Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

A0M4W4

- LIPA_GRAFK

UniProt

A0M4W4 - LIPA_GRAFK

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Lipoyl synthase

Gene

lipA

Organism
Gramella forsetii (strain KT0803)
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

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 bindingi47 – 471Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi52 – 521Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi58 – 581Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi73 – 731Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi77 – 771Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi80 – 801Iron-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

BioCyciGFOR411154:GI79-2703-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:GFO_2703
OrganismiGramella forsetii (strain KT0803)
Taxonomic identifieri411154 [NCBI]
Taxonomic lineageiBacteriaBacteroidetesFlavobacteriiaFlavobacterialesFlavobacteriaceaeGramella
ProteomesiUP000000755: 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 – 293293Lipoyl synthasePRO_0000325259Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi411154.GFO_2703.

Structurei

3D structure databases

ProteinModelPortaliA0M4W4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0320.
HOGENOMiHOG000235998.
KOiK03644.
OMAiHTICQEA.
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.

A0M4W4 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNTDVAPVKS KTERKPKPKW LRVKLPTGKK YTELRNLVDK YDLHTICTSG
60 70 80 90 100
SCPNMGECWS EGTATFMILG NVCTRSCGFC GVKTGRPETV DWDEPEKVAR
110 120 130 140 150
SIKLMQIKHA VVTSVDRDDL KDMGSIVWAE TVKAIRRMNP ETTLETLIPD
160 170 180 190 200
FQGNERNIDR IIEVAPEVVS HNMETVKRLT REVRIQAKYD RSLAVLKYLK
210 220 230 240 250
DNGIRRTKSG IMLGLGEQEE EVIQTLKDLR EAGVDVVTIG QYLQPSKKHL
260 270 280 290
PVKQFITPDQ FQKYEKIGLE LGFRHVESSA LVRSSYKAQK HLN
Length:293
Mass (Da):33,330
Last modified:December 12, 2006 - v1
Checksum:i22B5D2EE61FE9AF9
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CU207366 Genomic DNA. Translation: CAL67659.1.
RefSeqiYP_862726.1. NC_008571.1.

Genome annotation databases

EnsemblBacteriaiCAL67659; CAL67659; GFO_2703.
GeneIDi4650921.
KEGGigfo:GFO_2703.
PATRICi22074160. VBIGraFor5527_2608.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CU207366 Genomic DNA. Translation: CAL67659.1 .
RefSeqi YP_862726.1. NC_008571.1.

3D structure databases

ProteinModelPortali A0M4W4.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 411154.GFO_2703.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAL67659 ; CAL67659 ; GFO_2703 .
GeneIDi 4650921.
KEGGi gfo:GFO_2703.
PATRICi 22074160. VBIGraFor5527_2608.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00538 ; UER00593 .
BioCyci GFOR411154:GI79-2703-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. "Whole genome analysis of the marine Bacteroidetes'Gramella forsetii' reveals adaptations to degradation of polymeric organic matter."
    Bauer M., Kube M., Teeling H., Richter M., Lombardot T., Allers E., Wuerdemann C.A., Quast C., Kuhl H., Knaust F., Woebken D., Bischof K., Mussmann M., Choudhuri J.V., Meyer F., Reinhardt R., Amann R.I., Gloeckner F.O.
    Environ. Microbiol. 8:2201-2213(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: KT0803.

Entry informationi

Entry nameiLIPA_GRAFK
AccessioniPrimary (citable) accession number: A0M4W4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: December 12, 2006
Last modified: October 29, 2014
This is version 58 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