ID A0A0P7Y8H1_9BACT Unreviewed; 804 AA.
AC A0A0P7Y8H1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Pyruvate/2-oxoglutarate dehydrogenase complex, dehydrogenase (E1) component, eukaryotic type, beta s {ECO:0000313|EMBL:KPQ16407.1};
GN ORFNames=HLUCCX10_07845 {ECO:0000313|EMBL:KPQ16407.1};
OS Algoriphagus marincola HL-49.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Algoriphagus.
OX NCBI_TaxID=1305737 {ECO:0000313|EMBL:KPQ16407.1, ECO:0000313|Proteomes:UP000050421};
RN [1] {ECO:0000313|EMBL:KPQ16407.1, ECO:0000313|Proteomes:UP000050421}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL-49 {ECO:0000313|EMBL:KPQ16407.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (SEP-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:KPQ16407.1}.
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DR EMBL; LJXT01000040; KPQ16407.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7Y8H1; -.
DR STRING; 1305737.GCA_000526355_00389; -.
DR PATRIC; fig|1305737.6.peg.2246; -.
DR eggNOG; COG0022; Bacteria.
DR eggNOG; COG1071; Bacteria.
DR OrthoDB; 9769337at2; -.
DR Proteomes; UP000050421; 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 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:KPQ16407.1}.
FT DOMAIN 471..645
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 804 AA; 90283 MW; 3EB6DD3B174CD8C0 CRC64;
MATAEKSVKK TQDSTADREA VLNDFRIALI SRHASLMGRK EVFMGKAKFG IFGDGKELAQ
IAMARAFQKG DFRAGYYRDQ TFMFALGELT VQQYFAQLYA HTNVDAEPAS AGRLMNGHFA
TRSLNDDGSW KSLTDRYNSA ADISPTAAQM PKLLGLAFAS KLYRENKGLK GFKDFSINGN
EVAWGTIGNA STSEGMFFES INAAGVLQVP MVTAIWDDGY GISVPQEYHT TKGSISEVLE
GFQRNDEQKG FEIIRVKGWD YEALFNAFQK AGNIARSEHA PVLIHVQEMT QPQGHSTSGS
HERYKSKERL DWEKEWDCIK QFREYILSRE LASADELDKI DAEAKAQVKK EKEAAWNDFL
GEIKEELKEA VSLIRDAAQT SNRKVVLEQL VQDLSKTINP IRKDVISTVR KALLNLRFDQ
SEAKNKLQTW YQQQQEKNFD RYSSHLYSQS EWSALKVAER LPEFSEDSSI VDGREVLQAF
FDYKLENDPR FFAFGEDVGK IGDVNQAFAG LQAKYGDLRV SDTGIRECTI VGQGIGAALR
GLRPLAEIQY LDYLLYGIQL LSDDLASLQY RTKGGQKAPL IVRTRGHRLE GVWHAGSPMG
MILSALRGML ICVPRNMTQA AGMYNTLLQS DDPALVIECL NGYRLKEKMP ENMGEYTVPM
GKPEVLRSGK DITLVTYGSM CRIVLEAAEE LSEMDIDVEV IDVQTLIPFD RFGVIGESVK
KTNRVIFADE DVPGGASAYM LQQAIEEQQL FKFLDSEPQT LSAKAHRPAY SSDGDYFSKP
STEDVIEKVY LLMHEVNPKK FPKF
//
