ID   A0A1H5LJ60_9FLAO        Unreviewed;       804 AA.
AC   A0A1H5LJ60;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component {ECO:0000313|EMBL:SEE76218.1};
GN   ORFNames=SAMN04488034_102282 {ECO:0000313|EMBL:SEE76218.1};
OS   Salinimicrobium catena.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Salinimicrobium.
OX   NCBI_TaxID=390640 {ECO:0000313|EMBL:SEE76218.1, ECO:0000313|Proteomes:UP000199448};
RN   [1] {ECO:0000313|EMBL:SEE76218.1, ECO:0000313|Proteomes:UP000199448}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23553 {ECO:0000313|EMBL:SEE76218.1,
RC   ECO:0000313|Proteomes:UP000199448};
RA   de Groot N.N.;
RL   Submitted (OCT-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; FNUG01000002; SEE76218.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H5LJ60; -.
DR   STRING; 390640.SAMN04488034_102282; -.
DR   OrthoDB; 9769337at2; -.
DR   Proteomes; UP000199448; 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:SEE76218.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199448}.
FT   DOMAIN          470..644
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   804 AA;  90320 MW;  2C77C842CE102AB2 CRC64;
     MQSETSSKSA ISFEDFKTQV IEDYRLAVTS RECSLLGRRE VLTGKAKFGI FGDGKEVPQL
     AWAKVFQNGD FRSGYYRDQT FMMAIGALNI QQFFAGLYAT TNIEQEPSSA GRQMGGHFAT
     HSLQEDGTWK NLTQQKNSSA DISPTAGQMP RLVGLAQASK IYRNVEGIDA ANFSQNGNEI
     AWGTIGNAST SEGLFWEAIN AAGVLQVPMV MNVWDDEYGI SVHARHQTTK QNISEVLKGF
     QKDEDKNNGY EIFTVNGWDY PALIETYEKA SRIARENHTP VLIHVKELTQ PQGHSTSGSH
     ERYKSEERLQ WEREHDCNVK MREWMISGNI ATEEELQALE KEVKKEVRDG KKAAWEAHVS
     PVKHRHQEVL PLLDKAAASS SNKTFILQLK KELSENKEPL KKDLLVAARK TLRYMIGEES
     DAKQELINWI ESFTKDTQPQ YSSHLYSDSQ YNALNIDAVA PAYSEDSEEV DGRVVLRDNF
     DKIFEKYPES LIFGEDTGEI GDVNQGLEGL QEKYGEFRIS DTGIREATIL GQGIGMAMRG
     LRPIAEIQYL DYLLYALQIM SDDLATLQYR TAGKQKAPLI IRTRGHRLEG IWHSGSPMGG
     ILHLLRGIHV LVPRNMTKAA GFYNTLLESD EPALIVESLN GYRLKEKMPN NLGEFKTPLG
     VVETMKEGND ITLVSYGSTL RLVEQAAKEL LELGIDAEVI DVQSLLPFDL NQDVVKSVAK
     TSRLLVIDED VPGGASAYIM QKVLEEQNAW RYLDSKPQTL TAKEHRPAYG TDGDYFSKPS
     VEDIFEKVYA IMHESNPGKY PQLR
//