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⊟Summary[edit | edit source]
- pan ID?: SAUPAN004348000
- symbol?: accD
- synonym:
- description?: acetyl-CoA carboxylase carboxyl transferase subunit beta
- acetyl-CoA carboxylase carboxyl transferase subunit beta
- acetyl-CoA carboxylase subunit beta
- acetyl-CoA carboxylase, carboxyl transferase, beta subunit
- acetyl-CoA carboxylase, carboxyltransferase subunit beta
- acetyl-coenzyme A carboxylase carboxyltransferase subunit beta
- Acetyl-coenzyme A carboxyl transferase beta chain
descriptions from strain specific annotations:
- strand?: -
- coordinates?: 4587939..4588796
- synteny block?: BlockID0033530
- occurrence?: in 100% of 34 strains
accD : acetyl-CoA carboxylase carboxyltransferase subunit beta [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_1659 (accB)
08BA02176:
C248_1742 (accD)
11819-97:
MS7_1707 (accD)
6850:
RSAU_001558 (accD)
71193:
ST398NM01_1754
ECT-R 2:
ECTR2_1540 (accD)
ED133:
SAOV_1688 (accD)
ED98:
SAAV_1710 (accD)
HO 5096 0412:
SAEMRSA15_16100 (accD)
JH1:
SaurJH1_1791
JH9:
SaurJH9_1757
JKD6008:
SAA6008_01669 (accD)
JKD6159:
SAA6159_01624 (accD)
JSNZ:
JSNZ_001685 (accD)
LGA251:
SARLGA251_15920 (accD)
M013:
M013TW_1713
MRSA252:
SAR1779 (accD)
MSHR1132:
SAMSHR1132_15510
MSSA476:
SAS1628
Mu3:
SAHV_1687
Mu50:
SAV1701
MW2:
MW1644
RF122:
SAB1559c (accD)
ST398:
SAPIG1754 (accD)
T0131:
SAT0131_01804
TCH60:
HMPREF0772_11451 (accD)
TW20:
SATW20_16920 (accD)
USA300_TCH1516:
USA300HOU_1687 (accD)
VC40:
SAVC_07715
⊟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 MFKDFFNRTKKKKYLTVQDSKNNDVPAGIMTKCPKCKKIMYTKELAENLNVCFNCDHHIA
N315 MFKDFFNRTKKKKYLTVQDSKNNDVPAGIMTKCPKCKKIMYTKELAENLNVCFNCDHHIA
NCTC8325 MFKDFFNRTKKKKYLTVQDSKNNDVPAGIMTKCPKCKKIMYTKELAENLNVCFNCDHHIA
Newman MFKDFFNRTKKKKYLTVQDSKNKDVPAGIMTKCPKCKKIMYTKELAENLNVCFNCDHHIA
USA300_FPR3757 MFKDFFNRTKKKKYLTVQDSKNNDVPAGIMTKCPKCKKIMYTKELAENLNVCFNCDHHIA
**********************:*************************************
COL LTAYKRIEAISDEGSFTEFDKGMTSANPLDFPSYLEKIEKDQQKTGLKEAVVTGTAQLDG
N315 LTAYKRIEAISDEGSFTEFDKGMTSANPLDFPSYLEKIEKDQQKTGLKEAVVTGTAQLDG
NCTC8325 LTAYKRIEAISDEGSFTEFDKGMTSANPLDFPSYLEKIEKDQQKTGLKEAVVTGTAQLDG
Newman LTAYKRIEAISDEGSFTEFDKGMTSANPLDFPSYLEKIEKDQQKTGLKEAVVTGTAQLDG
USA300_FPR3757 LTAYKRIEAISDEGSFTEFDKGMTSANPLDFPSYLEKIEKDQQKTGLKEAVVTGTAQLDG
************************************************************
COL MKFGVAVMDSRFRMGSMGSVIGEKICRIIDYCTENRLPFILFSASGGARMQEGIISLMQM
N315 MKFGVAVMDSRFRMGSMGSVIGEKICRIIDYCTENRLPFILFSASGGARMQEGIISLMQM
NCTC8325 MKFGVAVMDSRFRMGSMGSVIGEKICRIIDYCTENRLPFILFSASGGARMQEGIISLMQM
Newman MKFGVAVMDSRFRMGSMGSVIGEKICRIIDYCTENRLPFILFSASGGARMQEGIISLMQM
USA300_FPR3757 MKFGVAVMDSRFRMGSMGSVIGEKICRIIDYCTENRLPFILFSASGGARMQEGIISLMQM
************************************************************
COL GKTSVSLKRHSDAGLLYISYLTHPTTGGVSASFASVGDINLSEPKALIGFAGRRVIEQTI
N315 GKTSVSLKRHSDAGLLYISYLTHPTTGGVSASFASVGDINLSEPKALIGFAGRRVIEQTI
NCTC8325 GKTSVSLKRHSDAGLLYISYLTHPTTGGVSASFASVGDINLSEPKALIGFAGRRVIEQTI
Newman GKTSVSLKRHSDAGLLYISYLTHPTTGGVSASFASVGDINLSEPKALIGFAGRRVIEQTI
USA300_FPR3757 GKTSVSLKRHSDAGLLYISYLTHPTTGGVSASFASVGDINLSEPKALIGFAGRRVIEQTI
************************************************************
COL NEKLPDDFQTAEFLLEHGQLDKVVHRNDMRQTLSEILKIHQEVTK
N315 NEKLPDDFQTAEFLLEHGQLDKVVHRNDMRQTLSEILKIHQEVTK
NCTC8325 NEKLPDDFQTAEFLLEHGQLDKVVHRNDMRQTLSEILKIHQEVTK
Newman NEKLPDDFQTAEFLLEHGQLDKVVHRNDMRQTLSEILKIHQEVTK
USA300_FPR3757 NEKLPDDFQTAEFLLEHGQLDKVVHRNDMRQTLSEILKIHQEVTK
*********************************************
- ↑ 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)