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Database: UniProt
Entry: A0A2K8XAA2_9FLAO
LinkDB: A0A2K8XAA2_9FLAO
Original site: A0A2K8XAA2_9FLAO 
ID   A0A2K8XAA2_9FLAO        Unreviewed;       666 AA.
AC   A0A2K8XAA2;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Dehydrogenase {ECO:0000313|EMBL:AUC79837.1};
GN   ORFNames=CW736_10900 {ECO:0000313|EMBL:AUC79837.1};
OS   Nonlabens sp. MB-3u-79.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Nonlabens.
OX   NCBI_TaxID=2058134 {ECO:0000313|EMBL:AUC79837.1, ECO:0000313|Proteomes:UP000232401};
RN   [1] {ECO:0000313|EMBL:AUC79837.1, ECO:0000313|Proteomes:UP000232401}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MB-3u-79 {ECO:0000313|EMBL:AUC79837.1,
RC   ECO:0000313|Proteomes:UP000232401};
RA   Collins E., Ducluzeau A.-L.;
RT   "Pharmacopeia of the Arctic Ocean.";
RL   Submitted (DEC-2017) 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; CP025116; AUC79837.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K8XAA2; -.
DR   KEGG; nob:CW736_10900; -.
DR   OrthoDB; 9769337at2; -.
DR   Proteomes; UP000232401; 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   Reference proteome {ECO:0000313|Proteomes:UP000232401}.
FT   DOMAIN          350..523
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   666 AA;  74784 MW;  F21648F4CEC2EF6A CRC64;
     MIDTDQTDLK KLYSNTLDHK VLIDLYKKML MPRLIEEKML ILLRQGRISK WFSGIGQEAI
     SIGLTAAMQK DEYILPMHRN LGVFTSREIP LWKLFAQWQG KAEGFTKGRD RSFHFGTQEY
     KIIGMISHLG PQLGVADGIA LAQKMNNTGK ATAVFTGEGG TSEGDFHEAL NVASVWSLPV
     LFCIENNGYG LSTPTSEQYN CEHLADRALG YGMESHIIDG NNIIEVYTKI SAILNDMRER
     PHPVLIEFKT FRRRGHEEAS GTKYVPDELL EYWEQRDPLS RFEKFLLEEH IISSDLIKNW
     NKEFKKEIND GLDTAFAKAL PESTTELELA DVFAPHTFNQ VNPDSSSQNI RLIDAIKDGL
     EEAMDAYDNL VIMGQDVAEY GGVFKITDGF VEKYGRERVR NTPICESAIV EAGMGLSIMG
     MKAVVEMQFA DFVSSGFNPI VNYLAKSYYR WNQKADVVIR MPCGAGVGAG PFHSQTNESW
     FYTVPGLKIV YPSTPADAKG LLIASIEDPN PVLFFEHKAL YRSIYDDVPD GYYNIELGKA
     LNICVGNDAT IITFGAGVHW AKQLIKEENL SIDLIDLRTL VPLDKQAIIK SVQKTGRVLL
     VTEDNLTGSV ISDIAAFISE ECFEYLDAPV MRLGSIDTPI PFEKGLENNY LPLQDLKEKL
     KKLLKY
//
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