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Protein

Lipoyl synthase

Gene

lipA

Organism
Corynebacterium sp. HMSC22B11
Status
Unreviewed-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 N6-(octanoyl)lysine + 2 sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + 2 reduced [2Fe-2S] ferredoxin = protein N6-(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: 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 bindingi55Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi60Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi66Iron-sulfur 1 (4Fe-4S)UniRule annotation1
Metal bindingi81Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi85Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation1
Metal bindingi88Iron-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:HMPREF3088_01155Imported
OrganismiCorynebacterium sp. HMSC22B11Imported
Taxonomic identifieri1581056 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesCorynebacteriaceaeCorynebacterium
Proteomesi
  • UP000179246 Componenti: Unassembled WGS sequence

Subcellular locationi

  • Cytoplasm UniRule annotationSAAS annotation

GO - Cellular componenti

Keywords - Cellular componenti

CytoplasmUniRule annotationSAAS annotation

Structurei

3D structure databases

SMRiA0A1F0CXR2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini71 – 277Elp3InterPro annotationAdd BLAST207

Sequence similaritiesi

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

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.

A0A1F0CXR2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTVSANGRRM LRIEAKNSQT PIEAKPRWIR TTAKMGPEYR DMKNRVTGMS
60 70 80 90 100
LHTVCQEAGC PNIHECWEDR EASFLIGGDT CSRRCDFCQI KSGKPTPLDR
110 120 130 140 150
DEPRRVAESV REMGLKYATV TGVTRDDLDD EGAWLYAEVV RKIHELNPNT
160 170 180 190 200
GVENLTPDFS NKPELLQIVF ESQPEVFAHN LETVPRIFKR IRPAFKYERS
210 220 230 240 250
LEVIRAAHDY GLITKSNLIL GMGETEEEVV EAMRDLREAG TDILTITQYL
260 270 280 290 300
RPTSMHHPIE RWVRPEEFVA HSEAAYDMGF PAVMSGPLVR SSYRSGRLYA
310 320 330 340
QAMRARGREI PENLSHLNEK LDGSTQQEAT NLLDKYGASE ETPVAYR
Length:347
Mass (Da):39,503
Last modified:February 15, 2017 - v1
Checksum:i9E125CDF7E5608E5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
LTNI01000007 Genomic DNA. Translation: OFO16743.1.
RefSeqiWP_012360497.1. NZ_KV823470.1.

Similar proteinsi

Entry informationi

Entry nameiA0A1F0CXR2_9CORY
AccessioniPrimary (citable) accession number: A0A1F0CXR2
Entry historyiIntegrated into UniProtKB/TrEMBL: February 15, 2017
Last sequence update: February 15, 2017
Last modified: October 25, 2017
This is version 7 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Caution

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

Keywords - Technical termi

Complete proteomeImported