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⊟Summary[edit | edit source]
- pan ID?: SAUPAN004347000
- symbol?: accA
- synonym:
- description?: acetyl-CoA carboxylase carboxyltransferase subunit alpha
- acetyl-CoA carboxylase carboxyltransferase subunit alpha
- acetyl-CoA carboxylase, carboxyl transferase, alpha subunit
- acetyl-coenzyme A carboxylase carboxyltransferase subunit alpha
- Acetyl-coenzyme A carboxyl transferase alpha chain
- acetyl-CoA carboxylase, carboxyl transferase subunit alpha
descriptions from strain specific annotations:
- strand?: -
- coordinates?: 4586995..4587939
- synteny block?: BlockID0033520
- occurrence?: in 100% of 34 strains
accA : acetyl-CoA carboxylase carboxyltransferase subunit alpha [1]
• A crystal structure is available : 2F9I
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_1658 (accA)
08BA02176:
C248_1741 (accA)
11819-97:
MS7_1706 (accA)
6850:
RSAU_001557 (accA)
71193:
ST398NM01_1753
ECT-R 2:
ECTR2_1539 (accA)
ED133:
SAOV_1687 (accA)
ED98:
SAAV_1709 (accA)
HO 5096 0412:
SAEMRSA15_16090 (accA)
JH1:
SaurJH1_1790
JH9:
SaurJH9_1756
JKD6008:
SAA6008_01668 (accA)
JKD6159:
SAA6159_01623 (accA)
JSNZ:
JSNZ_001684
LGA251:
SARLGA251_15910 (accA)
M013:
M013TW_1712
MRSA252:
SAR1778 (accA)
MSHR1132:
SAMSHR1132_15500
MSSA476:
SAS1627
Mu3:
SAHV_1686 (accA)
Mu50:
SAV1700 (accA)
MW2:
MW1643 (accA)
RF122:
SAB1558c (accA)
ST398:
SAPIG1753 (accA)
T0131:
SAT0131_01803
TCH60:
HMPREF0772_11452 (accA)
TW20:
SATW20_16910 (accA)
USA300_TCH1516:
USA300HOU_1686 (accA)
VC40:
SAVC_07710
⊟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 MLDFEKPLFEIRNKIESLKESQDKNDVDLQEEIDMLEASLERETKKIYTNLKPWDRVQIA
N315 MLDFEKPLFEIRNKIESLKESQDKNDVDLQEEIDMLEASLERETKKIYTNLKPWDRVQIA
NCTC8325 MLDFEKPLFEIRNKIESLKESQDKNDVDLQEEIDMLEASLERETKKIYTNLKPWDRVQIA
Newman MLDFEKPLFEIRNKIESLKESQDKNDVDLQEEIDMLEASLERETKKIYTNLKPWDRVQIA
USA300_FPR3757 MLDFEKPLFEIRNKIESLKESQDKNDVDLQEEIDMLEASLERETKKIYTNLKPWDRVQIA
************************************************************
COL RLQERPTTLDYIPYIFDSFMELHGDRNFRDDPAMIGGIGFLNGRAVTVIGQQRGKDTKDN
N315 RLQERPTTLDYIPYIFDSFMELHGDRNFRDDPAMIGGIGFLNGRAVTVIGQQRGKDTKDN
NCTC8325 RLQERPTTLDYIPYIFDSFMELHGDRNFRDDPAMIGGIGFLNGRAVTVIGQQRGKDTKDN
Newman RLQERPTTLDYIPYIFDSFMELHGDRNFRDDPAMIGGIGFLNGRAVTVIGQQRGKDTKDN
USA300_FPR3757 RLQERPTTLDYIPYIFDSFMELHGDRNFRDDPAMIGGIGFLNGRAVTVIGQQRGKDTKDN
************************************************************
COL IYRNFGMAHPEGYRKALRLMKQAEKFNRPIFTFIDTKGAYPGKAAEERGQSESIATNLIE
N315 IYRNFGMAHPEGYRKALRLMKQAEKFNRPIFTFIDTKGAYPGKAAEERGQSESIATNLIE
NCTC8325 IYRNFGMAHPEGYRKALRLMKQAEKFNRPIFTFIDTKGAYPGKAAEERGQSESIATNLIE
Newman IYRNFGMAHPEGYRKALRLMKQAEKFNRPIFTFIDTKGAYPGKAAEERGQSESIATNLIE
USA300_FPR3757 IYRNFGMAHPEGYRKALRLMKQAEKFNRPIFTFIDTKGAYPGKAAEERGQSESIATNLIE
************************************************************
COL MASLKVPVIAIVIGEGGSGGALGIGIANKVLMLENSTYSVISPEGAAALLWKDSNLAKIA
N315 MASLKVPVIAIVIGEGGSGGALGIGIANKVLMLENSTYSVISPEGAAALLWKDSNLAKIA
NCTC8325 MASLKVPVIAIVIGEGGSGGALGIGIANKVLMLENSTYSVISPEGAAALLWKDSNLAKIA
Newman MASLKVPVIAIVIGEGGSGGALGIGIANKVLMLENSTYSVISPEGAAALLWKDSNLAKIA
USA300_FPR3757 MASLKVPVIAIVIGEGGSGGALGIGIANKVLMLENSTYSVISPEGAAALLWKDSNLAKIA
************************************************************
COL AETMKITAHDIKQLGIIDDVISEPLGGAHKDIEQQALAIKSAFVAQLDSLESLSRDEIAN
N315 AETMKITAHDIKQLGIIDDVISEPLGGAHKDVEQQALAIKSAFVAQLDSLESLSRDEIAN
NCTC8325 AETMKITAHDIKQLGIIDDVISEPLGGAHKDIEQQALAIKSAFVAQLDSLESLSRDEIAN
Newman AETMKITAHDIKQLGIIDDVISEPLGGAHKDIEQQALAIKSAFVAQLDSLESLSRDEIAN
USA300_FPR3757 AETMKITAHDIKQLGIIDDVISEPLGGAHKDIEQQALAIKSAFVAQLDSLESLSRDEIAN
*******************************:****************************
COL DRFEKFRNIGSYIE
N315 DRFEKFRNIGSYIE
NCTC8325 DRFEKFRNIGSYIE
Newman DRFEKFRNIGSYIE
USA300_FPR3757 DRFEKFRNIGSYIE
**************
- ↑ 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)