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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//