ID   A0A136LZU1_9BACT        Unreviewed;       800 AA.
AC   A0A136LZU1;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Pyruvate/2-oxoglutarate dehydrogenase complex, dehydrogenase component beta subunit {ECO:0000313|EMBL:KXK27178.1};
GN   ORFNames=UZ12_BCD005001373 {ECO:0000313|EMBL:KXK27178.1};
OS   Bacteroidetes bacterium OLB12.
OC   Bacteria; Bacteroidota.
OX   NCBI_TaxID=1619897 {ECO:0000313|EMBL:KXK27178.1, ECO:0000313|Proteomes:UP000070129};
RN   [1] {ECO:0000313|EMBL:KXK27178.1, ECO:0000313|Proteomes:UP000070129}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OLB12 {ECO:0000313|EMBL:KXK27178.1};
RA   Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT   "Genome based microbial ecology of anammox granules in a full-scale
RT   wastewater treatment system.";
RL   Submitted (NOV-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:KXK27178.1}.
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DR   EMBL; LNFR01000052; KXK27178.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A136LZU1; -.
DR   STRING; 1619897.UZ12_BCD005001373; -.
DR   PATRIC; fig|1619897.3.peg.1496; -.
DR   Proteomes; UP000070129; 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:KXK27178.1}.
FT   DOMAIN          466..640
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   800 AA;  88759 MW;  1C0EBF2B0960DC57 CRC64;
     MAQTKTLVTG LSEKKVAAIL ADYRLACESR EASLLGRKEV FMGKAKFGIF GDGKELAQIA
     MAKIFRPGDH RAGYYRDQTF MLAIGELTLQ QYFAQLYAHT SVEADPASAG RLMNGHFATR
     MIDEQGAFKN LAHLKNSSSD ISPTAGQMPR LVGLAYASKL FRNNPGLAAY PELSTAGNEI
     AFGTIGNAST SEGHFFEAIN AAGVLQVPML ISVWDDEYGI SVPAEYQTTK GSISKILAGF
     QRNKSEKGYE IFTVKGWDYL SMISVYEKAE KICREEHVPV LVHVTEMTQP QGHSTSGSHE
     RYKSKERLAW ETEFDCIRKL RQWLIENGVA SADELDEIEK NAKTTARAAK DAAWKDFNKD
     IQKSQKELEQ ILNEAIGEQP AIEDILQELR KTINPLLMDA VKAARKAARL LRYSSSEIRS
     QLVAWIKSSE EKNFDRFSSY LHSQSSWSAL KVNPVAPVYH DNSPLIDGRE ILQACFREAL
     QRDPKVLAFG EDVGKIGDVN QGFAGLQQKF GELRVTDTGI RECTIIGQGI GAALRGLRPI
     AEVQYLDYLL YALQTLSDDL ACLQYRTKGG QKAPLIVRTR GHRLEGVWHA GSPMGMILHA
     LRGMFVLVPR NMTQAAGFYN TLLQSDDPAL IVECLNGYRL KEKLPVNIGE FTVPLGEPEI
     LKQGNDVTIV TYGSMCRIVL EAANELEAIG ISCEVIDVQT LLPFDLPKTI LQSIKKTNRV
     LFTDEDVPGG ATAFMMQQVL EEQGAYQFLD AVPRTLTAKE HRPAYGSDGD YFSKPNAEDV
     FDLVYAIMHE ADPGSFPELY
//