Jump to navigation
Jump to search
⊟Summary[edit | edit source]
- pan ID?: SAUPAN004070000
- symbol?: bfmBB
- synonym: bkdB
- description?: 2-oxoglutarate dehydrogenase E2
- 2-oxoglutarate dehydrogenase E2
- 2-oxoisovalerate dehydrogenase, E2 component, dihydrolipoamide acetyltransferase
- 2-oxo acid dehydrogenase subunit E2
- 2-oxoisovalerate dehydrogenase, E2 component
- branched-chain alpha-keto acid dehydrogenase E2 subunit
- dihydrolipoamide acetyltransferase family protein
- 2-oxoisovalerate dehydrogenase E2 component, dihydrolipamide acetyltransferase
- branched-chain alpha-keto aciddehydrogenase complex lipoamide acyltransferase subunit
- dehydrogenase catalytic domain-containing protein
- dihydrolipoamide acyltransferase
- Dihydrolipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex
- dihydrolipoyllysine-residue acetyltransferase
- lipoamide acyltransferase component ofbranched-chain alpha-keto acid dehydrogenase complex
- lipoamide acyltransferase component of branched-chain alpha-keto aciddehydrogenase complex (Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase) (E2) (Dihydrolipoamide branched chaintransacylase)
descriptions from strain specific annotations:
- strand?: -
- coordinates?: 4351157..4352445
- synteny block?: BlockID0031020
- occurrence?: in 100% of 34 strains
bkdB (bfmBB) : branched-chain alpha-keto acid dehydrogenase E2 (dihydrolipoamide transacylase) 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_1474 (bmfBB)
08BA02176:
C248_1558 (bfmB)
11819-97:
MS7_1533
6850:
RSAU_001381
71193:
ST398NM01_1581
ECT-R 2:
ECTR2_1367
ED133:
SAOV_1516
ED98:
SAAV_1508
HO 5096 0412:
SAEMRSA15_14360 (bfmB)
JH1:
SaurJH1_1607
JH9:
SaurJH9_1574
JKD6008:
SAA6008_01485 (bfmB)
JKD6159:
SAA6159_01451 (bfmB)
JSNZ:
JSNZ_001506
LGA251:
SARLGA251_14220 (bfmB)
M013:
M013TW_1531
MRSA252:
SAR1593 (bfmB)
MSHR1132:
SAMSHR1132_13560
MSSA476:
SAS1454
Mu3:
SAHV_1503 (bmfBB)
Mu50:
SAV1515 (bmfBB)
MW2:
MW1468 (bmfBB)
RF122:
SAB1388c
ST398:
SAPIG1581
T0131:
SAT0131_01609
TCH60:
HMPREF0772_11625 (bkdC)
TW20:
SATW20_15120 (bfmB)
USA300_TCH1516:
USA300HOU_1517 (bmfBB)
VC40:
SAVC_06825
⊟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 MEITMPKLGESVHEGTIEQWLVSVGDHIDEYEPLCEVITDKVTAEVPSTISGTITEILVE
N315 MEITMPKLGESVHEGTIEQWLVSVGDHIDEYEPLCEVITDKVTAEVPSTISGTITEILVE
NCTC8325 MEITMPKLGESVHEGTIEQWLVSVGDHIDEYEPLCEVITDKVTAEVPSTISGTITEILVE
Newman MEITMPKLGESVHEGTIEQWLVSVGDHIDEYEPLCEVITDKVTAEVPSTISGTITEILVE
USA300_FPR3757 MEITMPKLGESVHEGTIEQWLVSVGDHIDEYEPLCEVITDKVTAEVPSTISGTITEILVE
************************************************************
COL AGQTVAIDTIICKIETADEKTNETTEEIQAKVDEHTQKSTKKASATVEQTSTAKQNQPRN
N315 AGQTVAIDTIICKIETADEKTNETTEEIQAKVDEHTQKSTKKASATVEQTFTAKQNQPRN
NCTC8325 AGQTVAIDTIICKIETADEKTNETTEEIQAKVDEHTQKSTKKASATVEQTSTAKQNQPRN
Newman AGQTVAIDTIICKIETADEKTNETTEEIQAKVDEHTQKSTKKASATVEQTSTAKQNQPRN
USA300_FPR3757 AGQTVAIDTIICKIETADEKTNETTEEIQAKVDEHTQKSTKKASATVEQTSTAKQNQPRN
************************************************** *********
COL NGRFSPVVFKLASEHDIDLSQVVGSGFEGRVTKKDIMSVIENGGTTAQSDKQVQTKSTSV
N315 NGRFSPVVFKLASEHDIDLSQVVGSGFEGRVTKKDIMSVIENGGTTAQSDKQVQTKSTSV
NCTC8325 NGRFSPVVFKLASEHDIDLSQVVGSGFEGRVTKKDIMSVIENGGTTAQSDKQVQTKSTSV
Newman NGRFSPVVFKLASEHDIDLSQVVGSGFEGRVTKKDIMSVIENGGTTAQSDKQVQTKSTSV
USA300_FPR3757 NGRFSPVVFKLASEHDIDLSQVVGSGFEGRVTKKDIMSVIENGGTTAQSDKQVQTKSTSV
************************************************************
COL DTSSNQSSEDNSENSTIPVNGVRKAIAQNMVNSVTEIPHAWMMIEVDATNLVKTRNHYKN
N315 DTSSNQSSEDNSENSTIPVNGVRKAIAQNMVNSVTEIPHAWMMIEVDATNLVNTRNHYKN
NCTC8325 DTSSNQSSEDNSENSTIPVNGVRKAIAQNMVNSVTEIPHAWMMIEVDATNLVNTRNHYKN
Newman DTSSNQSSEDNSENSTIPVNGVRKAIAQNMVNSVTEIPHAWMMIEVDATNLVNTRNHYKN
USA300_FPR3757 DTSSNQSSEDNSENSTIPVNGVRKAIAQNMVNSVTEIPHAWMMIEVDATNLVNTRNHYKN
****************************************************:*******
COL SFKNKEGYNLTFFAFFVKAVADALKAYPLLNSSWQGNEIVLHKDINISIAVADENKLYVP
N315 SFKNKEGYNLTFFAFFVKAVADALKAYPLLNSSWQGNEIVLHKDINISIAVADENKLYVP
NCTC8325 SFKNKEGYNLTFFAFFVKAVADALKAYPLLNSSWQGNEIVLHKDINISIAVADENKLYVP
Newman SFKNKEGYNLTFFAFFVKAVADALKAYPLLNSSWQGNEIVLHKDINISIAVADENKLYVP
USA300_FPR3757 SFKNKEGYNLTFFAFFVKAVADALKAYPLLNSSWQGNEIVLHKDINISIAVADENKLYVP
************************************************************
COL VIKHADEKSIKGIAREINTLATKARNKQLTAEDMQGGTFTVNNTGTFGSVSSMGIINHPQ
N315 VIKHADEKSIKGIAREINTLATKARNKQLTTEDMQGGTFTVNNTGTFGSVSSMGIINHPQ
NCTC8325 VIKHADEKSIKGIAREINTLATKARNKQLTAEDMQGGTFTVNNTGTFGSVSSMGIINHPQ
Newman VIKHADEKSIKGIAREINTLATKARNKQLTAEDMQGGTFTVNNTGTFGSVSSMGIINHPQ
USA300_FPR3757 VIKHADEKSIKGIAREINTLATKARNKQLTAEDMQGGTFTVNNTGTFGSVSSMGIINHPQ
******************************:*****************************
COL AAILQVESIVKKPVVINDMIAIRNMVNLCISIDHRILDGLQTGKFMNHIKQRIEQYTLEN
N315 AAILQVESIVKKPVVINDMIAIRSMVNLCISIDHRILDGLQTGKFMNHIKQRIEQYTLEN
NCTC8325 AAILQVESIVKKPVVINDMIAIRNMVNLCISIDHRILDGLQTGKFMNHIKQRIEQYTLEN
Newman AAILQVESIVKKPVVINDMIAIRNMVNLCISIDHRILDGLQTGKFMNHIKQRIEQYTLEN
USA300_FPR3757 AAILQVESIIKKPVVINDMIAIRNMVNLCISIDHRILDGLQTGKFMNHIKQRIEQYTLEN
*********:*************.************************************
COL TNIY
N315 TNIY
NCTC8325 TNIY
Newman TNIY
USA300_FPR3757 TNIY
****
- ↑ 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)