ID A0A081PDQ0_9SPHI Unreviewed; 574 AA.
AC A0A081PDQ0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Pyruvate dehydrogenase {ECO:0000313|EMBL:KEQ28823.1};
GN ORFNames=N180_18445 {ECO:0000313|EMBL:KEQ28823.1};
OS Pedobacter antarcticus 4BY.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1358423 {ECO:0000313|EMBL:KEQ28823.1, ECO:0000313|Proteomes:UP000028007};
RN [1] {ECO:0000313|EMBL:KEQ28823.1, ECO:0000313|Proteomes:UP000028007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4BY {ECO:0000313|EMBL:KEQ28823.1,
RC ECO:0000313|Proteomes:UP000028007};
RA Shivaji S., Ray M.K., Rao N.S., Saiserr L., Jagannadham M.V., Kumar G.S.,
RA Reddy G., Bhargava P.M.;
RT "Sphingobacterium antarcticus sp. nov. a Psychrotrophic Bacterium from the
RT Soils of Schirmacher Oasis, Antarctica.";
RL Int. J. Syst. Bacteriol. 42:102-106(1992).
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:KEQ28823.1}.
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DR EMBL; JNFF01000103; KEQ28823.1; -; Genomic_DNA.
DR RefSeq; WP_037443361.1; NZ_JNFF01000103.1.
DR AlphaFoldDB; A0A081PDQ0; -.
DR eggNOG; COG0028; Bacteria.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000028007; 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:KEQ28823.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000028007};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..115
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 192..319
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 380..526
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 574 AA; 62426 MW; 742689CDBADFA41E CRC64;
MTKTVAAQFV EILEQAGVTA VHGVVGDSLN GIVEEIRQSK TIKWVHYRHE EAAAFAAGAE
AQITGKLAVC AGSCGPGNMH LINGLYDAHR SNAPVLAIAA HIPSEQIGTA YFQETRPESL
FRECSYYCET IASARQMPRV LQIAMQHAVG QSGVAVVSIS GDVAMEKAPS DQLEHQIFHN
KPVIRPADDD LRKLAALINQ HKKITLLCGA GCAGAHQELL SLAAAVKSPI VHALRGKEHV
QYDNPYDVGM TGLIGLTSGY QAVEDCELLI MLGTDFPYKE WYPPKAKIVQ LDIRPERLGR
RCKLEMGLVG SVKETLEALL PLIDHAQDSS FLHKSQERYQ DNRKNLMKHA QAVEGEAIHP
EYLTRLLSEQ ASTNAVFTAD VGTPSVWAAR YIDMTAGRRL IGSFNHGSMA SAMPQAIGAQ
LTDLNRQVIS LSGDGGFAMM MGDILTIHQY DLPVKLVIYN NSSLGFVAME MKVIGMPPFG
TDLKNPDFAK MAEAIGIRGI RVEKAEDLEA AVAAALAHPG PVVLDVVVNQ TELSMPPKID
LEQAKGFGIY MLKQTLKGDG KEVWDTIRSN FLSK
//