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⊟Summary[edit | edit source]

  • pan ID?: SAUPAN004082000
  • symbol?: accB
  • synonym:
  • description?: acetyl-CoA carboxylase biotin carboxyl carrier protein subunit

      descriptions from strain specific annotations:

    • acetyl-CoA carboxylase biotin carboxyl carrier protein subunit
    • acetyl-CoA carboxylase, biotin carboxyl carrier protein
    • acetyl-CoA carboxylase biotin carboxyl carrier protein
    • acetyl-CoA carboxylase biotin carboxyl carrier subunit
    • biotin carboxyl carrier protein of acetyl-CoAcarboxylase
  • strand?: -
  • coordinates?: 4363226..4363690
  • synteny block?: BlockID0031140
  • occurrence?: in 100% of 34 strains

accB : acetyl-CoA carboxylase biotin carboxyl carrier protein subunit [1]

Converting acetyl-CoA to malonyl-CoA is the first committed step in fatty acid biosynthesis. The mechanism of acetyl-CoA carboxylase (ACC) is conceptually analogous to pyruvate carboxylase except that (1) the functional domains are found distributed among discrete proteins and (2) the substrate, rather than a free metabolite, is a tethered Coenzyme A thioester. A biotin carboxyl carrier protein (AccB) is post-translationally biotinylated by BirA, a biotin carboxylase (AccC) modifies the AccB-bound biotin to carboxybiotin and a carboxyltransferase (AccAD) both activates the acetyl-CoA α carbon and releases CO2 locally from AccB-bound carboxybiotin, favoring production of malonyl-CoA.

⊟Orthologs[edit | edit source]

    COL:
    SACOL1572 (accB)
    N315:
    SA1358 (accB)
    NCTC8325:
    SAOUHSC_01624
    Newman:
    NWMN_1432 (accB)
    USA300_FPR3757:
    SAUSA300_1476 (accB)
    04-02981:
    SA2981_1486 (accB)
    08BA02176:
    C248_1570 (accB)
    11819-97:
    MS7_1545 (accB)
    6850:
    RSAU_001394 (accB1)
    71193:
    ST398NM01_1593
    ECT-R 2:
    ECTR2_1379 (accB)
    ED133:
    SAOV_1528 (accB)
    ED98:
    SAAV_1520 (accB)
    HO 5096 0412:
    SAEMRSA15_14480 (accB)
    JH1:
    SaurJH1_1619
    JH9:
    SaurJH9_1586
    JKD6008:
    SAA6008_01497 (accB)
    JKD6159:
    SAA6159_01463 (accB)
    JSNZ:
    JSNZ_001518 (accB)
    LGA251:
    SARLGA251_14340 (accB)
    M013:
    M013TW_1543
    MRSA252:
    SAR1605 (accB)
    MSHR1132:
    SAMSHR1132_13680
    MSSA476:
    SAS1466
    Mu3:
    SAHV_1515 (accB)
    Mu50:
    SAV1527 (accB)
    MW2:
    MW1480 (accB)
    RF122:
    SAB1400c (accB)
    ST398:
    SAPIG1593 (accB)
    T0131:
    SAT0131_01621
    TCH60:
    HMPREF0772_11613 (accB2)
    TW20:
    SATW20_15240 (accB)
    USA300_TCH1516:
    USA300HOU_1529 (accB)
    VC40:
    SAVC_06885

⊟Genome Viewer[edit | edit source]

COL
N315
NCTC8325
Newman
USA300_FPR3757

⊟Alignments[edit | edit source]

  • alignment of orthologues:
    CLUSTAL format alignment by MAFFT L-INS-i (v7.307)


    COL             MNFKEIKELIEILDKSTLTEINIEDTKGKVTLKKEKETEIITPQISQMPVEAAAMPMPQA
    N315            MNFKEIKELIEILDKSTLTEINIEDTKGKVTLKKEKETEIITPQISQMPVEAAAMPMPQA
    NCTC8325        MNFKEIKELIEILDKSTLTEINIEDTKGKVTLKKEKETEIITPQISQMPVEAAAMPMPQA
    Newman          MNFKEIKELIEILDKSTLTEINIEDTKGKVTLKKEKETEIITPQISQMPVEAAAMPMPQA
    USA300_FPR3757  MNFKEIKELIEILDKSTLTEINIEDTKGKVTLKKEKETEIITPQISQMPVEAAAMPMPQA
                    ************************************************************

    COL             QSTDSNKTEAPKPTSDNHKTINAPMVGTFYKSPSPDEEAYVQVGDTVSNETTVCILEAMK
    N315            QSTDSNKTEAPKPTSDNHKTINAPMVGTFYKSPSPDEEAYVQVGDTVSNETTVCILEAMK
    NCTC8325        QSTDSNKTEAPKPTSDNHKTINAPMVGTFYKSPSPDEEAYVQVGDTVSNETTVCILEAMK
    Newman          QSTDSNKTEAPKPTSDNHKTINAPMVGTFYKSPSPDEEAYVQVGDTVSNETTVCILEAMK
    USA300_FPR3757  QSTDSNKTEAPKPTSDNHKTINAPMVGTFYKSPSPDEEAYVQVGDTVSNETTVCILEAMK
                    ************************************************************

    COL             LFNEIQAEISGEIVEILVEDGQMVEYGQPLFKVK
    N315            LFNEIQAEISGEIVEILVEDGQMVEYGQPLFKVK
    NCTC8325        LFNEIQAEISGEIVEILVEDGQMVEYGQPLFKVK
    Newman          LFNEIQAEISGEIVEILVEDGQMVEYGQPLFKVK
    USA300_FPR3757  LFNEIQAEISGEIVEILVEDGQMVEYGQPLFKVK
                    **********************************

  1. ↑ Christoph Freiberg, Nina A Brunner, Guido Schiffer, Thomas Lampe, Jens Pohlmann, Michael Brands, Martin Raabe, Dieter Häbich, Karl Ziegelbauer
    Identification and characterization of the first class of potent bacterial acetyl-CoA carboxylase inhibitors with antibacterial activity.
    J Biol Chem: 2004, 279(25);26066-73
    [PubMed:15066985] [WorldCat.org] [DOI] (P p)    Patrick Bilder, Sandra Lightle, Graeme Bainbridge, Jeffrey Ohren, Barry Finzel, Fang Sun, Susan Holley, Loola Al-Kassim, Cindy Spessard, Michael Melnick, Marcia Newcomer, Grover L Waldrop
    The structure of the carboxyltransferase component of acetyl-coA carboxylase reveals a zinc-binding motif unique to the bacterial enzyme.
    Biochemistry: 2006, 45(6);1712-22
    [PubMed:16460018] [WorldCat.org] [DOI] (P p)    Igor Mochalkin, J Richard Miller, Artem Evdokimov, Sandra Lightle, Chunhong Yan, Charles Ken Stover, Grover L Waldrop
    Structural evidence for substrate-induced synergism and half-sites reactivity in biotin carboxylase.
    Protein Sci: 2008, 17(10);1706-18
    [PubMed:18725455] [WorldCat.org] [DOI] (I p)
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