ID A0A0Q5L0Q7_9MICO Unreviewed; 585 AA.
AC A0A0Q5L0Q7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Pyruvate dehydrogenase {ECO:0000313|EMBL:KQR43662.1};
GN ORFNames=ASF82_08430 {ECO:0000313|EMBL:KQR43662.1};
OS Frigoribacterium sp. Leaf164.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Frigoribacterium.
OX NCBI_TaxID=1736282 {ECO:0000313|EMBL:KQR43662.1, ECO:0000313|Proteomes:UP000051005};
RN [1] {ECO:0000313|EMBL:KQR43662.1, ECO:0000313|Proteomes:UP000051005}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf164 {ECO:0000313|EMBL:KQR43662.1,
RC ECO:0000313|Proteomes:UP000051005};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQR43662.1, ECO:0000313|Proteomes:UP000051005}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf164 {ECO:0000313|EMBL:KQR43662.1,
RC ECO:0000313|Proteomes:UP000051005};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQR43662.1}.
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DR EMBL; LMOX01000003; KQR43662.1; -; Genomic_DNA.
DR RefSeq; WP_056056302.1; NZ_LMOX01000003.1.
DR AlphaFoldDB; A0A0Q5L0Q7; -.
DR STRING; 1736282.ASF82_08430; -.
DR OrthoDB; 4959782at2; -.
DR Proteomes; UP000051005; 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 CDD; cd02014; TPP_POX; 1.
DR CDD; cd07039; TPP_PYR_POX; 1.
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; IPR000399; TPP-bd_CS.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR InterPro; IPR047212; TPP_POXB-like.
DR InterPro; IPR047210; TPP_PYR_POXB-like.
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.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Pyruvate {ECO:0000313|EMBL:KQR43662.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051005};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..120
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 195..325
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 388..534
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 585 AA; 61544 MW; 7C11227B5A15561E CRC64;
MADTVADQII AQLVQAGVRR IYGIVGDSLN PIVDAVRRTG GSDAGGIDWI HVRNEEAAAF
MASGDAQMSG ELAVCAGSCG PGNLHLINGL YDAHRSRAKV LAIASHIPSA MIGSDYFQET
HPDRLFVECS GYSEMISTSV QSPSVVAAAI RHTLAGHGVS VVTLPGDVAE LDAEGATPPH
LTTRAPELVP APEDVQALAD AINEAGTVAF FVGEGGRGAH DEIIELAGRV GAPIGHSLRG
KDVIQHDNPY DVGMTGLLGY GAAHAGIHDA DLLVLLGTDF PYPQFLPDGD QVRIAQVDVE
AAVIGRRATV HVPVHGAVLP TLRALAPLVR DKKSRRFLDK TLKKHDKLMN GVVGAYTKKA
DALVPIHPEY AASVLDEVAA DDAIFTADTG MSNVWAARYV TPTAGRRIFG SYLHGSMANA
LPHALGAQFA HPGRQVVSMS GDGGLSMLMG ELITAKMYEL PVKIVVFNNS TLGLVKLEML
VDGYPDFGVD VPYVDYAAVA RSIGIHAVHV DQPGDLRDGF EAVFEHDGPA LIDIATDPQA
LSLPPAITGS QVKGFSLAMS KIVMNGGAGE VVKMARSNLR NVPRP
//
