ID   A0A120N6Q8_9FLAO        Unreviewed;       820 AA.
AC   A0A120N6Q8;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component {ECO:0000313|EMBL:CVK15579.1};
GN   ORFNames=Ga0061079_102125 {ECO:0000313|EMBL:CVK15579.1};
OS   Apibacter mensalis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Apibacter.
OX   NCBI_TaxID=1586267 {ECO:0000313|EMBL:CVK15579.1, ECO:0000313|Proteomes:UP000182761};
RN   [1] {ECO:0000313|EMBL:CVK15579.1, ECO:0000313|Proteomes:UP000182761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R-53146 {ECO:0000313|EMBL:CVK15579.1,
RC   ECO:0000313|Proteomes:UP000182761};
RA   McClelland M., Jain A., Saraogi P., Mendelson R., Westerman R.,
RA   SanMiguel P., Csonka L.;
RL   Submitted (JAN-2016) 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; FCOR01000002; CVK15579.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A120N6Q8; -.
DR   STRING; 1586267.GCA_001418685_00404; -.
DR   Proteomes; UP000182761; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Pyruvate {ECO:0000313|EMBL:CVK15579.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000182761}.
FT   DOMAIN          486..660
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   COILED          345..372
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   820 AA;  93284 MW;  85C2BA1EFDDF4472 CRC64;
     MIKDIDPIIS DANLSFQEFK KEVLNDYRLC IISRYCSLLA RKEVLSGKAK FAILGDGKEL
     PQIAMAKVFR NGDFRSGYYR DQTIAFAIGE ITIENYFAQI YADTDDVREP QSGGRMMNCH
     YASHLIDEEG NWKVLTDQKN NAADLSPTAA QIPRLFGLAY ASKIYRNCPG LENKIQFSNQ
     GNEIAFGTIG DASTSEGHFW EALNAACALQ IPMVLSIWDD GYGISVESSK QRAKDDFSEL
     LQGFKRTHEE NSRGCEIITA HGWDYPELIE AYARAEKIAR EKHIPVIIHV SELTQPQGHS
     SSGSHERYKS AERLEWEKEY DCIKKFREWI INYEAYDQST NLKIHVATEE ELLTLEKEIK
     QLVKEHQKNE WNKFRTDMDA LSNHTLSLIS SLADESVKKA FINLEKENFL NLSLPYKKDI
     FHLIRKVLRI VREERTQAKT NLQNWLNQLA ENESHNYNSK LYTDTKFSAL QVPYIPPTYD
     ENAEQVDGRI VIRNNFDKLF EKYPEIIAFG EDVGKIGDVN QGFEGLQEKY GYYRVSDTGI
     RESTIIGQGL GMAMRGLRPI AEIQYLDYIL YCLQTMSDDL ASLSYRTKGK QKAPLIIRTR
     GHRLEGIWHS GSPMGGIINY IRGIYVLVPR NFVQAAGFYN TMIQAEEPCL LIECLNGYRL
     KETIPSNLGE FTTPVGKIEI TREGKDITVV TYGATWKIVS EAANELQTLG IDIEIIDIQS
     LIPFDLSHEI VESLKKTNRL VIADEDVSGG ASSYILQKII EEQNGFQYLD SAPKTITAKD
     HRPAYGSDGD YFSKPSVDDV IEKIYDIMHE VNPSEFPKIS
//