ID   A0A3N2R909_9RHOB        Unreviewed;       324 AA.
AC   A0A3N2R909;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   SubName: Full=Thiamine pyrophosphate-dependent dehydrogenase E1 component subunit alpha {ECO:0000313|EMBL:ROU03826.1};
GN   ORFNames=EAT49_04975 {ECO:0000313|EMBL:ROU03826.1};
OS   Histidinibacterium lentulum.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Histidinibacterium.
OX   NCBI_TaxID=2480588 {ECO:0000313|EMBL:ROU03826.1, ECO:0000313|Proteomes:UP000268016};
RN   [1] {ECO:0000313|EMBL:ROU03826.1, ECO:0000313|Proteomes:UP000268016}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B17 {ECO:0000313|EMBL:ROU03826.1,
RC   ECO:0000313|Proteomes:UP000268016};
RA   Wang G.;
RT   "Histidinibacterium lentulum gen. nov., sp. nov., a marine bacterium from
RT   the culture broth of Picochlorum sp. 122.";
RL   Submitted (OCT-2018) 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:ROU03826.1}.
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DR   EMBL; RDRB01000002; ROU03826.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N2R909; -.
DR   OrthoDB; 9766715at2; -.
DR   Proteomes; UP000268016; 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; 3.40.50.970; -; 1.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR029061; THDP-binding.
DR   PANTHER; PTHR11516:SF60; PYRUVATE DEHYDROGENASE E1 COMPONENT SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR11516; PYRUVATE DEHYDROGENASE E1 COMPONENT, ALPHA SUBUNIT BACTERIAL AND ORGANELLAR; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000268016}.
FT   DOMAIN          1..289
FT                   /note="Dehydrogenase E1 component"
FT                   /evidence="ECO:0000259|Pfam:PF00676"
SQ   SEQUENCE   324 AA;  34478 MW;  69A8DA83BCC82E44 CRC64;
     MRRIRTFEER VGELFVRGES AGSMLHLSIG EESPAVGVCT AMKDGDTFTT HHRGHGIFLA
     RGADPNRMMA EIAGKETGYC RGKGGSMHIA DMGLGHLGAN AIVGGGVPAV VGAALVAKRR
     NSGAVSVAFF GDGAMQQGVI YESMNMAALW GLPAVFVCIN NQWGMGTRID QATRATALHE
     RAKAFGLAAE TVDGRDVREV HAAAARILDG ARAGSPGFLA VDCYRFFGHA RKDKSPYRTP
     EEEDEGRARD PIAFARAALI EGGMAEGAIG AIDDEVAREM DASIDFAIAS AAPAMDTMFR
     DVYAPGEPEP EPLRTRIDRI LARD
//