Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Lipoyl synthase

Gene

lipA

Organism
Ochrobactrum sp. EGD-AQ16
Status
Unreviewed-Annotation score: -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

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.Imported

Catalytic activityi

Protein N6-(octanoyl)lysine + an [Fe-S] cluster scaffold protein carrying a [4Fe-4S]2+ cluster + 2 S-adenosyl-L-methionine + 6 reduced [2Fe-2S] ferredoxin + 6 H+ = protein N6-(dihydrolipoyl)lysine + an [Fe-S] cluster scaffold protein + 2 sulfide + 4 Fe3+ + 2 L-methionine + 2 5'-deoxyadenosine + 6 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: protein lipoylation via endogenous pathway

This protein is involved in step 2 of the subpathway that synthesizes protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein].UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Octanoyltransferase (lipB)
  2. Lipoyl synthase (lipA)
This subpathway is part of the pathway protein lipoylation via endogenous pathway, which is itself part of Protein modification.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein], the pathway protein lipoylation via endogenous pathway and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi60Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi65Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi71Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi86Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi90Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi93Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionTransferaseUniRule annotation
Ligand4Fe-4SUniRule annotation, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionineUniRule annotation

Enzyme and pathway databases

UniPathwayiUPA00538; UER00593

Names & Taxonomyi

Protein namesi
Recommended name:
Lipoyl synthaseUniRule annotation (EC:2.8.1.8UniRule annotation)
Alternative name(s):
Lip-synUniRule annotation
Short name:
LSUniRule annotation
Lipoate synthaseUniRule annotation
Lipoic acid synthaseUniRule annotation
Sulfur insertion protein LipAUniRule annotation
Gene namesi
Name:lipAUniRule annotation
ORF Names:O206_02065Imported
OrganismiOchrobactrum sp. EGD-AQ16Imported
Taxonomic identifieri1390361 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeOchrobactrum
Proteomesi
  • UP000016518 Componenti: Unassembled WGS sequence

Subcellular locationi

  • Cytoplasm UniRule annotationSAAS annotation

GO - Cellular componenti

Keywords - Cellular componenti

CytoplasmUniRule annotationSAAS annotation

Structurei

3D structure databases

ProteinModelPortaliU1X6S6
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini76 – 283Elp3InterPro annotationAdd BLAST208

Sequence similaritiesi

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

Phylogenomic databases

OrthoDBiPOG091H069D

Family and domain databases

Gene3Di3.20.20.70, 1 hit
HAMAPiMF_00206 Lipoyl_synth, 1 hit
InterProiView protein in InterPro
IPR013785 Aldolase_TIM
IPR006638 Elp3/MiaB/NifB
IPR031691 LIAS_N
IPR003698 Lipoyl_synth
IPR007197 rSAM
PfamiView protein in Pfam
PF16881 LIAS_N, 1 hit
PF04055 Radical_SAM, 1 hit
PIRSFiPIRSF005963 Lipoyl_synth, 1 hit
SFLDiSFLDG01058 lipoyl_synthase_like, 1 hit
SFLDS00029 Radical_SAM, 1 hit
SMARTiView protein in SMART
SM00729 Elp3, 1 hit
TIGRFAMsiTIGR00510 lipA, 1 hit

Sequencei

Sequence statusi: Complete.

U1X6S6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVTVLDLVNQ GKRERHPEKA HRPDNVVLKK PDWIRVKAPV SRGYSETRDI
60 70 80 90 100
VRSNKLVTVC EEAGCPNIGE CWEKKHATFM IMGEICTRAC AFCNVSTGIP
110 120 130 140 150
TALDPNEPEN VAKAVKQMGL THVVITSVDR DDLADGGAQH FAEVIQAIRE
160 170 180 190 200
ATPATTIEIL TPDFLRKEGA LEIVVKARPD VFNHNLETVP SKYLKVRPGA
210 220 230 240 250
RYFHSIRLLQ RVKELDPTIF TKSGIMVGLG EERNEILQLM DDLRSADVDF
260 270 280 290 300
MTIGQYLQPT RKHHPVIRFV TPDEFKSFET IGRTKGFLLV ASSPLTRSSH
310 320
HAGDDFAKLR AAREAQIAAR A
Length:321
Mass (Da):35,884
Last modified:November 13, 2013 - v1
Checksum:iFDC41674CF295651
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AWEU01000001 Genomic DNA Translation: ERI16544.1
RefSeqiWP_006470529.1, NZ_AWEU01000001.1

Genome annotation databases

EnsemblBacteriaiERI16544; ERI16544; O206_02065
PATRICifig|1390361.3.peg.415

Similar proteinsi

Entry informationi

Entry nameiU1X6S6_9RHIZ
AccessioniPrimary (citable) accession number: U1X6S6
Entry historyiIntegrated into UniProtKB/TrEMBL: November 13, 2013
Last sequence update: November 13, 2013
Last modified: June 20, 2018
This is version 37 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health