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A1AMT5

- LIPA_PELPD

UniProt

A1AMT5 - LIPA_PELPD

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Protein

Lipoyl synthase

Gene

lipA

Organism
Pelobacter propionicus (strain DSM 2379)
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 bindingi60 – 601Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi65 – 651Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi71 – 711Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi86 – 861Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi90 – 901Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi93 – 931Iron-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

BioCyciPPRO338966:GHL0-1040-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:Ppro_1029
OrganismiPelobacter propionicus (strain DSM 2379)
Taxonomic identifieri338966 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesPelobacteraceaePelobacter
ProteomesiUP000006732: 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 – 314314Lipoyl synthasePRO_1000012252Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi338966.Ppro_1029.

Structurei

3D structure databases

ProteinModelPortaliA1AMT5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0320.
HOGENOMiHOG000235997.
KOiK03644.
OMAiHPHIPTK.
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.

A1AMT5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDVQPTTMRG AVKTAHLGTD VSLATKPLPK PEWLRGKSAS TPDVERLVRI
60 70 80 90 100
LRDNRLHTVC EEASCPNLGE CFRKGTATFM IMGDVCTRHC PFCNVAHGSP
110 120 130 140 150
HELAADEPVN LARAVELLKL SYVVITSVTR DDLPDGGAGH YGACVRALRD
160 170 180 190 200
LKRSLKVEIL TPDFRGAVAV AFEELRMNLP DVFNHNLETV PRLYPRVRPQ
210 220 230 240 250
ADYHGSLDLL LRFREQFDHV PTKSGLMLGL GETEQEVRDV MEELRRHRCD
260 270 280 290 300
MLTLGQYMRP SPHHLPVERY VTPDEFERYR QFGLSIGFSH VESGPMVRSS
310
YHADMQAREL MLVN
Length:314
Mass (Da):35,484
Last modified:January 23, 2007 - v1
Checksum:i222D9BADED7A669D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000482 Genomic DNA. Translation: ABK98655.1.
RefSeqiWP_011734959.1. NC_008609.1.
YP_900713.1. NC_008609.1.

Genome annotation databases

EnsemblBacteriaiABK98655; ABK98655; Ppro_1029.
GeneIDi4572769.
KEGGippd:Ppro_1029.
PATRICi22895113. VBIPelPro64470_1187.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000482 Genomic DNA. Translation: ABK98655.1 .
RefSeqi WP_011734959.1. NC_008609.1.
YP_900713.1. NC_008609.1.

3D structure databases

ProteinModelPortali A1AMT5.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 338966.Ppro_1029.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABK98655 ; ABK98655 ; Ppro_1029 .
GeneIDi 4572769.
KEGGi ppd:Ppro_1029.
PATRICi 22895113. VBIPelPro64470_1187.

Phylogenomic databases

eggNOGi COG0320.
HOGENOMi HOG000235997.
KOi K03644.
OMAi HPHIPTK.
OrthoDBi EOG6038ZS.

Enzyme and pathway databases

UniPathwayi UPA00538 ; UER00593 .
BioCyci PPRO338966:GHL0-1040-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. "Complete sequence of chromosome of Pelobacter propionicus DSM 2379."
    US DOE Joint Genome Institute
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.
    , Land M., Hauser L., Kyrpides N., Kim E., Lovley D., Richardson P.
    Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 2379.

Entry informationi

Entry nameiLIPA_PELPD
AccessioniPrimary (citable) accession number: A1AMT5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 57 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