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Protein

Lipoyl synthase 1

Gene

lipA1

Organism
Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / MED4)
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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi41 – 411Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi46 – 461Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi52 – 521Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi67 – 671Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi71 – 711Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi74 – 741Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-HAMAP
  2. lipoate synthase activity Source: UniProtKB-HAMAP
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. protein lipoylation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciPMAR59919:GJMQ-1554-MONOMER.
UniPathwayiUPA00538; UER00593.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipoyl synthase 1UniRule annotation (EC:2.8.1.8UniRule annotation)
Alternative name(s):
Lip-syn 1UniRule annotation
Lipoate synthase 1UniRule annotation
Lipoic acid synthase 1UniRule annotation
Sulfur insertion protein lipA1
Gene namesi
Name:lipA1UniRule annotation
Synonyms:lipA
Ordered Locus Names:PMM1514
OrganismiProchlorococcus marinus subsp. pastoris (strain CCMP1986 / MED4)
Taxonomic identifieri59919 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus
ProteomesiUP000001026: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 297297Lipoyl synthase 1PRO_0000102340Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi59919.PMM1514.

Structurei

3D structure databases

ProteinModelPortaliQ7UZY1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0320.
HOGENOMiHOG000235997.
KOiK03644.
OMAiEEYVTPE.
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.

Q7UZY1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTNISKNAVT KPDWLRVKAP QVERIGNTAN LLSDLKLNTV CQEASCPNIG
60 70 80 90 100
ECFASGTATF LIMGPGCTRA CPYCDIDFDR SKRDLDPTEP DRLAEAVFRL
110 120 130 140 150
KLKHVVITSV NRDDLDDGGA SQFYKCVSEV RKKSPETTIE LLIPDLCGNW
160 170 180 190 200
SALEKILDSR PNVLNHNIET VSALYRKVRP QGNYQRTLEL LKRTREYFPS
210 220 230 240 250
VYTKSGFMLG LGEKDDEVLT LLMDLRKNDV DIVTIGQYLS PGPKHLQVQR
260 270 280 290
FVTPSKFNYF KLFGENELGF MQVVSSPLTR SSYHAEEIQK LMKKFPR
Length:297
Mass (Da):33,662
Last modified:October 1, 2003 - v1
Checksum:iE17EE4F68A67FC89
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX548174 Genomic DNA. Translation: CAE19973.1.
RefSeqiNP_893631.1. NC_005072.1.

Genome annotation databases

EnsemblBacteriaiCAE19973; CAE19973; PMM1514.
GeneIDi1726165.
KEGGipmm:PMM1514.
PATRICi23034206. VBIProMar68066_1756.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX548174 Genomic DNA. Translation: CAE19973.1.
RefSeqiNP_893631.1. NC_005072.1.

3D structure databases

ProteinModelPortaliQ7UZY1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi59919.PMM1514.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAE19973; CAE19973; PMM1514.
GeneIDi1726165.
KEGGipmm:PMM1514.
PATRICi23034206. VBIProMar68066_1756.

Phylogenomic databases

eggNOGiCOG0320.
HOGENOMiHOG000235997.
KOiK03644.
OMAiEEYVTPE.
OrthoDBiEOG6038ZS.

Enzyme and pathway databases

UniPathwayiUPA00538; UER00593.
BioCyciPMAR59919:GJMQ-1554-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: CCMP1986 / MED4.

Entry informationi

Entry nameiLIPA1_PROMP
AccessioniPrimary (citable) accession number: Q7UZY1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: October 1, 2003
Last modified: March 4, 2015
This is version 82 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.