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B2RKU2

- LIPA_PORG3

UniProt

B2RKU2 - LIPA_PORG3

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Protein

Lipoyl synthase

Gene

lipA

Organism
Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / JCM 12257)
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 bindingi37 – 371Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi42 – 421Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi48 – 481Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi63 – 631Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi67 – 671Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi70 – 701Iron-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

BioCyciPGIN431947:GC9J-1518-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:PGN_1468
OrganismiPorphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / JCM 12257)
Taxonomic identifieri431947 [NCBI]
Taxonomic lineageiBacteriaBacteroidetesBacteroidiaBacteroidalesPorphyromonadaceaePorphyromonas
ProteomesiUP000008842: 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 – 282282Lipoyl synthasePRO_1000099620Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi431947.PGN_1468.

Structurei

3D structure databases

ProteinModelPortaliB2RKU2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0320.
HOGENOMiHOG000235998.
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.

B2RKU2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAQHVKKPEW LKIRLGGNEK FTETKSIVEG HCLHTICTSG KCPNMGECWS
60 70 80 90 100
RGTATFMIGG DICTRACRFC NTLTGRPKPL NEAEPTHVAL SIKLMGLNHA
110 120 130 140 150
VVTSVDRDDL PDYGATHWVK TIQEIRRINS GVTLEVLIPD FKGRMDLVDM
160 170 180 190 200
IIEASPDVIS HNLETVRRLT PSVRSVATYD TSLAVLRHIA QSGKMPAKTG
210 220 230 240 250
MMLGLGETEE EILELMDDAL AAGVSVITIG QYLQPSRKNL PVVEYITPEQ
260 270 280
FEHLRLVGIE KGFRTIESAP LVRSSYHAER HL
Length:282
Mass (Da):31,299
Last modified:July 1, 2008 - v1
Checksum:i92463EECD01A8A81
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP009380 Genomic DNA. Translation: BAG33987.1.
RefSeqiYP_001929584.1. NC_010729.1.

Genome annotation databases

EnsemblBacteriaiBAG33987; BAG33987; PGN_1468.
GeneIDi6330782.
KEGGipgn:PGN_1468.
PATRICi22975909. VBIPorGin26334_1448.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP009380 Genomic DNA. Translation: BAG33987.1 .
RefSeqi YP_001929584.1. NC_010729.1.

3D structure databases

ProteinModelPortali B2RKU2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 431947.PGN_1468.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAG33987 ; BAG33987 ; PGN_1468 .
GeneIDi 6330782.
KEGGi pgn:PGN_1468.
PATRICi 22975909. VBIPorGin26334_1448.

Phylogenomic databases

eggNOGi COG0320.
HOGENOMi HOG000235998.
KOi K03644.
OMAi HPHIPTK.
OrthoDBi EOG6038ZS.

Enzyme and pathway databases

UniPathwayi UPA00538 ; UER00593 .
BioCyci PGIN431947:GC9J-1518-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. "Determination of the genome sequence of Porphyromonas gingivalis strain ATCC 33277 and genomic comparison with strain W83 revealed extensive genome rearrangements in P. gingivalis."
    Naito M., Hirakawa H., Yamashita A., Ohara N., Shoji M., Yukitake H., Nakayama K., Toh H., Yoshimura F., Kuhara S., Hattori M., Hayashi T., Nakayama K.
    DNA Res. 15:215-225(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 33277 / DSM 20709 / JCM 12257.

Entry informationi

Entry nameiLIPA_PORG3
AccessioniPrimary (citable) accession number: B2RKU2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: July 1, 2008
Last modified: November 26, 2014
This is version 47 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