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B0SYD1 (B0SYD1_CAUSK) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Lipoyl synthase HAMAP-Rule MF_00206
EC=2.8.1.8 HAMAP-Rule MF_00206
Alternative name(s):
Lip-syn HAMAP-Rule MF_00206
Lipoate synthase HAMAP-Rule MF_00206
Lipoic acid synthase HAMAP-Rule MF_00206
Sulfur insertion protein LipA HAMAP-Rule MF_00206
Gene names
Name:lipA HAMAP-Rule MF_00206
Ordered Locus Names:Caul_2751 EMBL ABZ71878.1
OrganismCaulobacter sp. (strain K31) [Complete proteome] [HAMAP] EMBL ABZ71878.1
Taxonomic identifier366602 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Caulobacterales › Caulobacteraceae › Caulobacter

Protein attributes

Sequence length351 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 + 2 S-adenosyl-L-methionine = protein N(6)-(lipoyl)lysine + 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. HAMAP-Rule MF_00206

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 By similarity SAAS SAAS003698 HAMAP-Rule MF_00206.

Sequence similarities

Belongs to the radical SAM superfamily. Lipoyl synthase family. HAMAP-Rule MF_00206

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Metal binding851Iron-sulfur 1 (4Fe-4S) By similarity HAMAP-Rule MF_00206
Metal binding901Iron-sulfur 1 (4Fe-4S) By similarity HAMAP-Rule MF_00206
Metal binding961Iron-sulfur 1 (4Fe-4S) By similarity HAMAP-Rule MF_00206
Metal binding1111Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity HAMAP-Rule MF_00206
Metal binding1151Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity HAMAP-Rule MF_00206
Metal binding1181Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity HAMAP-Rule MF_00206

Sequences

Sequence LengthMass (Da)Tools
B0SYD1 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 64E79F6474AE7D02

FASTA35138,935
        10         20         30         40         50         60 
MQERMLDPDA KKSDLGLMVT LIDTLSPRAP EAHPGDRAVR HPEKQNRPDT PVLRKPEWLR 

        70         80         90        100        110        120 
VRAPGSPGYN ETRSIVRDHK LTTVCEEAAC PNIGECWSQR HATMMIMGEI CTRACAFCNV 

       130        140        150        160        170        180 
STGLPNALDA DEPRRVAEAV AKMGLKHVVI TSVDRDDLAD GGARHFAEVV LAIRAAAPGT 

       190        200        210        220        230        240 
TIEILTPDFL RKDRAENVVI DARPDVFNHN LETVPRLYLK IRPGARYYHS LRLLERVKER 

       250        260        270        280        290        300 
DPSRFTKSGL MVGLGETKEE VMQVMDDMRS AGVDFITIGQ YLQPTRKHAA VDRFVTPDEF 

       310        320        330        340        350 
KAYEAIARAK GFLMVSASPL TRSSHHAGED FAKLQAARRA LDAQSPGPKA G

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References

[1]"Complete sequence of chromosome of Caulobacter sp. K31."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Bruce D., Goodwin L., Thompson L.S., Brettin T., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Kim E., Stephens C., Richardson P.
Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K31 EMBL ABZ71878.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000927 Genomic DNA. Translation: ABZ71878.1.
RefSeqYP_001684376.1. NC_010338.1.

3D structure databases

ProteinModelPortalB0SYD1.
ModBaseSearch...

Protein-protein interaction databases

STRING366602.Caul_2751.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABZ71878; ABZ71878; Caul_2751.
GeneID5900206.
KEGGcak:Caul_2751.
PATRIC21318578. VBICauSp18104_3146.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0320.
HOGENOMHOG000235997.
KOK03644.
OMAEEYVTPE.
ProtClustDBPRK05481.

Enzyme and pathway databases

BioCycCSP366602:GH0Y-2749-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 nameB0SYD1_CAUSK
AccessionPrimary (citable) accession number: B0SYD1
Entry history
Integrated into UniProtKB/TrEMBL: April 8, 2008
Last sequence update: April 8, 2008
Last modified: May 1, 2013
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info