ID I4EVY2_9ACTN Unreviewed; 578 AA.
AC I4EVY2;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Pyruvate dehydrogenase/oxidase: FAD-and thiamine PPi-binding {ECO:0000313|EMBL:CCH87545.1};
DE EC=1.2.5.1 {ECO:0000313|EMBL:CCH87545.1};
GN Name=poxB {ECO:0000313|EMBL:CCH87545.1};
GN OrderedLocusNames=MODMU_2110 {ECO:0000313|EMBL:CCH87545.1};
OS Modestobacter marinus.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Modestobacter.
OX NCBI_TaxID=477641 {ECO:0000313|EMBL:CCH87545.1, ECO:0000313|Proteomes:UP000006461};
RN [1] {ECO:0000313|EMBL:CCH87545.1, ECO:0000313|Proteomes:UP000006461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BC501 {ECO:0000313|EMBL:CCH87545.1,
RC ECO:0000313|Proteomes:UP000006461};
RX PubMed=22887672; DOI=10.1128/JB.01029-12;
RA Normand P., Gury J., Pujic P., Chouaia B., Crotti E., Brusetti L.,
RA Daffonchio D., Vacherie B., Barbe V., Medigue C., Calteau A.,
RA Ghodhbane-Gtari F., Essoussi I., Nouioui I., Abbassi-Ghozzi I., Gtari M.;
RT "Genome Sequence of Radiation-Resistant Modestobacter marinus Strain BC501,
RT a Representative Actinobacterium That Thrives on Calcareous Stone
RT Surfaces.";
RL J. Bacteriol. 194:4773-4774(2012).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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; FO203431; CCH87545.1; -; Genomic_DNA.
DR RefSeq; WP_014740140.1; NC_017955.1.
DR AlphaFoldDB; I4EVY2; -.
DR STRING; 477641.MODMU_2110; -.
DR KEGG; mmar:MODMU_2110; -.
DR PATRIC; fig|477641.3.peg.2002; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_0_11; -.
DR OMA; YEATHEC; -.
DR OrthoDB; 4959782at2; -.
DR Proteomes; UP000006461; Chromosome.
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 CDD; cd02014; TPP_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 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 Oxidoreductase {ECO:0000313|EMBL:CCH87545.1};
KW Pyruvate {ECO:0000313|EMBL:CCH87545.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006461};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 5..116
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 191..318
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 381..526
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 578 AA; 61292 MW; C9B4DEB99326CB0E CRC64;
MAHPTVAAQL VEMLRDAGVE RIYGVVGDSL NPVVDAVRHT AGIEWVHVSN EEGGAFAAAA
EAQVTGKLAV CAGSCGPGNT HLLQGLFDAH RSGAPVLAIA SHIQSQEIGM AFFQETHPER
MFQECSYWCE VMTPKQMPHA LRVAVQTAVG KRGVSVVVLP GDLAAEESGG PTVPTAMVTT
PSPVRPAAGQ VQALADAINA ARTVTLFCGA GCAGAHDEVM ELAGTVLSPV GHALGGKEVI
QYDNPYDVGM NGLLGYGAAH KATHEADLLV LLGTDFPYTN FLPQARTAQV DADASHLGRR
TPLEVAVHGD VGETIRALLP LLERKTDRTF LDAMLRDHAH ALEKVVDAYT RKVEKMRPIH
PEYVAAQLDE LAADDAVFTV DTGMCNVWAA RYLSPNGRRR VIGSFRHGSM ANALPHAVGA
QFADRGRQVV SMSGDGGLAM LLGELITVRL HRLPVKIVLF NNASLGMVKL EMMVDGIPDF
ETDHEPTDFA AIAAGVGIPS YRVEDPAQVR ETLVRGLAEP GPVLMEFVTD ANALSIPPAI
TGEQVRGFAT TATKMVLGGG VGKMVDLARA NLRNVPRP
//
