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Database: UniProt
Entry: A0A0N1L4K1_9SPHN
LinkDB: A0A0N1L4K1_9SPHN
Original site: A0A0N1L4K1_9SPHN 
ID   A0A0N1L4K1_9SPHN        Unreviewed;       569 AA.
AC   A0A0N1L4K1;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Pyruvate dehydrogenase {ECO:0000313|EMBL:KPF55811.1};
GN   ORFNames=IP65_07335 {ECO:0000313|EMBL:KPF55811.1};
OS   Novosphingobium sp. AAP1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=1523413 {ECO:0000313|EMBL:KPF55811.1, ECO:0000313|Proteomes:UP000037880};
RN   [1] {ECO:0000313|EMBL:KPF55811.1, ECO:0000313|Proteomes:UP000037880}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAP1 {ECO:0000313|EMBL:KPF55811.1,
RC   ECO:0000313|Proteomes:UP000037880};
RA   Zeng Y., Feng F., Liu Y., Koblizek M.;
RT   "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT   Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL   Submitted (AUG-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:KPF55811.1}.
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DR   EMBL; LJHO01000002; KPF55811.1; -; Genomic_DNA.
DR   RefSeq; WP_022677889.1; NZ_LJHO01000002.1.
DR   AlphaFoldDB; A0A0N1L4K1; -.
DR   STRING; 1523413.IP65_07335; -.
DR   PATRIC; fig|1523413.3.peg.2193; -.
DR   OrthoDB; 4494979at2; -.
DR   Proteomes; UP000037880; 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   GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
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:KPF55811.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037880};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          3..117
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          189..316
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          377..523
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   569 AA;  60485 MW;  4076EFF809862086 CRC64;
     MTTVADVIVK TLEAAGVERC YGIPGDTLNH ITDAIRTSAI RWVHVRHEEA GGFAAGADAM
     LTGKLAACAG SCGPGSLHFI NGLFESHRNR APVVLIASQI VRDELGFDFP QEVDFKAVYA
     SCSVFCEEIR TPGQARRMTA MAAQAALAKR GVAVLIVPAD VSSAKAADEP DFAVHRAAPV
     IRPADAELDR LAAALNSGRR IAIYGGSGCE QAHDAVVALA ERLRAPVVRT SRAKDFLEYD
     NPFDVGMTGI FGSEAGYHAL VSCDVLLLLG CDFAWRQFYP EKATILQVDL DGTHLGRRHP
     VDVGVVGDIA PTLDALLPRI TPCDDNAFLD ECLDHHRKAH AAQAKHATVG KGGAIHPQYL
     TQTISRHAAP DAVFTADGGS PMVWSLRHIA ATGQNRTVVS LTHGTMANAM PQALGAKAAF
     PDRQVIALSG DGGLAMLLGD LLTAVQEKLP IKVVVFNNGA LDFVEIEQKV EGLLDAYTEL
     VNPDFARVAE AIGFSGRRVE RAEDLEAAVQ AWLQEPGTAL LDVVTDRYEL VMPPAVKPGQ
     VAGMALYSAK AVLGGRGREV VGIIRNLIA
//
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