ID W5WBW8_9PSEU Unreviewed; 580 AA.
AC W5WBW8;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Pyruvate dehydrogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=KALB_4684 {ECO:0000313|EMBL:AHH98046.1};
OS Kutzneria albida DSM 43870.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Kutzneria.
OX NCBI_TaxID=1449976 {ECO:0000313|EMBL:AHH98046.1, ECO:0000313|Proteomes:UP000019225};
RN [1] {ECO:0000313|EMBL:AHH98046.1, ECO:0000313|Proteomes:UP000019225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43870 {ECO:0000313|EMBL:AHH98046.1};
RX PubMed=25301375; DOI=10.1186/1471-2164-15-885;
RA Rebets Y., Tokovenko B., Lushchyk I., Ruckert C., Zaburannyi N.,
RA Bechthold A., Kalinowski J., Luzhetskyy A.;
RT "Complete genome sequence of producer of the glycopeptide antibiotic
RT Aculeximycin Kutzneria albida DSM 43870T, a representative of minor genus
RT of Pseudonocardiaceae.";
RL BMC Genomics 15:885-885(2014).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP007155; AHH98046.1; -; Genomic_DNA.
DR RefSeq; WP_025358089.1; NZ_CP007155.1.
DR AlphaFoldDB; W5WBW8; -.
DR STRING; 1449976.KALB_4684; -.
DR KEGG; kal:KALB_4684; -.
DR PATRIC; fig|1449976.3.peg.4717; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_0_11; -.
DR OrthoDB; 4959782at2; -.
DR Proteomes; UP000019225; Chromosome.
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; 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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000019225};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 5..116
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 193..320
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 383..529
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 580 AA; 62720 MW; 6EDBB3F413B1FBB4 CRC64;
MASQTVAEQF VDILVQAGVR RLYGVVGDSL NPVTDAVRRS SRIEWVQVRH EETAAFAAGA
EAQVTGRLTA CAGSCGPGNL HLINGLFDAH RSMAPVLALA AHIPSGEIGT GYFQETHPDR
LFAECSHYSE MISHPGQMPR VAQTAVQHAV GRSGVAVISM PGDVAGQSVP VRPGRSALVN
RRPTVRPGEA ELDELARLVD GAERITLFCG SGTAGAHAEV MALADRVKSP VGHALRGKEW
IQYDNPFDVG MSGLLGYGAA YEAMHECDLL LLLGTDFPYN AFLPEDVRIV QVDIRPEHLG
RRSRLDLGVW GDVAETLRCL TPKVRRRTDR SFLDRMLRKH SSALEHVVSA YTREVERHRP
IHPEYVASVL DEVAAEDAVF TVDTGMCNVW AARYLTPNGR RRIIGSFTHG SMANALPQAI
GAQAVDRGRQ VVTLSGDGGF SMLMGDFLTL VQYDLPVKVV LFNNSSLGMV DLEMMVAGMQ
PHATRYQGTD YAAIARAAGA HGIRVEDPHE VRRALEEALS HKGPALVDVV TDPNALSIPP
HITGEQMAGF AVATSKMVLN GGVGRMIQLA RANLRNIPRP
//
