ID A0A495IIB6_9MICO Unreviewed; 614 AA.
AC A0A495IIB6;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 11.
DE SubName: Full=Pyruvate dehydrogenase (Quinone) {ECO:0000313|EMBL:RKR74855.1};
GN ORFNames=C8E83_1987 {ECO:0000313|EMBL:RKR74855.1};
OS Frondihabitans australicus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Frondihabitans.
OX NCBI_TaxID=386892 {ECO:0000313|EMBL:RKR74855.1, ECO:0000313|Proteomes:UP000280008};
RN [1] {ECO:0000313|EMBL:RKR74855.1, ECO:0000313|Proteomes:UP000280008}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17894 {ECO:0000313|EMBL:RKR74855.1,
RC ECO:0000313|Proteomes:UP000280008};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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:RKR74855.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; RBKS01000001; RKR74855.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A495IIB6; -.
DR OrthoDB; 4959782at2; -.
DR Proteomes; UP000280008; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR047211; POXB-like.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR42981; PYRUVATE DEHYDROGENASE [UBIQUINONE]; 1.
DR PANTHER; PTHR42981:SF2; PYRUVATE DEHYDROGENASE [UBIQUINONE]; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 3: Inferred from homology;
KW Pyruvate {ECO:0000313|EMBL:RKR74855.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000280008};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..118
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 200..329
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 391..545
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 614 AA; 66366 MW; B4875D5C3603354A CRC64;
MAINVSEFII QRIREWGVTR VFGFPGDGIG EFDGMLGKTD RDGDGLEYIR PTHEEICSLM
ATAHAKFTGE VGVCVATSSP GAFHMLNGLY DAQMDNQPVV AIVGQQGLAA LGTFVQQESN
LERTFADVAC YVETITTPDQ AQVVVDTAFR TAKLRLQPAV IVLPHDVQAM DWQEPAPANW
VSRSSAVAAS TAITPPIAEI QAMAEIINAG QKVTFLVGHG ATGATDEVLE AADLAGAGII
TSLRGKAVVP SDVAYHTQQL GLLGSKPSLD QMKGCDTLVI LGANYPYGQF LPATGQARAV
QVDLKPEQLG IRYPTEVNLW GDVKSVLTAV IPLLKRHDDR SWQEKAAADM ADWETEMQDQ
ADIAYDDGVN PRRVFAGLND RLPDGAIVTC DAGTTADWYG HHIRLRRGMM GDLSGRLATM
LAAMPYATAA KFAYPDRPVV CTIGDGAFQM LGMNELITVK KYLSRWKNKQ LIVVIMHNDD
LGQVSWEMRT EDGNPMWRGS QDVETVDYAG YAELLGFRGI AVKDDDAVAA ALDAAFAHDG
VTVIDAYVSR NVPPLPPHIT REYALNTAKS LIKGDPVELD VIKDSAKAMA AEGLDRVKGA
LHLGGDRDLD EKDD
//
