ID A0A147K7Q6_9BACI Unreviewed; 327 AA.
AC A0A147K7Q6;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=2-oxoisovalerate dehydrogenase {ECO:0000313|EMBL:KUP06154.1};
GN ORFNames=Q75_09470 {ECO:0000313|EMBL:KUP06154.1};
OS Bacillus coahuilensis p1.1.43.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1150625 {ECO:0000313|EMBL:KUP06154.1, ECO:0000313|Proteomes:UP000074108};
RN [1] {ECO:0000313|EMBL:KUP06154.1, ECO:0000313|Proteomes:UP000074108}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=p1.1.43 {ECO:0000313|Proteomes:UP000074108};
RX PubMed=26903955; DOI=10.3389/fmicb.2016.00058;
RA Gomez-Lunar Z., Hernandez-Gonzalez I., Rodriguez-Torres M.D., Souza V.,
RA Olmedo-Alvarez G.;
RT "Microevolution Analysis of Bacillus coahuilensis Unveils Differences in
RT Phosphorus Acquisition Strategies and Their Regulation.";
RL Front. Microbiol. 7:58-58(2016).
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUP06154.1}.
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DR EMBL; LDYG01000030; KUP06154.1; -; Genomic_DNA.
DR RefSeq; WP_059283053.1; NZ_LDYG01000030.1.
DR AlphaFoldDB; A0A147K7Q6; -.
DR STRING; 1150625.Q75_09470; -.
DR PATRIC; fig|1150625.3.peg.2014; -.
DR OrthoDB; 9771835at2; -.
DR Proteomes; UP000074108; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR CDD; cd07036; TPP_PYR_E1-PDHc-beta_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR033248; Transketolase_C.
DR PANTHER; PTHR42980:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR42980; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA-RELATED; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000074108}.
FT DOMAIN 4..179
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 327 AA; 35968 MW; 9494F22F47DF103E CRC64;
MAVMSYIDAV TLAIREEMER DPKVFVLGED VGKKGGVFKA THGLYDQFGE ERVIDTPLAE
SAIAGVGIGA AMYGMRPIAE MQFADFIMPA VNQIISEAAR IRYRSNNDWS CPMVIRAPYG
GGVHGALYHS QSVEAVFANQ PGLKIVMPST PYDVKGLLKA AIRDEDPVLF FEHKRAYRLI
KGEVPEEDYT LPIGKADVKR EGDDITVITY GLCVHFALQA AERLAQDGIE AHILDLRTIY
PLDKEAIIEA ASKTGKVLLV TEDNKEGSII GEVAAIIAEN CLFDLDAPVK RLAGPDVPAM
PYAPTMEKYF MVNPDKIEKA MRELAEF
//