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Protein

Lipoyl synthase, mitochondrial

Gene

AO090020000344

Organism
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
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:AO090020000344
OrganismiAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Taxonomic identifieri510516 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006564: Chromosome 6

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 – 3232MitochondrionUniRule annotationAdd
BLAST
Chaini33 – 415383Lipoyl synthase, mitochondrialPRO_0000398256Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi5062.CADAORAP00006700.

Structurei

3D structure databases

ProteinModelPortaliQ2U4H2.
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]
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.

Q2U4H2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASTNRLRF LYSSARTVPQ TGSITPISRR TYATTEPSPS ATGAPATARK
60 70 80 90 100
RTNFTDKLNA GPSFADFVSG GEDNAPLEPS EAYALKTAMV GPAGRKKEMT
110 120 130 140 150
RLPSWLKTPI PDSKNYQRLK KDLRGLNLHT VCEEARCPNI SDCWGGSDKS
160 170 180 190 200
AATATIMLMG DTCTRGCRFC SVKTNRRPPP LDPHEPENTA EAISRWSLGY
210 220 230 240 250
VVLTSVDRDD LADGGARHFA ETVIKIKQKK PSMLVECLTG DYLGDLEMVK
260 270 280 290 300
LVARSGLDVY AHNVETVEAL TPFVRDRRAT FQQSLRVLEA AKQARPDLIT
310 320 330 340 350
KTSLMLGFGE TEEQLWDALR QLRSVGVDVV TFGQYMRPTK RHMPVHEYVT
360 370 380 390 400
PDQFELWRQR ALDMGFLYCA SGPLVRSSYK AGEAFIENVL KKRRAAGTAG
410
ESVTDSKAAV DEATR
Length:415
Mass (Da):45,818
Last modified:January 24, 2006 - v1
Checksum:iD70539BCDC1DF0FB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP007167 Genomic DNA. Translation: BAE63543.1.
RefSeqiXP_001824676.1. XM_001824624.2.

Genome annotation databases

EnsemblFungiiCADAORAT00006831; CADAORAP00006700; CADAORAG00006831.
GeneIDi5996762.
KEGGiaor:AOR_1_608084.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP007167 Genomic DNA. Translation: BAE63543.1.
RefSeqiXP_001824676.1. XM_001824624.2.

3D structure databases

ProteinModelPortaliQ2U4H2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5062.CADAORAP00006700.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADAORAT00006831; CADAORAP00006700; CADAORAG00006831.
GeneIDi5996762.
KEGGiaor:AOR_1_608084.

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

Publicationsi

  1. "Genome sequencing and analysis of Aspergillus oryzae."
    Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.
    , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H.
    Nature 438:1157-1161(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 42149 / RIB 40.

Entry informationi

Entry nameiLIPA_ASPOR
AccessioniPrimary (citable) accession number: Q2U4H2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: January 24, 2006
Last modified: March 4, 2015
This is version 61 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.