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
//