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B8A031 (LIAS_MAIZE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 33. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:LIP1
OrganismZea mays (Maize)
Taxonomic identifier4577 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogoneaeZea

Protein attributes

Sequence length383 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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. HAMAP-Rule MF_03128

Catalytic activity

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. HAMAP-Rule MF_03128

Cofactor

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

Pathway

Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 2/2. HAMAP-Rule MF_03128

Subcellular location

Mitochondrion By similarity HAMAP-Rule MF_03128.

Sequence similarities

Belongs to the radical SAM superfamily. Lipoyl synthase family.

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   Ligand4Fe-4S
Iron
Iron-sulfur
Metal-binding
S-adenosyl-L-methionine
   Molecular functionTransferase
Gene Ontology (GO)
   Biological_processprotein lipoylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function4 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

lipoate synthase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 383Lipoyl synthase, mitochondrial HAMAP-Rule MF_03128PRO_0000398846

Sites

Metal binding1101Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1151Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1211Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding1411Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1451Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1481Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
B8A031 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: D049717212C2F537

FASTA38341,886
        10         20         30         40         50         60 
MHGRRHLAAS LTRALIQAPS RSISSTPSLL QTLDPSVPSP PAAGAGRLAE LRRRLQADAP 

        70         80         90        100        110        120 
SLGDFTYSVE VGTRQRPLPK PKWMKETVPG GAKYAAIKAK LRELKLHTVC EEARCPNLGE 

       130        140        150        160        170        180 
CWSGGETGTA TATIMILGDT CTRGCRFCNV KTSRTPPPPD PDEPSNVAQA IASWGLEYIV 

       190        200        210        220        230        240 
ITSVDRDDLP DQGSGHFAET VQKLKALKPE MLIEALVPDF RGDPSCVEKV ATSGLHVFAH 

       250        260        270        280        290        300 
NIETVEELQR NVRDYRANFK QSIDVLEMAK EYAPPGTLTK TSIMLGCGET PDQVIRTMEK 

       310        320        330        340        350        360 
VRAADVDVIT FGQYMRPSKR HMPVSEYVTP EAFEKYRALG VEMGFRYVAS GPMVRSSYKA 

       370        380 
GEFYIKAMIE AERAKGTAAD SSA 

« Hide

References

[1]"Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs."
Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J., Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J., Walbot V., Yu Y.
PLoS Genet. 5:E1000740-E1000740(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: B73.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BT054923 mRNA. Translation: ACL53530.1.
BT061114 mRNA. Translation: ACN25811.1.
BT086520 mRNA. Translation: ACR36873.1.
RefSeqNP_001146235.1. NM_001152763.1.
UniGeneZm.6442.

3D structure databases

ProteinModelPortalB8A031.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100279807.
KEGGzma:100279807.

Organism-specific databases

GrameneB8A031.

Phylogenomic databases

HOGENOMHOG000235998.
KOK03644.
OMAVQKYWTP.

Enzyme and pathway databases

UniPathwayUPA00538; UER00593.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00206. Lipoyl_synth.
MF_03128. Lipoyl_synth_plantM.
InterProIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR027527. Lipoyl_synth_mt.
IPR007197. rSAM.
[Graphical view]
PANTHERPTHR10949. PTHR10949. 1 hit.
PfamPF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFPIRSF005963. Lipoyl_synth. 1 hit.
SMARTSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsTIGR00510. lipA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameLIAS_MAIZE
AccessionPrimary (citable) accession number: B8A031
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: March 3, 2009
Last modified: February 19, 2014
This is version 33 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways