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⊟Summary[edit | edit source]
- pan ID?: SAUPAN004081000
- symbol?: accC
- synonym:
- description?: acetyl-CoA carboxylase biotin carboxylase subunit
- acetyl-CoA carboxylase biotin carboxylase subunit
- acetyl-CoA biotin carboxylase
- acetyl-CoA carboxylase accC (biotin carboxylase subunit)
- acetyl-CoA carboxylase, biotin carboxylase
- acetyl-CoA carboxylase, biotin carboxylase subunit
- Biotin carboxylase of acetyl-CoA carboxylase
- biotin carboxylase subunit of acetyl-CoAcarboxylase
descriptions from strain specific annotations:
- strand?: -
- coordinates?: 4361868..4363226
- synteny block?: BlockID0031130
- occurrence?: in 100% of 34 strains
accC : acetyl-CoA carboxylase biotin carboxylase subunit [1]
• A crystal structure is available : 2VPQ
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]
04-02981:
SA2981_1485 (accC)
08BA02176:
C248_1569 (accC)
11819-97:
MS7_1544 (accC)
6850:
RSAU_001393 (accC1)
71193:
ST398NM01_1592
ECT-R 2:
ECTR2_1378 (accC)
ED133:
SAOV_1527
ED98:
SAAV_1519 (accC)
HO 5096 0412:
SAEMRSA15_14470 (accC)
JH1:
SaurJH1_1618
JH9:
SaurJH9_1585
JKD6008:
SAA6008_01496 (accC)
JKD6159:
SAA6159_01462 (accC)
JSNZ:
JSNZ_001517 (accC)
LGA251:
SARLGA251_14330 (accC)
M013:
M013TW_1542
MRSA252:
SAR1604 (accC)
MSHR1132:
SAMSHR1132_13670
MSSA476:
SAS1465
Mu3:
SAHV_1514 (accC)
Mu50:
SAV1526 (accC)
MW2:
MW1479 (accC)
RF122:
SAB1399c (accC)
ST398:
SAPIG1592 (accC)
T0131:
SAT0131_01620
TCH60:
HMPREF0772_11614 (accC2)
TW20:
SATW20_15230 (accC)
USA300_TCH1516:
USA300HOU_1528 (accC)
VC40:
SAVC_06880
⊟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 MKKVLIANRGEIAVRIIRACRDLGIQTVAIYSEGDKDALHTQIADEAYCVGPTLSKDSYL
N315 MKKVLIANRGEIAVRIIRACRDLGIQTVAIYSEGDKDALHTQIADEAYCVGPTLSKDSYL
NCTC8325 MKKVLIANRGEIAVRIIRACRDLGIQTVAIYSEGDKDALHTQIADEAYCVGPTLSKDSYL
Newman MKKVLIANRGEIAVRIIRACRDLGIQTVAIYSEGDKDALHTQIADEAYCVGPTLSKDSYL
USA300_FPR3757 MKKVLIANRGEIAVRIIRACRDLGIQTVAIYSEGDKDALHTQIADEAYCVGPTLSKDSYL
************************************************************
COL NIPNILSIATSTGCDGVHPGYGFLAENADFAELCEACQLKFIGPSYQSIQKMGIKDVAKA
N315 NIPNILSIATSTGCDGVHPGYGFLAENADFAELCEACQLKFIGPSYQSIQKMGIKDVAKA
NCTC8325 NIPNILSIATSTGCDGVHPGYGFLAENADFAELCEACQLKFIGPSYQSIQKMGIKDVAKA
Newman NIPNILSIATSTGCDGVHPGYGFLAENADFAELCEACQLKFIGPSYQSIQKMGIKDVAKA
USA300_FPR3757 NIPNILSIATSTGCDGVHPGYGFLAENADFAELCEACQLKFIGPSYQSIQKMGIKDVAKA
************************************************************
COL EMIKANVPVVPGSDGLMKDVSEAKKIAKKIGYPVIIKATAGGGGKGIRVARDEKELETGF
N315 EMIKANVPVVPGSDGLMKDVSEAKKIAKKIGYPVIIKATAGGGGKGIRVARDEKELETGF
NCTC8325 EMIKANVPVVPGSDGLMKDVSEAKKIAKKIGYPVIIKATAGGGGKGIRVARDEKELETGF
Newman EMIKANVPVVPGSDGLMKDVSEAKKIAKKIGYPVIIKATAGGGGKGIRVARDEKELETGF
USA300_FPR3757 EMIKANVPVVPGSDGLMKDVSEAKKIAKKIGYPVIIKATAGGGGKGIRVARDEKELETGF
************************************************************
COL RMTEQEAQTAFGNGGLYMEKFIENFRHIEIQIVGDSYGNVIHLGERDCTIQRRMQKLVEE
N315 RMTEQEAQTAFGNGGLYMEKFIENFRHIEIQIVGDSYGNVIHLGERDCTIQRRMQKLVEE
NCTC8325 RMTEQEAQTAFGNGGLYMEKFIENFRHIEIQIVGDSYGNVIHLGERDCTIQRRMQKLVEE
Newman RMTEQEAQTAFGNGGLYMEKFIENFRHIEIQIVGDSYGNVIHLGERDCTIQRRMQKLVEE
USA300_FPR3757 RMTEQEAQTAFGNGGLYMEKFIENFRHIEIQIVGDSYGNVIHLGERDCTIQRRMQKLVEE
************************************************************
COL APSPILDDETRREMGNAAVRAAKAVNYENAGTIEFIYDLNDNKFYFMEMNTRIQVEHPVT
N315 APSPILDDETRREMGNAAVRAAKAVNYENAGTIEFIYDLNDNKFYFMEMNTRIQVEHPVT
NCTC8325 APSPILDDETRREMGNAAVRAAKAVNYENAGTIEFIYDLNDNKFYFMEMNTRIQVEHPVT
Newman APSPILDDETRREMGNAAVRAAKAVNYENAGTIEFIYDLNDNKFYFMEMNTRIQVEHPVT
USA300_FPR3757 APSPILDDETRREMGNAAVRAAKAVNYENAGTIEFIYDLNDNKFYFMEMNTRIQVEHPVT
************************************************************
COL EMVTGIDLVKLQLQVAMGDVLPYKQEDIKLTGHAIEFRINAENPYKNFMPSPGKIEQYLA
N315 EMVTGIDLVKLQLQVAMGDVLPYKQEDIKLTGHAIEFRINAENPYKNFMPSPGKIEQYLA
NCTC8325 EMVTGIDLVKLQLQVAMGDVLPYKQEDIKLTGHAIEFRINAENPYKNFMPSPGKIEQYLA
Newman EMVTGIDLVKLQLQVAMGDVLPYKQEDIKLTGHAIEFRINAENPYKNFMPSPGKIEQYLA
USA300_FPR3757 EMVTGIDLVKLQLQVAMGDVLPYKQEDIKLTGHAIEFRINAENPYKNFMPSPGKIEQYLA
************************************************************
COL PGGYGVRIESACYTNYTIPPYYDSMVAKLIIHEPTRDEAIMAGIRALSEFVVLGIDTTIP
N315 PGGYGVRIESACYTNYTIPPYYDSMVAKLIIHEPTRDEAIMAGIRALSEFVVLGIDTTIP
NCTC8325 PGGYGVRIESACYTNYTIPPYYDSMVAKLIIHEPTRDEAIMAGIRALSEFVVLGIDTTIP
Newman PGGYGVRIESACYTNYTIPPYYDSMVAKLIIHEPTRDEAIMAGIRALSEFVVLGIDTTIP
USA300_FPR3757 PGGYGVRIESACYTNYTIPPYYDSMVAKLIIHEPTRDEAIMAGIRALSEFVVLGIDTTIP
************************************************************
COL FHIKLLNNDIFRSGKFNTNFLEQNSIMNDEG
N315 FHIKLLNNDIFRSGKFNTNFLEQNSIMNDEG
NCTC8325 FHIKLLNNDIFRSGKFNTNFLEQNSIMNDEG
Newman FHIKLLNNDIFRSGKFNTNFLEQNSIMNDEG
USA300_FPR3757 FHIKLLNNDIFRSGKFNTNFLEQNSIMNDEG
*******************************
- ↑ 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)