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Database: UniProt
Entry: A0A126PHF9_9BACT
LinkDB: A0A126PHF9_9BACT
Original site: A0A126PHF9_9BACT 
ID   A0A126PHF9_9BACT        Unreviewed;       485 AA.
AC   A0A126PHF9;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Pyruvate oxidase {ECO:0000313|EMBL:AMJ67482.1};
GN   ORFNames=AXW84_20200 {ECO:0000313|EMBL:AMJ67482.1};
OS   Hymenobacter sp. PAMC 26628.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Hymenobacter.
OX   NCBI_TaxID=1484118 {ECO:0000313|EMBL:AMJ67482.1, ECO:0000313|Proteomes:UP000059956};
RN   [1] {ECO:0000313|EMBL:AMJ67482.1, ECO:0000313|Proteomes:UP000059956}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PAMC26628 {ECO:0000313|EMBL:AMJ67482.1,
RC   ECO:0000313|Proteomes:UP000059956};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP014304; AMJ67482.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A126PHF9; -.
DR   STRING; 1484118.AXW84_20200; -.
DR   KEGG; hyz:AXW84_20200; -.
DR   Proteomes; UP000059956; Chromosome.
DR   GO; GO:0003824; F:catalytic activity; 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; 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; 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   4: Predicted;
KW   Pyruvate {ECO:0000313|EMBL:AMJ67482.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000059956}.
FT   DOMAIN          4..117
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          276..423
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   485 AA;  51700 MW;  AF9332B03D041E32 CRC64;
     MANNGVDLLI ERLLAWGVGT VFSLPGDGIN GLYEALRTRQ DNIRLVQVRH EEATAFMAGG
     YAKFTGRLGV CLATSGCGGT HLLNGLYDAK YDGQPVLAIT GHTYHDLSGT FYQQDVDLVR
     VFTDVAAYNE RVMGPSHVEN VLDEAIRTAL GQRTVAHLSF PKGYQDWTLD DKARDPSNMA
     GYSAPTPMSP AGSAPAGPLQ AAADLINAGQ RVAILAGRGA LGARAEVLQL AELVGGPVVK
     ALLAERGTQD TIPTKPQVVP HTLSPLLAAD ASVTCDCGNN TTGAARHIQM QEHMLFSTSG
     LRATMGAGLP YAVAAALAYP GRQVEALAGD GGFTMLMGEL ATAVKYRLSI KVFIFHNNAL
     GQIKWEQIAM DGTPEFGVDL QSIDFAQYAQ ACGATGFTLT ETKDADRVIR AALAHDGPVV
     VDCHVGPNEP PMPPHVHHRA GHRLRQGPAM GRARHQRDCQ NVFRDQYHEA VATKDRSLLS
     VVPGL
//
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