UniProtKB - O32129 (LIPA_BACSU)
Protein
Lipoyl synthase
Gene
lipA
Organism
Bacillus subtilis (strain 168)
Status
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
- [[Fe-S] cluster scaffold protein carrying a second [4Fe-4S]2+ cluster] + 4 H+ + N6-octanoyl-L-lysyl-[protein] + 2 oxidized [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = (R)-N6-dihydrolipoyl-L-lysyl-[protein] + 2 5'-deoxyadenosine + [[Fe-S] cluster scaffold protein] + 4 Fe3+ + 2 hydrogen sulfide + 2 L-methionine + 2 reduced [2Fe-2S]-[ferredoxin]UniRule annotationEC:2.8.1.8UniRule 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
: protein lipoylation via endogenous pathway Pathwayi
This protein is involved in the subpathway that synthesizes protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein].UniRule annotation1 Publication 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 pathway protein lipoylation via endogenous pathway and in Protein modification.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 40 | Iron-sulfur 1 (4Fe-4S)UniRule annotation | 1 | |
Metal bindingi | 45 | Iron-sulfur 1 (4Fe-4S)UniRule annotation | 1 | |
Metal bindingi | 51 | Iron-sulfur 1 (4Fe-4S)UniRule annotation | 1 | |
Metal bindingi | 67 | Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation | 1 | |
Metal bindingi | 71 | Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation | 1 | |
Metal bindingi | 74 | Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation | 1 | |
Metal bindingi | 280 | Iron-sulfur 1 (4Fe-4S)UniRule annotation | 1 |
GO - Molecular functioni
- 4 iron, 4 sulfur cluster binding Source: UniProtKB-UniRule
- lipoate synthase activity Source: UniProtKB
- lipoyl synthase activity (acting on glycine-cleavage complex H protein Source: UniProtKB-EC
- lipoyl synthase activity (acting on pyruvate dehydrogenase E2 protein) Source: UniProtKB-EC
- metal ion binding Source: UniProtKB-KW
GO - Biological processi
- lipoate biosynthetic process Source: UniProtKB
- protein lipoylation Source: UniProtKB
Keywordsi
Molecular function | Transferase |
Ligand | 4Fe-4S, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine |
Enzyme and pathway databases
BioCyci | BSUB:BSU32330-MONOMER MetaCyc:BSU32330-MONOMER |
SABIO-RKi | O32129 |
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 |
Organismi | Bacillus subtilis (strain 168) |
Taxonomic identifieri | 224308 [NCBI] |
Taxonomic lineagei | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › |
Proteomesi |
|
Subcellular locationi
- Cytoplasm UniRule annotation
GO - Cellular componenti
- cytoplasm Source: UniProtKB-SubCell
Keywords - Cellular componenti
CytoplasmPathology & 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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000102288 | 1 – 298 | Lipoyl synthaseAdd BLAST | 298 |
Proteomic databases
jPOSTi | O32129 |
PaxDbi | O32129 |
PRIDEi | O32129 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 53 – 269 | Radical SAM corePROSITE-ProRule annotationAdd BLAST | 217 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG0320, Bacteria |
InParanoidi | O32129 |
OMAi | PYCDIDF |
PhylomeDBi | O32129 |
Family and domain databases
Gene3Di | 3.20.20.70, 1 hit |
HAMAPi | MF_00206, Lipoyl_synth, 1 hit |
InterProi | View protein in InterPro IPR013785, Aldolase_TIM IPR006638, Elp3/MiaB/NifB IPR031691, LIAS_N IPR003698, Lipoyl_synth IPR007197, rSAM |
PANTHERi | PTHR10949, PTHR10949, 1 hit |
Pfami | View protein in Pfam PF16881, LIAS_N, 1 hit PF04055, Radical_SAM, 1 hit |
PIRSFi | PIRSF005963, Lipoyl_synth, 1 hit |
SFLDi | SFLDF00271, lipoyl_synthase, 1 hit SFLDS00029, Radical_SAM, 1 hit |
SMARTi | View protein in SMART SM00729, Elp3, 1 hit |
TIGRFAMsi | TIGR00510, lipA, 1 hit |
PROSITEi | View protein in PROSITE PS51918, RADICAL_SAM, 1 hit |
i Sequence
Sequence statusi: Complete.
O32129-1 [UniParc]FASTAAdd to basket
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
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL009126 Genomic DNA Translation: CAB15223.2 |
PIRi | D70023 |
RefSeqi | NP_391113.2, NC_000964.3 WP_003222888.1, NZ_JNCM01000033.1 |
Genome annotation databases
EnsemblBacteriai | CAB15223; CAB15223; BSU32330 |
GeneIDi | 51993284 938861 |
KEGGi | bsu:BSU32330 |
PATRICi | fig|224308.179.peg.3500 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL009126 Genomic DNA Translation: CAB15223.2 |
PIRi | D70023 |
RefSeqi | NP_391113.2, NC_000964.3 WP_003222888.1, NZ_JNCM01000033.1 |
3D structure databases
SMRi | O32129 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 224308.BSU32330 |
Proteomic databases
jPOSTi | O32129 |
PaxDbi | O32129 |
PRIDEi | O32129 |
Protocols and materials databases
DNASUi | 938861 |
Genome annotation databases
EnsemblBacteriai | CAB15223; CAB15223; BSU32330 |
GeneIDi | 51993284 938861 |
KEGGi | bsu:BSU32330 |
PATRICi | fig|224308.179.peg.3500 |
Phylogenomic databases
eggNOGi | COG0320, Bacteria |
InParanoidi | O32129 |
OMAi | PYCDIDF |
PhylomeDBi | O32129 |
Enzyme and pathway databases
BioCyci | BSUB:BSU32330-MONOMER MetaCyc:BSU32330-MONOMER |
SABIO-RKi | O32129 |
Miscellaneous databases
PROi | PR:O32129 |
Family and domain databases
Gene3Di | 3.20.20.70, 1 hit |
HAMAPi | MF_00206, Lipoyl_synth, 1 hit |
InterProi | View protein in InterPro IPR013785, Aldolase_TIM IPR006638, Elp3/MiaB/NifB IPR031691, LIAS_N IPR003698, Lipoyl_synth IPR007197, rSAM |
PANTHERi | PTHR10949, PTHR10949, 1 hit |
Pfami | View protein in Pfam PF16881, LIAS_N, 1 hit PF04055, Radical_SAM, 1 hit |
PIRSFi | PIRSF005963, Lipoyl_synth, 1 hit |
SFLDi | SFLDF00271, lipoyl_synthase, 1 hit SFLDS00029, Radical_SAM, 1 hit |
SMARTi | View protein in SMART SM00729, Elp3, 1 hit |
TIGRFAMsi | TIGR00510, lipA, 1 hit |
PROSITEi | View protein in PROSITE PS51918, RADICAL_SAM, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | LIPA_BACSU | |
Accessioni | O32129Primary (citable) accession number: O32129 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | May 30, 2000 |
Last sequence update: | May 30, 2000 | |
Last modified: | December 2, 2020 | |
This is version 148 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families