Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(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)

A5UFJ8

- LIPA_HAEIG

UniProt

A5UFJ8 - LIPA_HAEIG

Protein

Lipoyl synthase

Gene

lipA

Organism
Haemophilus influenzae (strain PittGG)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 52 (01 Oct 2014)
      Sequence version 1 (10 Jul 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 bindingi67 – 671Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi72 – 721Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi78 – 781Iron-sulfur 1 (4Fe-4S)UniRule annotation
    Metal bindingi93 – 931Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi97 – 971Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
    Metal bindingi100 – 1001Iron-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

    Keywords - Molecular functioni

    Transferase

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BioCyciHINF374931:GJA4-440-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:CGSHiGG_02615
    OrganismiHaemophilus influenzae (strain PittGG)
    Taxonomic identifieri374931 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus
    ProteomesiUP000001990: Chromosome

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 320320Lipoyl synthasePRO_1000012229Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi374931.CGSHiGG_02615.

    Structurei

    3D structure databases

    ProteinModelPortaliA5UFJ8.
    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.

    A5UFJ8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSTPFKMERG VKYRDAAKTS IIPVKNIDPN QELLKKPEWM KIKLPASSAK    50
    IESIKNGMRR HGLHSVCEEA SCPNLHECFN HGTATFMILG AICTRRCPFC 100
    DVAHGKPLPP DPEEPQKLAE TIQDMKLKYV VITSVDRDDL PDRGAGHFSE 150
    CVKAVRELNP NIKIEILVPD FRGRVTQALE KLKDNPPDVF NHNLENVPRL 200
    YKEIRPGADY EWSLKLLREF KEMFPNIPTK SGLMVGLGET NEEILQVMQD 250
    LRDNGVTMLT LGQYLQPSRH HLPVARYVPP TEFDIFRDKA NEMGFEHAAC 300
    GPFVRSSYHA DLQASGGLVK 320
    Length:320
    Mass (Da):36,199
    Last modified:July 10, 2007 - v1
    Checksum:i98C0B70ED6AB89DF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000672 Genomic DNA. Translation: ABQ99553.1.
    RefSeqiWP_012054772.1. NC_009567.1.
    YP_001291937.1. NC_009567.1.

    Genome annotation databases

    EnsemblBacteriaiABQ99553; ABQ99553; CGSHiGG_02615.
    GeneIDi5227031.
    KEGGihiq:CGSHiGG_02615.
    PATRICi20185215. VBIHaeInf102487_0527.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000672 Genomic DNA. Translation: ABQ99553.1 .
    RefSeqi WP_012054772.1. NC_009567.1.
    YP_001291937.1. NC_009567.1.

    3D structure databases

    ProteinModelPortali A5UFJ8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 374931.CGSHiGG_02615.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABQ99553 ; ABQ99553 ; CGSHiGG_02615 .
    GeneIDi 5227031.
    KEGGi hiq:CGSHiGG_02615.
    PATRICi 20185215. VBIHaeInf102487_0527.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00538 ; UER00593 .
    BioCyci HINF374931:GJA4-440-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. "Characterization and modeling of the Haemophilus influenzae core and supragenomes based on the complete genomic sequences of Rd and 12 clinical nontypeable strains."
      Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C., Ehrlich G.D.
      Genome Biol. 8:R103.1-R103.18(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: PittGG.

    Entry informationi

    Entry nameiLIPA_HAEIG
    AccessioniPrimary (citable) accession number: A5UFJ8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: July 10, 2007
    Last modified: October 1, 2014
    This is version 52 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