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Q1GYC1 (LIPA_METFK) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 58. 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

EC=2.8.1.8
Alternative name(s):
Lip-syn
Short name=LS
Lipoate synthase
Lipoic acid synthase
Sulfur insertion protein LipA
Gene names
Name:lipA
Ordered Locus Names:Mfla_2501
OrganismMethylobacillus flagellatus (strain KT / ATCC 51484 / DSM 6875) [Complete proteome] [HAMAP]
Taxonomic identifier265072 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaMethylophilalesMethylophilaceaeMethylobacillus

Protein attributes

Sequence length325 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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_00206

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_00206

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_00206

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_00206.

Sequence similarities

Belongs to the radical SAM superfamily. Lipoyl synthase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Ligand4Fe-4S
Iron
Iron-sulfur
Metal-binding
S-adenosyl-L-methionine
   Molecular functionTransferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processprotein lipoylation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

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

Chain1 – 325325Lipoyl synthase HAMAP-Rule MF_00206
PRO_0000325276

Sites

Metal binding711Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding761Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding821Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding971Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1011Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
Metal binding1041Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1GYC1 [UniParc].

Last modified June 27, 2006. Version 1.
Checksum: AFE66D27AED7C95E

FASTA32536,464
        10         20         30         40         50         60 
MTEITERIVP PPRKVAGVKE SSAEKMARIP IKIIPMPAMR KPEWIRMKVP DSARFREIKQ 

        70         80         90        100        110        120 
VLRENNLHTV CEEASCPNIG ECFSGGTATF MILGDICTRR CPFCDVSHGK PLPPDANEPE 

       130        140        150        160        170        180 
NLGRTIAQMR LKYVVITSVD RDDLRDGGAQ HFVDCIAAVR AHSPQIKVEI LVPDFRGRLD 

       190        200        210        220        230        240 
RAIHILKAAP PDVMNHNLET VPRLYKEARP GSDYQNSLDL LKEFGKLHPE VPTKSGLMLG 

       250        260        270        280        290        300 
LGETDEEILD VMRDLRAHNV TMLTLGQYLQ PSPHHLPVKR FVTPQRFAEF ERQALAMGFT 

       310        320 
HAACGPMVRS SYHADHQAQQ AGVNF 

« Hide

References

[1]"Complete sequence of Methylobacillus flagellatus KT."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Kyrpides N., Anderson I., Richardson P.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KT / ATCC 51484 / DSM 6875.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000284 Genomic DNA. Translation: ABE50766.1.
RefSeqYP_546607.1. NC_007947.1.

3D structure databases

ProteinModelPortalQ1GYC1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING265072.Mfla_2501.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE50766; ABE50766; Mfla_2501.
GeneID4001597.
KEGGmfa:Mfla_2501.
PATRIC32270825. VBIMetFla97085_2621.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0320.
HOGENOMHOG000235997.
KOK03644.
OMAEEYVTPE.
OrthoDBEOG6038ZS.
ProtClustDBPRK05481.

Enzyme and pathway databases

BioCycMFLA265072:GHWJ-2560-MONOMER.
UniPathwayUPA00538; UER00593.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00206. Lipoyl_synth.
InterProIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
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 nameLIPA_METFK
AccessionPrimary (citable) accession number: Q1GYC1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: June 27, 2006
Last modified: February 19, 2014
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways