ID   A0A0N8W546_9SPHI        Unreviewed;       658 AA.
AC   A0A0N8W546;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Dehydrogenase {ECO:0000313|EMBL:KQB99682.1};
GN   ORFNames=AQF98_18560 {ECO:0000313|EMBL:KQB99682.1};
OS   Pedobacter sp. Hv1.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=1740090 {ECO:0000313|EMBL:KQB99682.1, ECO:0000313|Proteomes:UP000050543};
RN   [1] {ECO:0000313|EMBL:KQB99682.1, ECO:0000313|Proteomes:UP000050543}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hv1 {ECO:0000313|EMBL:KQB99682.1,
RC   ECO:0000313|Proteomes:UP000050543};
RA   Ott B.M., Beka L., Graf J., Rio R.;
RT   "Draft Genome Sequence of a Pedobacter sp. Strain Hv1, an Isolate From
RT   Medicinal Leech Mucosal Castings.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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:KQB99682.1}.
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DR   EMBL; LLWP01000009; KQB99682.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N8W546; -.
DR   STRING; 1740090.AQF98_18560; -.
DR   OrthoDB; 9769337at2; -.
DR   Proteomes; UP000050543; Unassembled WGS sequence.
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   Reference proteome {ECO:0000313|Proteomes:UP000050543}.
FT   DOMAIN          341..514
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   658 AA;  73239 MW;  49BAA7944166686C CRC64;
     MQFDRKDKDD NRLLTLYKTL LYPRMVEEKM LILLRQGRIG KWFSGIGQEA IAVGSTLAMQ
     SEEYILPMHR NLGVFTSRNI PLKKLMAQWQ GKISGFTKGR DRSFHFGTQD YKIIGMISHL
     GPQMALADGI ALADLIANKK QATLVFTGEG ATSEGDFHEA INVASVWNLP VIFLIENNGY
     GLSTPINEQF NCKHLVDRAI GYGIEGIQLD GNNILEVYDK LSEIAASIRE NPRPVLVECL
     TFRMRGHEEA SGTKYVPQHL FDEWTKKDPV KNFEDYLVAE NILNEELIAT IKREYKAEIE
     QDVEEAFNEQ EPEAHTAVEV ADMFAPYEAQ QSLPSAAQSE KRYLDAITDG LREGMQRYEN
     LVIMGQDIAE YGGAFKITDG FVAQFGKARV RNTPICESAI VGTGLGLSIN GYKAVVEMQF
     ADFVTCGFNQ IVNNLAKTHY RWGEKADVVV RMPTGAGTGA GPFHSQSNEA WFTKTPGLKV
     VYPAFPYDAK GLLIAAIEDP NPVIYFEHKY LYRSLSGLVP DGYYTVEIGK AKVLKEGEQL
     AIITYGLGVH WALDYLNKHP EISATLVDLV SLQPWDKETV AAAVKATGRV IILHEDTLSS
     GFGAELAAWI GENCFQDLDA PVMRCASLDT AIPMSKVLED DFLAKARLAE TVEKLLVY
//