ID A0A101NUB1_9ACTN Unreviewed; 579 AA.
AC A0A101NUB1;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Pyruvate dehydrogenase {ECO:0000313|EMBL:KUM99508.1};
GN ORFNames=AQI95_39010 {ECO:0000313|EMBL:KUM99508.1};
OS Streptomyces yokosukanensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=67386 {ECO:0000313|EMBL:KUM99508.1, ECO:0000313|Proteomes:UP000053127};
RN [1] {ECO:0000313|EMBL:KUM99508.1, ECO:0000313|Proteomes:UP000053127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40224 {ECO:0000313|EMBL:KUM99508.1,
RC ECO:0000313|Proteomes:UP000053127};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces yokosukanensis DSM 40224, type
RT strain for the species Streptomyces yokosukanensis.";
RL Submitted (OCT-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:KUM99508.1}.
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DR EMBL; LMWN01000063; KUM99508.1; -; Genomic_DNA.
DR RefSeq; WP_067135417.1; NZ_KQ948229.1.
DR AlphaFoldDB; A0A101NUB1; -.
DR STRING; 67386.AQI95_39010; -.
DR OrthoDB; 4959782at2; -.
DR Proteomes; UP000053127; 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; 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:KUM99508.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053127};
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 192..318
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 382..527
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 579 AA; 62249 MW; B2488AC0BDCC1100 CRC64;
MGKRTVAQQL VDVLRQAGVS RIYGVVGDSL NPVVDAVRRT KGIEWVHVHN EEAAAFAAAA
EAQLTGRLAV CAGSSGPGNT HLIQGLYDAH RSGAPVLALA SHIPSHQIGT NYFQETHPER
LFAECSDYCE LVSTPDQMPR VLRIAMQRAV GHSDVSVLVL PGDLAAAAAT VPTGTSPLVS
SAGRVTPDES QVQALADRLN SARTVMLFAG AGVRDAHAEV MRLAERLKAP IGHTLRGKEW
IQYDNPYDVG MSGLLGYGAC FDTMQDADLV LLLGTDFPYD DFLPQQRTVQ IDHDLGRLGR
RTVLDLGVHG DVRETLRAVL PLVRDKENRS FLDAGLRKHA QSLETVVSAY THDVDRRIPI
HPEFPAAVLD ELADDDAVFT VDTGMCNVWA ARYITPNGRR RILGSFLHGT MANALPHAIG
AQMADRSRQV ISMSGDGGLA MLLGELLTVK QHNLPIKTVL FNNSSLGMVK LEMLVDGLPE
HETDHEPVDF SAIAAAVGIH AVRIERPGEV RDGLKEALAF PGPCLVELVT DANALAIPPR
ISAEQIKGFA LAAGRTVLAG GVGQMLDVAR ANLRNIPRP
//