ID A0A1R4J9N7_9MICO Unreviewed; 367 AA.
AC A0A1R4J9N7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Branched-chain alpha-keto acid dehydrogenase, E1 component, alpha subunit {ECO:0000313|EMBL:SJN28505.1};
DE EC=1.2.4.4 {ECO:0000313|EMBL:SJN28505.1};
GN ORFNames=FM104_06080 {ECO:0000313|EMBL:SJN28505.1};
OS Microbacterium esteraromaticum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=57043 {ECO:0000313|EMBL:SJN28505.1, ECO:0000313|Proteomes:UP000196320};
RN [1] {ECO:0000313|EMBL:SJN28505.1, ECO:0000313|Proteomes:UP000196320}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B Mb 05.01 {ECO:0000313|EMBL:SJN28505.1,
RC ECO:0000313|Proteomes:UP000196320};
RA Peterson S.W.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR EMBL; FUKO01000019; SJN28505.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R4J9N7; -.
DR OrthoDB; 9766715at2; -.
DR Proteomes; UP000196320; Unassembled WGS sequence.
DR GO; GO:0003863; F:3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR017596; PdhA/BkdA.
DR InterPro; IPR029061; THDP-binding.
DR NCBIfam; TIGR03181; PDH_E1_alph_x; 1.
DR PANTHER; PTHR43380; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43380:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR Pfam; PF00676; E1_dh; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:SJN28505.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000196320}.
FT DOMAIN 48..313
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
SQ SEQUENCE 367 AA; 39899 MW; 3DBCC5EE275A87FA CRC64;
MQQDDLLPRD VPVRLIDEDG TAVEDTQYQM PDADHLLAAY RGLVEGRRIN DQANALVRQG
RLAVYPSSHG QEACQIGASL VLGEHDWLFP TYRDSVAVIA RGVTPADAMV LLKGDWHSGY
DPAEHRVAPQ ATPLATQLLH AVGFAYAAKR RGEDTVVMAM CGDGSTSEGD FHEALNFAAV
FHVPVVFFIQ NNEFAISVPL SRQTAAPSLA HKAIGYGMPG QRVDGNDVAA VLAVLGDAVE
RARSGGGPAL IEAHTYRMQA HTNADDDTRY RERDEVQAWV ARDPLARLRA LLRAQGVLDD
AAEEQLAAGA EEIAAAMRVA LNTDSTLDPE DLFRFVTADR SPQLEEQWQL LRGEIDRTAL
AESGGTR
//
