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⊟Summary[edit | edit source]
- pan ID?: SAUPAN004072000
- symbol?: bfmBAA
- synonym: bkdAA
- description?: 2-oxoisovalerate dehydrogenase subunit alpha
- 2-oxoisovalerate dehydrogenase subunit alpha
- 2-oxoisovalerate dehydrogenase, E1 component, alpha subunit
- 2-oxoisovalerate dehydrogenase, E1 component subunit alpha
- branched-chain alpha-keto acid dehydrogenase E1
- thiamine pyrophosphate-dependent dehydrogenase E1 component subunit alpha
- Branched-chain alpha-keto acid dehydrogenase, E1 component, alpha subunit
- 2-oxoisovalerate dehydrogenase alpha subunit
- 2-oxoisovalerate dehydrogenase E1 subunit alpha
- 2-oxoisovalerate dehydrogenase subunit alpha (branched-chain alpha-keto acid dehydrogenase e1 component alpha chain) (bckdhe1-alpha)
- 3-methyl-2-oxobutanoate dehydrogenase
- pyruvate dehydrogenase (acetyl-transferring) alpha subunit
descriptions from strain specific annotations:
- strand?: -
- coordinates?: 4353434..4354433
- synteny block?: BlockID0031040
- occurrence?: in 100% of 33 strains
bkdA1 (bfmBAA, bkdAA) : branched-chain alpha-keto acid dehydrogenase E1 (decarboxylase-acyltransferase alpha) subunit [1]
To maintain or modulate their membrane fluidity, staphylococci catabolize deaminated branched-chain amino acids and use the Branched-Chain Alpha-Keto Acid Dehydrogenase (BCAKAD) complex to immobilize them as branched-chain Coenzyme A thioesters for subsequent modification into branched-chain fatty acids. The E1 heterodimer decarboxylates and thioesterifies BCAKAs to the lipoylated-E2 subunit, then the E2 subunit (transacylase) converts the BCAKA-dihydrolipoyl thioester to a BCAKA-CoA thioester and releases the product. Finally, the E3 subunit reduces the dehydrolipoylated-E2 subunit regenerating a functional lipoylated-E2.
⊟Orthologs[edit | edit source]
04-02981:
SA2981_1476 (bfmBAA)
08BA02176:
C248_1560 (bfmBAA)
11819-97:
MS7_1535 (bfmBAA)
6850:
RSAU_001384
71193:
ST398NM01_1583
ECT-R 2:
ECTR2_1369
ED133:
SAOV_1518
ED98:
SAAV_1510
HO 5096 0412:
SAEMRSA15_14380 (bfmBAA)
JH1:
SaurJH1_1609
JH9:
SaurJH9_1576
JKD6008:
SAA6008_01487 (acoA)
JKD6159:
SAA6159_01453 (acoA)
LGA251:
SARLGA251_14240 (bfmBAA)
M013:
M013TW_1533
MRSA252:
SAR1595 (bfmBAA)
MSHR1132:
SAMSHR1132_13580
MSSA476:
SAS1456
Mu3:
SAHV_1505 (bfmBAA)
Mu50:
SAV1517 (bfmBAA)
MW2:
MW1470 (bfmBAA)
RF122:
SAB1390c
ST398:
SAPIG1583
T0131:
SAT0131_01611
TCH60:
HMPREF0772_11623 (bkdA)
TW20:
SATW20_15140 (bfmBAA)
USA300_TCH1516:
USA300HOU_1519 (odpA)
VC40:
SAVC_06835
⊟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 MIDYKSLGLSEEDLKVIYKWMDLGRKIDERLWLLNRAGKIPFVVSGQGQEATQIGMAYAL
N315 MIDYKSLGLSEEDLKVIYKWMDLGRKIDERLWLLNRAGKIPFVVSGQGQEATQIGMAYAL
NCTC8325 MIDYKSLGLSEEDLKVIYKWMDLGRKIDERLWLLNRAGKIPFVVSGQGQEATQIGMAYAL
Newman MIDYKSLGLSEEDLKVIYKWMDLGRKIDERLWLLNRAGKIPFVVSGQGQEATQIGMAYAL
USA300_FPR3757 MIDYKSLGLSEEDLKVIYKWMDLGRKIDERLWLLNRAGKIPFVVSGQGQEATQIGMAYAL
************************************************************
COL EEGDITAPYYRDLAFVTYMGISAYDTFLSAFGKKDDVNSGGKQMPSHFSSRAKNILSQSS
N315 EEGDITAPYYRDLAFVTYMGISAYDTFLSAFGKKDDVNSGGKQMPSHFSSRAKNILSQSS
NCTC8325 EEGDITAPYYRDLAFVTYMGISAYDTFLSAFGKKDDVNSGGKQMPSHFSSRAKNILSQSS
Newman EEGDITAPYYRDLAFVTYMGISAYDTFLSAFGKKDDVNSGGKQMPSHFSSRAKNILSQSS
USA300_FPR3757 EEGDITAPYYRDLAFVTYMGISAYDTFLSAFGKKDDVNSGGKQMPSHFSSRAKNILSQSS
************************************************************
COL PVATQIPHAVGAALALKMDGKKKIATATVGEGSSNQGDFHEGLNFAGVHKLPFVCVIINN
N315 PVATQIPHAVGAALALKMDGKKKIATATVGEGSSNQGDFHEGLNFAGVHKLPFVCVIINN
NCTC8325 PVATQIPHAVGAALALKMDGKKKIATATVGEGSSNQGDFHEGLNFAGVHKLPFVCVIINN
Newman PVATQIPHAVGAALALKMDGKKKIATATVGEGSSNQGDFHEGLNFAGVHKLPFVCVIINN
USA300_FPR3757 PVATQIPHAVGAALALKMDGKKKIATATVGEGSSNQGDFHEGLNFAGVHKLPFVCVIINN
************************************************************
COL KYAISVPDSLQYAAEKLSDRALGYGIHGEQVDGNDPLAMYKAMKEARDRAISGQGSTLIE
N315 KYAISVPDSLQYAAEKLSDRALGYGIHGEQVDGNDPLAMYKAMKEARDRAISGQGSTLIE
NCTC8325 KYAISVPDSLQYAAEKLSDRALGYGIHGEQVDGNDPLAMYKAMKEARDRAISGQGSTLIE
Newman KYAISVPDSLQYAAEKLSDRALGYGIHGEQVDGNDPLAMYKAMKEARDRAISGQGSTLIE
USA300_FPR3757 KYAISVPDSLQYAAEKLSDRALGYGIHGEQVDGNDPLAMYKAMKEARDRAISGQGSTLIE
************************************************************
COL AVTSRMTAHSSDDDDQYRTKEERETLKKADCNEKFKKELLSAGIIDDAWLAEIEAEHKDI
N315 AVTSRMTAHSSDDDDQYRTKEEREALKKADCNEKFKKELLSAGIIDDAWLAEIEAEHKDI
NCTC8325 AVTSRMTAHSSDDDDQYRTKEERETLKKADCNEKFKKELLSAGIIDDAWLAEIEAEHKDI
Newman AVTSRMTAHSSDDDDQYRTKEERETLKKADCNEKFKKELLSAGIIDDAWLAEIEAEHKDI
USA300_FPR3757 AVTSRMTAHSSDDDDQYRTKEERETLKKADCNEKFKKELLSAGIIDDAWLAEIEAEHKDI
************************:***********************************
COL INKATKAAEDAPYPSVEEAYAFVYEEGSLN
N315 INKATKAAEDAPYPSVEEAYAFVYEEGSLN
NCTC8325 INKATKAAEDAPYPSVEEAYAFVYEEGSLN
Newman INKATKAAEDAPYPSVEEAYAFVYEEGSLN
USA300_FPR3757 INKATKAAEDAPYPSVEEAYAFVYEEGSLN
******************************
- ↑ Vineet K Singh, Dipti S Hattangady, Efstathios S Giotis, Atul K Singh, Neal R Chamberlain, Melissa K Stuart, Brian J Wilkinson
Insertional inactivation of branched-chain alpha-keto acid dehydrogenase in Staphylococcus aureus leads to decreased branched-chain membrane fatty acid content and increased susceptibility to certain stresses.
Appl Environ Microbiol: 2008, 74(19);5882-90
[PubMed:18689519] [WorldCat.org] [DOI] (I p)Vineet K Singh, Sirisha Sirobhushanam, Robert P Ring, Saumya Singh, Craig Gatto, Brian J Wilkinson
Roles of pyruvate dehydrogenase and branched-chain α-keto acid dehydrogenase in branched-chain membrane fatty acid levels and associated functions in Staphylococcus aureus.
J Med Microbiol: 2018, 67(4);570-578
[PubMed:29498620] [WorldCat.org] [DOI] (I p)