ID A2U228_9FLAO Unreviewed; 663 AA.
AC A2U228;
DT 20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 3.
DT 24-JAN-2024, entry version 76.
DE SubName: Full=2-oxoisovalerate dehydrogenase, E1 component, alpha and beta subunit {ECO:0000313|EMBL:EAQ41489.3};
DE EC=1.2.4.4 {ECO:0000313|EMBL:EAQ41489.3};
GN ORFNames=MED152_02205 {ECO:0000313|EMBL:EAQ41489.3};
OS Polaribacter sp. MED152.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=313598 {ECO:0000313|EMBL:EAQ41489.3, ECO:0000313|Proteomes:UP000006470};
RN [1] {ECO:0000313|EMBL:EAQ41489.3, ECO:0000313|Proteomes:UP000006470}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MED152 {ECO:0000313|EMBL:EAQ41489.3};
RX PubMed=17215843; DOI=10.1038/nature05381;
RA Gomez-Consarnau L., Gonzalez J.M., Coll-Llado M., Gourdon P., Pascher T.,
RA Neutze R., Pedros-Alio C., Pinhassi J.;
RT "Light stimulates growth of proteorhodopsin-containing marine
RT Flavobacteria.";
RL Nature 445:210-213(2007).
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR EMBL; CP004349; EAQ41489.3; -; Genomic_DNA.
DR RefSeq; WP_015480213.1; NC_020830.1.
DR AlphaFoldDB; A2U228; -.
DR STRING; 313598.MED152_02205; -.
DR KEGG; pom:MED152_02205; -.
DR eggNOG; COG0022; Bacteria.
DR eggNOG; COG1071; Bacteria.
DR HOGENOM; CLU_012907_2_1_10; -.
DR OrthoDB; 9771835at2; -.
DR Proteomes; UP000006470; Chromosome.
DR GO; GO:0003863; F:3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity; IEA:UniProtKB-EC.
DR CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1.
DR CDD; cd07036; TPP_PYR_E1-PDHc-beta_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR001017; DH_E1.
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; PF00676; E1_dh; 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); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:EAQ41489.3};
KW Reference proteome {ECO:0000313|Proteomes:UP000006470}.
FT DOMAIN 346..519
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 663 AA; 74144 MW; 6002220859A53820 CRC64;
MTDNIDYNSN YNLDHSTLLN LYQSMLKPRL IEEKMLILLR QGKISKWFSG IGQEAISVGV
TKALDTDEYI LPMHRNLGVF TTREIPLYRL FAQWQGKMSG FTKGRDRSFH FGTQEFNIIG
MISHLGPQLG VADGIALANK LQNKQKVCAV FTGEGGTSEG DFHEALNIAS VWSLPVLFCV
ENNGYGLSTP TSEQFNCKNI ADKGIGYGME SHIIEGNNIL EVYTKVKELA ESMRLTPRPI
LIEFKTFRVR GHEEASGTKY VPQELLDFWG AKDPIINFEN YLRSKSILND EIDNEFKTII
TSEINEHLEI AYAEEKIIPN LEKELNDVYK PFQFKEIKPS KLTNNIRFVD AISEGLEQAM
EQDDHLVIMG QDVAGYGGVF KITDGFTDKF GKDRVRNTPI CESAIVSTAY GLSLNGIKAV
VEMQFADFVS SGFNPIVNLL AKSHYRWAQN ADVVIRMPCG AGVGAGPFHS QTNEAWFTKT
PGLKVVYPAF PEDAKGLLGS AIQDPNPVLF FEHKALYRSV YQDVPKNNYT VEIGKANLIK
EGVNLTIIAY GATVHWVLEV LNKHKEISAD VIDLRTLQPL DTETIYKSVR KTNKAVIVQE
DSLFGGIASD ISALITENCF NSLDAPVKRV GSLDTPIPFQ SDLEQQYLSK SILTNVILEI
NNY
//
