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Protein

Lipoyl synthase, mitochondrial

Gene

CAGL0I10923g

Organism
Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata)
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 bindingi120 – 1201Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi125 – 1251Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi131 – 1311Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi151 – 1511Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi155 – 1551Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi158 – 1581Iron-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
Ordered Locus Names:CAGL0I10923g
OrganismiCandida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata)
Taxonomic identifieri284593 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeNakaseomycesNakaseomyces/Candida clade
ProteomesiUP000002428: Chromosome I

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 – 1818MitochondrionUniRule annotationAdd
BLAST
Chaini19 – 388370Lipoyl synthase, mitochondrialPRO_0000398260Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ6FPY0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

InParanoidiQ6FPY0.
KOiK03644.
OMAiEEYVTPE.
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.

Q6FPY0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLTTVQRRF LVSTKAKVSG ASISSTANTG SASAGAPNGQ TRRRRRITEF
60 70 80 90 100
KDALNLGPSF EDFVSGRAAG FTVVDPLEQM RQDREEYKKL PKWLKVPIPK
110 120 130 140 150
GVNYHKLKKD VKELKLSTVC EEARCPNIGE CWGGKDKSKA TATIMLLGDT
160 170 180 190 200
CTRGCRFCSV KTNRNPAKPD PTEPENTAEA ISRWGLGYVV LTTVDRDDLP
210 220 230 240 250
DGGAHHLAET VIKIKQKAPK TLVEALTGDF LGNLEMVDVM AKSGLDVYAH
260 270 280 290 300
NLETVEALTP HVRDRRAGYR QSLNVLKRAK ETVPSLITKT SVMLGLGETD
310 320 330 340 350
DQIIQTMQDL RAINCDVITF GQYMRPTKRH MKVVEYVRPE KFDYWKDKAK
360 370 380
EMGFLYCASG PLVRSSYKAG EAFIENVLNK RKQDNKRI
Length:388
Mass (Da):43,401
Last modified:July 19, 2004 - v1
Checksum:i457598F13CF7B740
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR380955 Genomic DNA. Translation: CAG60659.1.
RefSeqiXP_447714.1. XM_447714.1.

Genome annotation databases

GeneIDi2889354.
KEGGicgr:CAGL0I10923g.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR380955 Genomic DNA. Translation: CAG60659.1.
RefSeqiXP_447714.1. XM_447714.1.

3D structure databases

ProteinModelPortaliQ6FPY0.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2889354.
KEGGicgr:CAGL0I10923g.

Phylogenomic databases

InParanoidiQ6FPY0.
KOiK03644.
OMAiEEYVTPE.
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]
PIRSFiPIRSF005963. Lipoyl_synth. 1 hit.
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00510. lipA. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiLIPA_CANGA
AccessioniPrimary (citable) accession number: Q6FPY0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: July 19, 2004
Last modified: March 4, 2015
This is version 76 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.