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A1CJC4

- LIPA_ASPCL

UniProt

A1CJC4 - LIPA_ASPCL

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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: 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 By similarity.UniRule annotation

Catalytic activityi

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

Cofactori

Binds 2 4Fe-4S clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine By similarity.

Pathwayi

Sites

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

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, mitochondrial (EC:2.8.1.8)
Alternative name(s):
Lipoate synthase
Short name:
LS
Short name:
Lip-syn
Lipoic acid synthase
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: Unassembled WGS sequence

Subcellular locationi

Mitochondrion Reviewed prediction 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 – 3333Mitochondrion Reviewed prediction
Add
BLAST
Chaini34 – 415382Lipoyl synthase, mitochondrialUniRule annotation
PRO_0000398251Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi5057.CADACLAP00003729.

Structurei

3D structure databases

ProteinModelPortaliA1CJC4.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0320.
HOGENOMiHOG000235998.
KOiK03644.
OMAiPEEPYNT.
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]
PIRSFiPIRSF005963. Lipoyl_synth. 1 hit.
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

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MAASTSHLRS LCSSTRSLSR SGVIVTPIAC RGYATTDPSP SATTPTPVRR    50
RTTFKDKLNA GPSFSDFVSN GNDNAPLDPS EAYALKTALV GPAGRKKEMT 100
RLPSWLKTPI PDSKNYQRLK KDLRGLNLHT VCEEARCPNI SDCWGGSDKS 150
SATATIMLMG DTCTRGCRFC SVKTSRAPPP LDPHEPENTA EAISRWGLGY 200
VVLTSVDRDD LVDGGARHFA ETVIKIKQKA PSILVECLTG DYAGDLDMVK 250
LVARSGLDVY AHNVETVEAL TPQVRDRRAN FQQSLRVLDA AKKAQPTLIT 300
KTSLMLGLGE TDEQLWDALR QLRAVNVDVV TFGQYMRPTK RHMAVHEYVT 350
PDRFELWRQR ALEMGFLYCA SGPLVRSSYK AGEAFIENVL KKRRAASGGA 400
ETIGERPVAV DEASR 415
Length:415
Mass (Da):45,519
Last modified:January 23, 2007 - v1
Checksum:iDE25AD5BD2982A90
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
DS027056 Genomic DNA. Translation: EAW09248.1 .
RefSeqi XP_001270674.1. XM_001270673.1.

3D structure databases

ProteinModelPortali A1CJC4.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5057.CADACLAP00003729.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADACLAT00003809 ; CADACLAP00003729 ; CADACLAG00003809 .
GeneIDi 4702900.
KEGGi act:ACLA_034510.

Phylogenomic databases

eggNOGi COG0320.
HOGENOMi HOG000235998.
KOi K03644.
OMAi PEEPYNT.
OrthoDBi EOG79KPR7.

Enzyme and pathway databases

UniPathwayi UPA00538 ; UER00593 .

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
HAMAPi MF_00206. Lipoyl_synth.
InterProi IPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
[Graphical view ]
PANTHERi PTHR10949. PTHR10949. 1 hit.
Pfami PF04055. Radical_SAM. 1 hit.
[Graphical view ]
PIRSFi PIRSF005963. Lipoyl_synth. 1 hit.
SMARTi SM00729. Elp3. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00510. lipA. 1 hit.
ProtoNeti Search...

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: June 11, 2014
This is version 47 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

Documents

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

External Data

Dasty 3

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