACLAT00003809; CADACLAP00003729; CADACLAG00003809.
GeneIDi4702900.
KEGGiact:ACLA_034510.

Phylogenomic databases

eggNOGiCOG0320.
HOGENOMiHOG000235998.
KOiK03644.
OMAiCAFCQVE.
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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1.

Entry informationi

Entry nameiLIPA_ASPCL
AccessioniPrimary (citable) accession number: A1CJC4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: January 23, 2007
Last modified: April 1, 2015
This is version 53 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.