ID A0A0U3PV08_9ACTN Unreviewed; 580 AA.
AC A0A0U3PV08;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Pyruvate dehydrogenase {ECO:0000313|EMBL:ALV32611.1};
GN ORFNames=AS200_11545 {ECO:0000313|EMBL:ALV32611.1};
OS Streptomyces sp. CdTB01.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1725411 {ECO:0000313|EMBL:ALV32611.1, ECO:0000313|Proteomes:UP000068029};
RN [1] {ECO:0000313|EMBL:ALV32611.1, ECO:0000313|Proteomes:UP000068029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CdTB01 {ECO:0000313|EMBL:ALV32611.1,
RC ECO:0000313|Proteomes:UP000068029};
RA Tian Y., Zhou G., Yang H., Lu X.;
RT "Complete genome sequence of the Streptomyces sp. strain CdTB01, a
RT bacterium tolerant to cadmium.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; CP013743; ALV32611.1; -; Genomic_DNA.
DR RefSeq; WP_058922293.1; NZ_CP013743.1.
DR AlphaFoldDB; A0A0U3PV08; -.
DR STRING; 1725411.AS200_11545; -.
DR KEGG; scx:AS200_11545; -.
DR OrthoDB; 4959782at2; -.
DR Proteomes; UP000068029; 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 Pyruvate {ECO:0000313|EMBL:ALV32611.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000068029};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 5..120
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 192..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; 62498 MW; C3723C27E43360CC CRC64;
MAKQNVAEQF VDTLVRAGVK RLYGVVGDSL NPVVDAVRRN AAIDWVHVRH EETAAFAAGA
EAQITGKLAA CAGSCGPGNL HLINGLYDAH RSMAPVLALA SHIPSSEIGL GYFQETHPDQ
LFRECSHYSE LISSPQQMPR LLQTAIQHAV GRSGVAVVSL PGDIADQPAP ERAAQSALVT
SRPTVRPGDA EIDRLADLID RAEKVTLFCG SGTAGAHAEV MEFAGKIKSP VGHALRGKEW
IQYDNPYDVG MSGLLGYGAA YEATHECDLL ILLGTDFPYN AFLPDDVTIV QVDVRPEHLG
RRSKLDLAVW GDVRETLRCL IPRVKEKTNR RFLDRMLKKH ADALEGVVKA YTRKVDKHVP
IHPEYVASVL DELADDDAVF TVDTGMCNVW AARYISPNGR RRVIGSFSHG SMANALPMAI
GAQFTDRGRQ VVSMSGDGGF SMLMGDFLTL VQYDLPVKVV LFNNSSLGMV ELEMLVAGLP
SYGTTNKNPD FAAVARACGA HGVRVEKPKD LAGALKSAFK HKGPALVDVV TDPNALSIPP
KISAEMVTGF ALSASKIVLD GGVGRMLQMA RSNLRNVPRP
//
