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)

O31550

- ACOC_BACSU

UniProt

O31550 - ACOC_BACSU

Protein

Dihydrolipoyllysine-residue acetyltransferase component of acetoin cleaving system

Gene

acoC

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalytic activityi

    Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.

    Cofactori

    Binds 1 lipoyl cofactor covalently.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei371 – 3711Sequence Analysis
    Active sitei375 – 3751Sequence Analysis

    GO - Molecular functioni

    1. dihydrolipoyllysine-residue acetyltransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. acetoin catabolic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Acetoin catabolism

    Enzyme and pathway databases

    BioCyciBSUB:BSU08080-MONOMER.
    UniPathwayiUPA00040.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dihydrolipoyllysine-residue acetyltransferase component of acetoin cleaving system (EC:2.3.1.12)
    Alternative name(s):
    Acetoin dehydrogenase E2 component
    Dihydrolipoamide acetyltransferase component of acetoin cleaving system
    Gene namesi
    Name:acoC
    Synonyms:yfjI
    Ordered Locus Names:BSU08080
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU08080. [Micado]

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 398398Dihydrolipoyllysine-residue acetyltransferase component of acetoin cleaving systemPRO_0000162306Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei43 – 431N6-lipoyllysineBy similarity

    Proteomic databases

    PaxDbiO31550.

    Interactioni

    Protein-protein interaction databases

    IntActiO31550. 4 interactions.
    STRINGi224308.BSU08080.

    Structurei

    3D structure databases

    ProteinModelPortaliO31550.
    SMRiO31550. Positions 16-77, 118-155, 162-398.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 7676Lipoyl-bindingAdd
    BLAST

    Sequence similaritiesi

    Belongs to the 2-oxoacid dehydrogenase family.Curated
    Contains 1 lipoyl-binding domain.Curated

    Keywords - Domaini

    Lipoyl

    Phylogenomic databases

    eggNOGiCOG0508.
    HOGENOMiHOG000281566.
    KOiK00627.
    OMAiVESCIIT.
    OrthoDBiEOG610413.
    PhylomeDBiO31550.

    Family and domain databases

    Gene3Di3.30.559.10. 1 hit.
    4.10.320.10. 1 hit.
    InterProiIPR001078. 2-oxoacid_DH_actylTfrase.
    IPR000089. Biotin_lipoyl.
    IPR023213. CAT-like_dom.
    IPR004167. E3-bd.
    IPR011053. Single_hybrid_motif.
    [Graphical view]
    PfamiPF00198. 2-oxoacid_dh. 1 hit.
    PF00364. Biotin_lipoyl. 1 hit.
    PF02817. E3_binding. 1 hit.
    [Graphical view]
    SUPFAMiSSF47005. SSF47005. 1 hit.
    SSF51230. SSF51230. 1 hit.
    PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O31550-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAVKVVMPKL GMAMKQGEVS IWNKKVGDPV EKGESIASIQ SEKIEMEIEA    50
    PEKGTLIDIK VKEGEEVPPG TAICYIGDAN ESVQEEAGAP VAEDNMPQAV 100
    QPVKQENKPA ASKKDRMKIS PVARKIAEKA GLDLKQLKGT GPGGRIVKDD 150
    VTKALAEQKK DQAKPVSEQK AQEIPVTGMR KVIAARMQES LANSAQLTIT 200
    MKADITKLAT LQKQLSPTAE ERYGTKLTIT HFVSRAAVLA LQAHPVLNSF 250
    YQNERIITHP HVHLGMAVAL ENGLVVPVIR HAEKLSLIEL AQSISENAKK 300
    AREGRAGSEE LQGSTFSITN LGAFGVEHFT PILNPPETGI LGIGASYDTP 350
    VYQGEEIVRS TILPLSLTFD HRACDGAPAA AFLKAMKTYL EEPAALIL 398
    Length:398
    Mass (Da):42,886
    Last modified:January 1, 1998 - v1
    Checksum:i559564C27C1C64F6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D78509 Genomic DNA. Translation: BAA24294.1.
    AL009126 Genomic DNA. Translation: CAB12637.1.
    PIRiF69581.
    RefSeqiNP_388689.1. NC_000964.3.
    WP_003244059.1. NZ_CM000487.1.

    Genome annotation databases

    EnsemblBacteriaiCAB12637; CAB12637; BSU08080.
    GeneIDi936147.
    KEGGibsu:BSU08080.
    PATRICi18973266. VBIBacSub10457_0847.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D78509 Genomic DNA. Translation: BAA24294.1 .
    AL009126 Genomic DNA. Translation: CAB12637.1 .
    PIRi F69581.
    RefSeqi NP_388689.1. NC_000964.3.
    WP_003244059.1. NZ_CM000487.1.

    3D structure databases

    ProteinModelPortali O31550.
    SMRi O31550. Positions 16-77, 118-155, 162-398.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi O31550. 4 interactions.
    STRINGi 224308.BSU08080.

    Proteomic databases

    PaxDbi O31550.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB12637 ; CAB12637 ; BSU08080 .
    GeneIDi 936147.
    KEGGi bsu:BSU08080.
    PATRICi 18973266. VBIBacSub10457_0847.

    Organism-specific databases

    GenoListi BSU08080. [Micado ]

    Phylogenomic databases

    eggNOGi COG0508.
    HOGENOMi HOG000281566.
    KOi K00627.
    OMAi VESCIIT.
    OrthoDBi EOG610413.
    PhylomeDBi O31550.

    Enzyme and pathway databases

    UniPathwayi UPA00040 .
    BioCyci BSUB:BSU08080-MONOMER.

    Family and domain databases

    Gene3Di 3.30.559.10. 1 hit.
    4.10.320.10. 1 hit.
    InterProi IPR001078. 2-oxoacid_DH_actylTfrase.
    IPR000089. Biotin_lipoyl.
    IPR023213. CAT-like_dom.
    IPR004167. E3-bd.
    IPR011053. Single_hybrid_motif.
    [Graphical view ]
    Pfami PF00198. 2-oxoacid_dh. 1 hit.
    PF00364. Biotin_lipoyl. 1 hit.
    PF02817. E3_binding. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47005. SSF47005. 1 hit.
    SSF51230. SSF51230. 1 hit.
    PROSITEi PS50968. BIOTINYL_LIPOYL. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and sequencing of a 40.6 kb segment in the 73 degrees-76 degrees region of the Bacillus subtilis chromosome containing genes for trehalose metabolism and acetoin utilization."
      Yamamoto H., Uchiyama S., Sekiguchi J.
      Microbiology 142:3057-3065(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168 / AC327.
    2. "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(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.

    Entry informationi

    Entry nameiACOC_BACSU
    AccessioniPrimary (citable) accession number: O31550
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 110 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. 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