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Protein

Lipoyl synthase 2

Gene

lipA2

Organism
Prochlorococcus marinus (strain SARG / CCMP1375 / SS120)
Status
Reviewed-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 N(6)-(octanoyl)lysine + 2 sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + 2 reduced [2Fe-2S] ferredoxin = protein N(6)-(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

Pathway:iprotein 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 2 (lipA2), Lipoyl synthase 1 (lipA1)
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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi49 – 491Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi54 – 541Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi60 – 601Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi75 – 751Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi79 – 791Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi82 – 821Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciPMAR167539:GJN2-1126-MONOMER.
UniPathwayiUPA00538; UER00593.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipoyl synthase 2UniRule annotation (EC:2.8.1.8UniRule annotation)
Alternative name(s):
Lip-syn 2UniRule annotation
Lipoate synthase 2UniRule annotation
Lipoic acid synthase 2UniRule annotation
Sulfur insertion protein lipA2
Gene namesi
Name:lipA2UniRule annotation
Synonyms:lipA
Ordered Locus Names:Pro_1099
OrganismiProchlorococcus marinus (strain SARG / CCMP1375 / SS120)
Taxonomic identifieri167539 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus
ProteomesiUP000001420 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 308308Lipoyl synthase 2PRO_0000102337Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi167539.Pro1099.

Structurei

3D structure databases

ProteinModelPortaliQ7VBJ3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0320.
KOiK03644.
OMAiRSCAFCQ.
OrthoDBiEOG6038ZS.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00206. Lipoyl_synth.
InterProiIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
[Graphical view]
PANTHERiPTHR10949. PTHR10949. 1 hit.
PfamiPF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFiPIRSF005963. Lipoyl_synth. 1 hit.
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00510. lipA. 1 hit.

Sequencei

Sequence statusi: Complete.

Q7VBJ3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTTNKKTRY SAIKPSERLP EWIKPSLGTA SQLEKVQNLV KEYRLNTICE
60 70 80 90 100
EGRCPNRGEC YASGTATFLL GGSICTRSCA FCQVEKGMPP QNIDPNESIR
110 120 130 140 150
VAKAVLKLQL KYVVLTSVAR DDLDDHGAIH FSRTIHAIRK TSPTTSIEVL
160 170 180 190 200
TPDFWGGCID KIKATKIQRE RLKIVLKAKP VCFNHNLETV ERLQKEVRRG
210 220 230 240 250
ATYHRSLELL KASREIDNEI PTKSGLMLGL GERSDEIIQT LKDLRSVNCQ
260 270 280 290 300
QVTIGQYLRP SLAHIPVQKY WLPKDFEHFK RIAEGLGFKK VNSGPLVRSS

YHAELPQT
Length:308
Mass (Da):34,785
Last modified:October 1, 2003 - v1
Checksum:iA6760C5902291F92
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017126 Genomic DNA. Translation: AAQ00144.1.
RefSeqiNP_875491.1. NC_005042.1.
WP_011125251.1. NC_005042.1.

Genome annotation databases

EnsemblBacteriaiAAQ00144; AAQ00144; Pro_1099.
GeneIDi1462481.
KEGGipma:Pro_1099.
PATRICi23028917. VBIProMar8617_1149.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017126 Genomic DNA. Translation: AAQ00144.1.
RefSeqiNP_875491.1. NC_005042.1.
WP_011125251.1. NC_005042.1.

3D structure databases

ProteinModelPortaliQ7VBJ3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi167539.Pro1099.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAQ00144; AAQ00144; Pro_1099.
GeneIDi1462481.
KEGGipma:Pro_1099.
PATRICi23028917. VBIProMar8617_1149.

Phylogenomic databases

eggNOGiCOG0320.
KOiK03644.
OMAiRSCAFCQ.
OrthoDBiEOG6038ZS.

Enzyme and pathway databases

UniPathwayiUPA00538; UER00593.
BioCyciPMAR167539:GJN2-1126-MONOMER.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00206. Lipoyl_synth.
InterProiIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
[Graphical view]
PANTHERiPTHR10949. PTHR10949. 1 hit.
PfamiPF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFiPIRSF005963. Lipoyl_synth. 1 hit.
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00510. lipA. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SARG / CCMP1375 / SS120.

Entry informationi

Entry nameiLIPA2_PROMA
AccessioniPrimary (citable) accession number: Q7VBJ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: October 1, 2003
Last modified: July 22, 2015
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.