ID A0A0X3WL54_9ACTN Unreviewed; 580 AA.
AC A0A0X3WL54;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Pyruvate dehydrogenase {ECO:0000313|EMBL:KUL57579.1};
GN ORFNames=ADL30_11405 {ECO:0000313|EMBL:KUL57579.1};
OS Streptomyces sp. NRRL S-1521.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1609100 {ECO:0000313|EMBL:KUL57579.1, ECO:0000313|Proteomes:UP000053420};
RN [1] {ECO:0000313|EMBL:KUL57579.1, ECO:0000313|Proteomes:UP000053420}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL S-1521 {ECO:0000313|EMBL:KUL57579.1,
RC ECO:0000313|Proteomes:UP000053420};
RA Gilbert D.G.;
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:KUL57579.1}.
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DR EMBL; LLZK01000133; KUL57579.1; -; Genomic_DNA.
DR RefSeq; WP_062773340.1; NZ_LLZK01000133.1.
DR AlphaFoldDB; A0A0X3WL54; -.
DR Proteomes; UP000053420; 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:KUL57579.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053420};
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..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; 62386 MW; 045E598B6E5C63AC CRC64;
MAKQNIAEQF VDILVRAGVR RLYGVVGDSL NPVVDAIRRT PDIDWIQVRH EETAAFAAGA
EAQITGRLAA CAGSCGPGNL HLINGLYDAH RSMAPVLALA SHIPSSEIGL NFFQETHPDR
LFQECSHYSE LISSPKQMPR LLQTAIQNAV GQSGVSVVAL PGDVAGEPAP AKAAETALVT
SRPSVRPGDA EIERLTKMID AADKVTLFCG SGTAGAHAEV MEFAEKIKSP VGHALRGKEF
IQYDNPFDVG MSGLLGYGAA YEATHECDLL ILLGTDFPYN AFLPDDVKIA QVDVRPEHLG
RRSKLDLAVW GDVRETLRCL TPRVSPKTNR KFLDKMLKKH ADALEGVVKA YTRKVDKHVP
IHPEYVASVL DEVAADDAVF TVDTGMCNVW AARYLTPNGK RRIIGSFSHG SMANALPQAI
GAQFVDRRRQ VVSMSGDGGF SMLMGDFLTL VQHDLPVKVV LFNNSSLGMV ELEMLVAGLP
SYGTDNHNPD FAAIARAAGA YGVRVEKPKQ LAGALKDAFS HKGPALVDVV TDPNALSIPP
KISSDMVTGF ALSAGKIVLD GGVGRMLQMA RSNLRNMPRP
//
