ID A0A2A9G016_9PSEU Unreviewed; 582 AA.
AC A0A2A9G016;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Pyruvate dehydrogenase (Quinone) {ECO:0000313|EMBL:PFG57067.1};
GN ORFNames=ATK36_0620 {ECO:0000313|EMBL:PFG57067.1};
OS Amycolatopsis sulphurea.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=76022 {ECO:0000313|EMBL:PFG57067.1, ECO:0000313|Proteomes:UP000243542};
RN [1] {ECO:0000313|EMBL:PFG57067.1, ECO:0000313|Proteomes:UP000243542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 46092 {ECO:0000313|EMBL:PFG57067.1,
RC ECO:0000313|Proteomes:UP000243542};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (OCT-2017) 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:PFG57067.1}.
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DR EMBL; PDJK01000001; PFG57067.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A9G016; -.
DR Proteomes; UP000243542; 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:PFG57067.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000243542};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 3..119
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 195..321
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 385..531
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 582 AA; 61582 MW; E52A3DE35665D53B CRC64;
MATVAEQLID VLRQSGVRRI YGVVGDSLNP VVDAVRRSGG PARGGIDWVH VRNEEAGAFA
AAAEAQLTGR LAVCAGSCGP GNLHLLQGVY DAHRSGAPVL AIASHIPAAQ IGTGFFQETR
PQHLFAECSY YCELVSTPEQ MPRLARIAVQ NAVGRRGAAV LVLPGDVSHE TAAHATGESA
SLGSPPAMLP AEDDVARLAE RIDRAEKVMI MAGAGCRDAH ADVLALAGTV GAPVGHSLRG
KEFVQYDNPF DVGMSGLLGY GACYQAMHEA DLVLLLGTDF PYDTFLPQRN TVQVDIDAAR
IGRRTVLEFG VQGDVGATIR AVLPKLRGRE DRSFLHDMLR KHERSLQRVV DAYTTDVSQH
VPLHPEYVAD VLDEEAAADA VFTVDTGMCN VWAARYVSPN GHRRILGSFV HGSMANALPH
AIGAQSAAPG RQVIAMCGDG GLAMLLGELL TLKTHGLPVK VVVFNNSSLG MVKLEMLVDG
LPEFGTDHDR VDFAALARAA GLHARRIEDP ADVRDGIREI LACDGPALLD VVTDPNALSI
PPSITAAQVR GFALAASKTV LGGGVGKMLT LAKSNLRNIP RP
//
