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Q9PJI2

- LIPA_CHLMU

UniProt

Q9PJI2 - LIPA_CHLMU

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Protein

Lipoyl synthase

Gene

lipA

Organism
Chlamydia muridarum (strain MoPn / Nigg)
Status
Reviewed - 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 = protein N(6)-(lipoyl)lysine + 2 (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine.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 bindingi48 – 481Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi53 – 531Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi59 – 591Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi74 – 741Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi78 – 781Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi81 – 811Iron-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

BioCyciCMUR243161:GHYU-877-MONOMER.
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
Ordered Locus Names:TC_0847
OrganismiChlamydia muridarum (strain MoPn / Nigg)
Taxonomic identifieri243161 [NCBI]
Taxonomic lineageiBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia
ProteomesiUP000000800: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 308308Lipoyl synthasePRO_0000102303Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi243161.TC0847.

Structurei

3D structure databases

ProteinModelPortaliQ9PJI2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0320.
KOiK03644.
OMAiRPMMSET.
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.

Q9PJI2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSNSPESSTP KQSIPARFPK WLRQKLPLGK VFSRTDGTIK NKGLPTVCEE
60 70 80 90 100
ASCPNRTHCW SRHTATYLAL GDACTRRCGF CDIDFTKKPL PPDPQEGEKI
110 120 130 140 150
AASAKALGLK HIVITMVSRD DLEDGGADAL ARIITTLHIE LPEATIEVLA
160 170 180 190 200
SDFEGNIDAL HHLLDARIAI YNHNVETVER LSPLVRHKAT YRRSLMMLEQ
210 220 230 240 250
AAQYLPDLMI KSGIMVGLGE QESEIKQTLK DLADHGVKIV TIGQYLRPSR
260 270 280 290 300
RHIPVKSYVS PETFDYYRSV GEALGLFIYA GPFVRSSFNA DAVFEAMSQR

ERLSASIQ
Length:308
Mass (Da):34,278
Last modified:October 1, 2000 - v1
Checksum:i617846CB79C12A92
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE002160 Genomic DNA. Translation: AAF39645.1.
PIRiC81658.
RefSeqiNP_297220.1. NC_002620.2.

Genome annotation databases

EnsemblBacteriaiAAF39645; AAF39645; TC_0847.
GeneIDi1246215.
KEGGicmu:TC_0847.
PATRICi20373208. VBIChlMur19118_0908.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE002160 Genomic DNA. Translation: AAF39645.1 .
PIRi C81658.
RefSeqi NP_297220.1. NC_002620.2.

3D structure databases

ProteinModelPortali Q9PJI2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 243161.TC0847.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAF39645 ; AAF39645 ; TC_0847 .
GeneIDi 1246215.
KEGGi cmu:TC_0847.
PATRICi 20373208. VBIChlMur19118_0908.

Phylogenomic databases

eggNOGi COG0320.
KOi K03644.
OMAi RPMMSET.
OrthoDBi EOG6038ZS.

Enzyme and pathway databases

UniPathwayi UPA00538 ; UER00593 .
BioCyci CMUR243161:GHYU-877-MONOMER.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
HAMAPi MF_00206. Lipoyl_synth.
InterProi IPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
[Graphical view ]
PANTHERi PTHR10949. PTHR10949. 1 hit.
Pfami PF04055. Radical_SAM. 1 hit.
[Graphical view ]
PIRSFi PIRSF005963. Lipoyl_synth. 1 hit.
SMARTi SM00729. Elp3. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00510. lipA. 1 hit.
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MoPn / Nigg.

Entry informationi

Entry nameiLIPA_CHLMU
AccessioniPrimary (citable) accession number: Q9PJI2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: October 1, 2000
Last modified: November 26, 2014
This is version 99 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

Documents

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

External Data

Dasty 3