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Protein

Lipoyl synthase

Gene

lipA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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 annotation1 Publication

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

Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein].

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi40 – 401Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi45 – 451Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi51 – 511Iron-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
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. lipoate biosynthetic process Source: UniProtKB
  2. protein lipoylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciBSUB:BSU32330-MONOMER.
MetaCyc:BSU32330-MONOMER.
SABIO-RKO32129.

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
Synonyms:yutB
Ordered Locus Names:BSU32330
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570 Componenti: Chromosome

Organism-specific databases

GenoListiBSU32330. [Micado]

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Disruption of this gene interrupts lipoate-dependent reactions, which strongly inhibits growth in minimal medium, impairing the generation of branched-chain fatty acids and leading to accumulation of copious amounts of straight-chain saturated fatty acids in B.subtilis membranes.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 298298Lipoyl synthasePRO_0000102288Add
BLAST

Proteomic databases

PaxDbiO32129.

Interactioni

Protein-protein interaction databases

STRINGi224308.BSU32330.

Structurei

3D structure databases

ProteinModelPortaliO32129.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0320.
HOGENOMiHOG000235998.
InParanoidiO32129.
KOiK03644.
OMAiEEYVTPE.
OrthoDBiEOG6038ZS.
PhylomeDBiO32129.

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.

O32129-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKKDEHLRK PEWLKIKLNT NENYTGLKKL MRENNLHTVC EEAKCPNIHE
60 70 80 90 100
CWAVRRTATF MILGSVCTRA CRFCAVKTGL PTELDLQEPE RVADSVALMN
110 120 130 140 150
LKHAVITAVA RDDQKDGGAG IFAETVRAIR RKSPFTTIEV LPSDMGGNYD
160 170 180 190 200
NLKTLMDTRP DILNHNIETV RRLTPRVRAR ATYDRSLEFL RRAKEMQPDI
210 220 230 240 250
PTKSSIMIGL GETKEEIIEV MDDLLANNVD IMAIGQYLQP TKKHLKVQKY
260 270 280 290
YHPDEFAELK EIAMQKGFSH CEAGPLVRSS YHADEQVNEA SKKRQAQA
Length:298
Mass (Da):33,921
Last modified:May 30, 2000 - v2
Checksum:iE6BEEB81C6ECC6FF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB15223.2.
PIRiD70023.
RefSeqiNP_391113.2. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB15223; CAB15223; BSU32330.
GeneIDi938861.
KEGGibsu:BSU32330.
PATRICi18978438. VBIBacSub10457_3382.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB15223.2.
PIRiD70023.
RefSeqiNP_391113.2. NC_000964.3.

3D structure databases

ProteinModelPortaliO32129.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.BSU32330.

Proteomic databases

PaxDbiO32129.

Protocols and materials databases

DNASUi938861.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15223; CAB15223; BSU32330.
GeneIDi938861.
KEGGibsu:BSU32330.
PATRICi18978438. VBIBacSub10457_3382.

Organism-specific databases

GenoListiBSU32330. [Micado]

Phylogenomic databases

eggNOGiCOG0320.
HOGENOMiHOG000235998.
InParanoidiO32129.
KOiK03644.
OMAiEEYVTPE.
OrthoDBiEOG6038ZS.
PhylomeDBiO32129.

Enzyme and pathway databases

BioCyciBSUB:BSU32330-MONOMER.
MetaCyc:BSU32330-MONOMER.
SABIO-RKO32129.

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

« Hide 'large scale' publications
  1. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  2. "A lipA (yutB) mutant, encoding lipoic acid synthase, provides insight into the interplay between branched-chain and unsaturated fatty acid biosynthesis in Bacillus subtilis."
    Martin N., Lombardia E., Altabe S.G., de Mendoza D., Mansilla M.C.
    J. Bacteriol. 191:7447-7455(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A LIPOYL SYNTHASE, PATHWAY, DISRUPTION PHENOTYPE.
    Strain: 168 / JH642.

Entry informationi

Entry nameiLIPA_BACSU
AccessioniPrimary (citable) accession number: O32129
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: March 4, 2015
This is version 119 of the entry and version 2 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. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.