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⊟Summary[edit | edit source]
- pan ID?: SAUPAN004071000
- symbol?: bfmBAB
- synonym: bkdAB
- description?: alpha-ketoacid dehydrogenase subunit beta
- alpha-ketoacid dehydrogenase subunit beta
- 2-oxoisovalerate dehydrogenase, E1 component, beta subunit
- 2-oxoisovalerate dehydrogenase, E1 component subunit beta
- branched-chain alpha-keto acid dehydrogenase E1
- Branched-chain alpha-keto acid dehydrogenase, E1 component, beta subunit
- 2-oxoisovalerate dehydrogenase (acylating) beta subunit
- 2-oxoisovalerate dehydrogenase beta subunit
- 2-oxoisovalerate dehydrogenase subunit beta
- 2-oxoisovalerate dehydrogenase subunit beta (branched-chain alpha-keto acid dehydrogenase e1 component beta chain) (bckdhe1-beta)
- acetoin:2,6-dichlorophenolindophenol oxidoreductase subunit beta
- transketolase, central region
descriptions from strain specific annotations:
- strand?: -
- coordinates?: 4352458..4353441
- synteny block?: BlockID0031030
- occurrence?: in 100% of 34 strains
bkdA2 (bfmBAB, bkdAB) : branched-chain alpha-keto acid dehydrogenase E1 (decarboxylase-acyltransferase beta) 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_1475 (bfmBAB)
08BA02176:
C248_1559 (bfmBAB)
11819-97:
MS7_1534 (bfmBAB)
6850:
RSAU_001383
71193:
ST398NM01_1582
ECT-R 2:
ECTR2_1368
ED133:
SAOV_1517
ED98:
SAAV_1509
HO 5096 0412:
SAEMRSA15_14370 (bfmBAB)
JH1:
SaurJH1_1608
JH9:
SaurJH9_1575
JKD6008:
SAA6008_01486 (bfmBAB)
JKD6159:
SAA6159_01452 (bfmBAB)
JSNZ:
JSNZ_001507
LGA251:
SARLGA251_14230 (bfmBAB)
M013:
M013TW_1532
MRSA252:
SAR1594 (bfmBAB)
MSHR1132:
SAMSHR1132_13570
MSSA476:
SAS1455
Mu3:
SAHV_1504 (bfmBAB)
Mu50:
SAV1516 (bfmBAB)
MW2:
MW1469 (bfmBAB)
RF122:
SAB1389c
ST398:
SAPIG1582
T0131:
SAT0131_01610
TCH60:
HMPREF0772_11624 (acoB)
TW20:
SATW20_15130 (bfmBAB)
USA300_TCH1516:
USA300HOU_1518
VC40:
SAVC_06830
⊟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 MAKLSYLEAIRQAQDLALQQNKDVFILGEDVGRKGGVFGTTQGLQQKYGEDRVIDTPLAE
N315 MAKLSYLEAIRQAQDLALQQNKDVFILGEDVGKKGGVFGTTQGLQQQYGEDRVIDTPLAE
NCTC8325 MAKLSYLEAIRQAQDLALQQNKDVFILGEDVGRKGGVFGTTQGLQQKYGEDRVIDTPLAE
Newman MAKLSYLEAIRQAQDLALQQNKDVFILGEDVGRKGGVFGTTQGLQQKYGEDRVIDTPLAE
USA300_FPR3757 MAKLSYLEAIRQAQDLALQQNKDVFILGEDVGRKGGVFGTTQGLQQKYGEDRVIDTPLAE
********************************:*************:*************
COL SNIVGTAIGAAMVGKRPIAEIQFADFILPATNQIISEAAKMRYRSNNDWQCPLTIRAPFG
N315 SNIVGTAIGAAMVGKRPIAEIQFADFILPATNQIISEAAKMRYRSNNDWQCPLTIRAPFG
NCTC8325 SNIVGTAIGAAMVGKRPIAEIQFADFILPATNQIISEAAKMRYRSNNDWQCPLTIRAPFG
Newman SNIVGTAIGAAMVGKRPIAEIQFADFILPATNQIISEAAKMRYRSNNDWQCPLTIRAPFG
USA300_FPR3757 SNIVGTAIGAAMVGKRPIAEIQFADFILPATNQIISEAAKMRYRSNNDWQCPLTIRAPFG
************************************************************
COL GGVHGGLYHSQSIESIFASSPGLTIVIPSTPYDAKGLLLSSIESNDPVLYFEHKKAYRFL
N315 GGVHGGLYHSQSIESIFASSPGLTIVIPSTPYDAKGLLLSSIESNDPVLYFEHKKAYRFL
NCTC8325 GGVHGGLYHSQSIESIFASSPGLTIVIPSTPYDAKGLLLSSIESNDPVLYFEHKKAYRFL
Newman GGVHGGLYHSQSIESIFASSPGLTIVIPSTPYDAKGLLLSSIESNDPVLYFEHKKAYRFL
USA300_FPR3757 GGVHGGLYHSQSIESIFASSPGLTIVIPSTPYDAKGLLLSSIESNDPVLYFEHKKAYRFL
************************************************************
COL KEEVPEEYYTVPLGKADVKREGEDLTVFCYGLMVNYCLQAADILAADGINVEVVDLRTVY
N315 KEEVPEEYYTVPLGKADVKREGEDLTVFCYGLMVNYCLQAADILAADGINVEVVDLRTVY
NCTC8325 KEEVPEEYYTVPLGKADVKREGEDLTVFCYGLMVNYCLQAADILAADGINVEVVDLRTVY
Newman KEEVPEEYYTVPLGKADVKREGEDLTVFCYGLMVNYCLQAADILAADGINVEVVDLRTVY
USA300_FPR3757 KEEVPEEYYTVPLGKADVKREGEDLTVFCYGLMVNYCLQAADILAADGINVEVVDLRTVY
************************************************************
COL PLDKETIIDRAKHTGKVLLVTEDNLEGSIMSEVSAIIAEHCLFDLDAPIMRLAAPDVPSM
N315 PLDKETIIDRAKNTGKVLLVTEDNLEGSIMSEVSAIIAEHCLFDLDAPIMRLAAPDVPSM
NCTC8325 PLDKETIIDRAKHTGKVLLVTEDNLEGSIMSEVSAIIAEHCLFDLDAPIMRLAAPDVPSM
Newman PLDKETIIDRAKHTGKVLLVTEDNLEGSIMSEVSAIIAEHCLFDLDAPIMRLAAPDVPSM
USA300_FPR3757 PLDKETIIDRAKHTGKVLLVTEDNLEGSIMSEVSAIIAEHCLFDLDAPIMRLAAPDVPSM
************:***********************************************
COL PFSPVLENEIMMNPEKILNKMRELAEF
N315 PFSPVLENEIMMNPEKILNKMRELAEF
NCTC8325 PFSPVLENEIMMNPEKILNKMRELAEF
Newman PFSPVLENEIMMNPEKILNKMRELAEF
USA300_FPR3757 PFSPVLENEIMMNPEKILNKMRELAEF
***************************
- ↑ 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)