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Database: UniProt
Entry: I1D851_9PSEU
LinkDB: I1D851_9PSEU
Original site: I1D851_9PSEU 
ID   I1D851_9PSEU            Unreviewed;       346 AA.
AC   I1D851;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   SubName: Full=Pyruvate/2-oxoglutarate dehydrogenase complex, dehydrogenase component beta subunit {ECO:0000313|EMBL:EIF01126.1};
GN   ORFNames=SacglDRAFT_04297 {ECO:0000313|EMBL:EIF01126.1};
OS   Saccharomonospora glauca K62.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharomonospora.
OX   NCBI_TaxID=928724 {ECO:0000313|EMBL:EIF01126.1, ECO:0000313|Proteomes:UP000005087};
RN   [1] {ECO:0000313|EMBL:EIF01126.1, ECO:0000313|Proteomes:UP000005087}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K62 {ECO:0000313|EMBL:EIF01126.1,
RC   ECO:0000313|Proteomes:UP000005087};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Land M.L., Hauser L., Brambilla E., Klenk H.-P., Woyke T.J.;
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000005087}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K62 {ECO:0000313|Proteomes:UP000005087};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Held B., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Pagani I., Brambilla E.-M.,
RA   Klenk H.-P., Woyke T.;
RT   "Noncontiguous Finished sequence of chromosome of Saccharomonospora glauca
RT   K62.";
RL   Submitted (JAN-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; CM001484; EIF01126.1; -; Genomic_DNA.
DR   RefSeq; WP_005467014.1; NZ_CM001484.1.
DR   AlphaFoldDB; I1D851; -.
DR   STRING; 928724.SacglDRAFT_04297; -.
DR   eggNOG; COG0022; Bacteria.
DR   HOGENOM; CLU_012907_1_0_11; -.
DR   OrthoDB; 9766715at2; -.
DR   Proteomes; UP000005087; Chromosome.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR   CDD; cd07036; TPP_PYR_E1-PDHc-beta_like; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
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; 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); 1.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE   4: Predicted;
KW   Pyruvate {ECO:0000313|EMBL:EIF01126.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005087}.
FT   DOMAIN          23..198
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   346 AA;  37150 MW;  94110D1C79ADA639 CRC64;
     MAAPVNAKPA TPTTQAATNV QNLTIGKALN AGLRAAMEAD EKVIVMGEDV GKLGGVFRIT
     DGLRKDFGEH RVLDTPLAES GIVGTAVGLA VRGFRPVCEI QFEGFIFPAF DQISSQLAKL
     HYRTQGAIKV PVVIRVPFGG GIGAVEHHSE SPESLFAHIP GLKVVSCSNP VDAYWMIQQA
     IQCDDPVLFF EPKKLYHSGA LKAPVDPSAT PDPLFASRVL RQGTAATLVA YGPSVQVCLA
     AADAAAEEGT ELEVIDLRTL SPLDLEPVFE SVRRTGRLIA VSEASSEASL TSEIAARVQQ
     ECFYSLEAPV LRVTGFDTPY PPSKLEEHFL PDLDRVLHAV DRALEW
//
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