ID A0A0W0WW81_9GAMM Unreviewed; 577 AA.
AC A0A0W0WW81;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Pyruvate dehydrogenase {ECO:0000313|EMBL:KTD36516.1};
DE EC=1.2.5.1 {ECO:0000313|EMBL:KTD36516.1};
GN Name=poxB_2 {ECO:0000313|EMBL:KTD36516.1};
GN ORFNames=Lnau_1500 {ECO:0000313|EMBL:KTD36516.1};
OS Legionella nautarum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=45070 {ECO:0000313|EMBL:KTD36516.1, ECO:0000313|Proteomes:UP000054725};
RN [1] {ECO:0000313|EMBL:KTD36516.1, ECO:0000313|Proteomes:UP000054725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49506 {ECO:0000313|EMBL:KTD36516.1,
RC ECO:0000313|Proteomes:UP000054725};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-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:KTD36516.1}.
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DR EMBL; LNYO01000013; KTD36516.1; -; Genomic_DNA.
DR RefSeq; WP_058504503.1; NZ_LNYO01000013.1.
DR AlphaFoldDB; A0A0W0WW81; -.
DR STRING; 45070.Lnau_1500; -.
DR PATRIC; fig|45070.6.peg.1570; -.
DR OrthoDB; 9785953at2; -.
DR Proteomes; UP000054725; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0052737; F:pyruvate dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid 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 Oxidoreductase {ECO:0000313|EMBL:KTD36516.1};
KW Pyruvate {ECO:0000313|EMBL:KTD36516.1};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..114
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 577 AA; 63285 MW; 245DBD48A15FE43E CRC64;
MALTTAEQMV ELLKSAGIRR IYGVTGDSLN FLNDALRRDG TIEWIHVRHE EAGAFAAMAE
GVLGGLGCCA GSSGPGHVHL LNGFYDAHRW GAPVLALAST IISQDYGSES FQSTDLSMFD
GCSYYNEIAQ TPKQLPRMVQ QAMQYAWNRK GVGVCAFPGD LMMQQAYEGI PLATLYRPDA
VTCPSERELN DLAALINNTE KVSIYAGIGC TNARAEVLKL AEKLKAPIAY TLKAKMVMEH
ENPFVVGMTG LLGSSAGARA ITECKVLLML GSDFPWREFL DGEVKIVQID TKPERLGRRV
ALHRGLTGDI NSTLKALLPL VQIKNDDTFL KDCLKDYDAV QKLQHHHAEE AGQENLIKPE
FLATKIDELA DKDAIFTADT GMCTVWAARY IRSTGKRSLM GSFSHGSMAN AMPQAIGAAL
HSPSRQVVAF CGDGGISMLL GDLMTIAQYK LPIKLIVFNN RTLGMVELEM QVAGLPNWQT
KMVNPNFAQL AEACGIRGYS IKNPEELEPT LREAFSYEAA VLVEVFTNPD VPVLPPHTSI
GVITRYVESE VKLTKAGRFK EAWLSLKTSI KYVRDLW
//
