ID A0A1Q4UUA7_9PROT Unreviewed; 576 AA.
AC A0A1Q4UUA7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Pyruvate dehydrogenase {ECO:0000313|EMBL:OKH89160.1};
GN ORFNames=LF95_03695 {ECO:0000313|EMBL:OKH89160.1};
OS Thalassospira sp. TSL5-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Thalassospiraceae; Thalassospira.
OX NCBI_TaxID=1544451 {ECO:0000313|EMBL:OKH89160.1, ECO:0000313|Proteomes:UP000186302};
RN [1] {ECO:0000313|EMBL:OKH89160.1, ECO:0000313|Proteomes:UP000186302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSL5-1 {ECO:0000313|EMBL:OKH89160.1,
RC ECO:0000313|Proteomes:UP000186302};
RA Zhou H., Wang H.;
RT "Genome sequencing of Thalassospira sp. TSL5-1.";
RL Submitted (SEP-2014) 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:OKH89160.1}.
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DR EMBL; JRJD01000001; OKH89160.1; -; Genomic_DNA.
DR RefSeq; WP_073953696.1; NZ_KV880637.1.
DR AlphaFoldDB; A0A1Q4UUA7; -.
DR STRING; 1544451.LF95_03695; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000186302; 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:OKH89160.1};
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 190..317
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 379..525
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 576 AA; 62216 MW; 17C916911A573534 CRC64;
MSRTIAETIV DMLADAGVKR LYAVTGDSLN LLNDAIRRDG RIDWIHVRHE EAGAYAAMAE
GVLGGLGCCA GSSGPGHVHL INGLYDAHRW GAPVIALPST IDRADYGMES FQETDLGMFD
GCSWYNELAQ IPEQAPRMLQ QALQNAITRK GVGVFGYSGD ILPLDLPETA IASPVYRPGT
VLRPDDGALD DLAKMLTGAK RPFIYGGMGC DAARDQVREL ARRLNAPVGW TLKGKMALEH
DNPNGVGMTG FIGGKACADA IARADVVLLL GTDFPWKDFL QTDARIAQVL THGERLGRRT
HVKMGLVGDV RATLDALLPR LETRADDSFL QDRLKAVKSD RDNMVHHAQK PGKKGEISPE
YLTTAISRLA DDDAIFTADT GMTTVWAARY IESTGKRSFM GSFSHGSMAN AMPQAIGAAL
AGNGRQTIAL CGDGGISMLL GDLATIGQYQ LPVKMVVYNN SSLGMVEIEM QLAGIPNFQT
EMVNPDFAAI AEACGIRGVQ VEDPEKLDDA LEMAMNHEGP VLLDVKTDRY AVAMPPHTSP
EQLGKYALSE AKMVLNGRGT EVIEQLKTNF KYLRDL
//
