ID L0FZI3_ECHVK Unreviewed; 661 AA.
AC L0FZI3;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Pyruvate/2-oxoglutarate dehydrogenase complex, dehydrogenase component beta subunit {ECO:0000313|EMBL:AGA78015.1};
GN OrderedLocusNames=Echvi_1750 {ECO:0000313|EMBL:AGA78015.1};
OS Echinicola vietnamensis (strain DSM 17526 / LMG 23754 / KMM 6221).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Echinicola.
OX NCBI_TaxID=926556 {ECO:0000313|EMBL:AGA78015.1, ECO:0000313|Proteomes:UP000010796};
RN [1] {ECO:0000313|Proteomes:UP000010796}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17526 / LMG 23754 / KMM 6221
RC {ECO:0000313|Proteomes:UP000010796};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Teshima H.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Echinicola vietnamensis DSM 17526.";
RL Submitted (FEB-2012) 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; CP003346; AGA78015.1; -; Genomic_DNA.
DR RefSeq; WP_015265577.1; NC_019904.1.
DR AlphaFoldDB; L0FZI3; -.
DR STRING; 926556.Echvi_1750; -.
DR KEGG; evi:Echvi_1750; -.
DR PATRIC; fig|926556.3.peg.1867; -.
DR eggNOG; COG0022; Bacteria.
DR eggNOG; COG1071; Bacteria.
DR HOGENOM; CLU_012907_2_1_10; -.
DR Proteomes; UP000010796; Chromosome.
DR GO; GO:0016624; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor; IEA:InterPro.
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 Pyruvate {ECO:0000313|EMBL:AGA78015.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010796}.
FT DOMAIN 345..518
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 661 AA; 73089 MW; 6389635B0324F13B CRC64;
MAPNMVFDRK DLSDGDLLHF YEMLLMPRKI EEKMLLLLRQ GKISKWFSGW GQEAISIAAV
MAMREDEFLL PMHRNLGVFT GRGLPLGKLF AQFQGKYSGF TKGRDRSFHF GSVAHHVVGM
ISHLGPQLAV ADGIALASKL GGERKATLVF TGDGATSEGD FHEALNVAAV WQLPVIFVVE
HNGYGLSTPS AEQFRFKQFI DKGPGYGMEA VKVDGNNVLE LYHALSGIAE DIRHRPRPFL
VEAMTYRMRG HEESSGTKYV PKAYFEEGEK YDPVRNFEDY LQEIGVLDQS AKGVIEKRLS
EQIEAGLASA FSAEFPVAGE EELADVYCPS EGKPKEPHSS ATTEKRLVDA ISDGLRLSMR
QFSNLVLMGQ DIGEYGGAFK VTAGFLSEFG AERVRNTPLC ESAIIGAALG LSVKGFKSVV
EMQFADFVSC GFNQIVNNLA KVHYRWGQHA DVVIRMPTGA GVGAGPFHSQ SNEAWFFHTP
GLKILYPSSP QDAKGLLAAA IEDPNPCLFF EHKALYRSVI GQVPDEYYTV EIGKAHLVKE
GDQATVVTYG MGVHWAKRVM ESLDVRVDLL DLRTLLPWDK EAVEKSVKKT NKVMILHEDC
LTGGIGAEIA AWISEHCFEC LDAPVMREGS LDTPVPFAAN LEENFLPENR FKDKLMALLA
Y
//
