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Database: UniProt
Entry: A0A366ZRC6_9ACTN
LinkDB: A0A366ZRC6_9ACTN
Original site: A0A366ZRC6_9ACTN 
ID   A0A366ZRC6_9ACTN        Unreviewed;       588 AA.
AC   A0A366ZRC6;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Pyruvate oxidase {ECO:0000313|EMBL:RBY78881.1};
GN   ORFNames=DQ238_10790 {ECO:0000313|EMBL:RBY78881.1};
OS   Geodermatophilus sp. TF02-6.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Geodermatophilus.
OX   NCBI_TaxID=2250575 {ECO:0000313|EMBL:RBY78881.1, ECO:0000313|Proteomes:UP000253027};
RN   [1] {ECO:0000313|EMBL:RBY78881.1, ECO:0000313|Proteomes:UP000253027}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TF02-6 {ECO:0000313|EMBL:RBY78881.1,
RC   ECO:0000313|Proteomes:UP000253027};
RA   Ennis N., Dharumadurai D., Sevigny J., Hall J., Simposon S., Morris K.,
RA   Thomas W.K., Tisa L.S.;
RT   "Genome Sequence of Geodermatophilus sp. TF02-6.";
RL   Submitted (JUL-2018) 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:RBY78881.1}.
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DR   EMBL; QOHF01000010; RBY78881.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A366ZRC6; -.
DR   OrthoDB; 4959782at2; -.
DR   Proteomes; UP000253027; 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; 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   Pyruvate {ECO:0000313|EMBL:RBY78881.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000253027};
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          202..331
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          391..539
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   588 AA;  63046 MW;  2E88FAD5C0072949 CRC64;
     MDEIVGESLA KRLVAWGVDT VFGLPGDGIN GLMEGFRRTS DQLRFVLVHH EEAAAFMATG
     YAKATGKLGV CVATSGPGAI HLLNGLYDAK LDHVPVLALT GMQATNVLGT NYQQEVHLDR
     LYQDLAAYNL MVTSPLQMPA VVDLAIRNAL AKRTVAHLTF PNDLQVAPVT EDPYRHVGPG
     EAPASDPNIS VPQLPPDPAD LARAAEVLNA GAKVAMLVGV GAKHAREEVL AVADALGAPI
     IKTLPGKQVV PDDHPLTTGG LGLLGTRPSD EVVAGCDTLL MVGTSYPYAS YLPKPGSVRA
     VQIDADPTLL GMRLPVEAPV TADAKKALAA LLPMLTRAED RSFLQGAQED MAKWRREMES
     LEDADRDPIA PQYLMGVIDD VATDDAILTC DSGTIATWAA RHWTIRGGRE FYLSGNLATM
     APGLPYAIGI QRAFPGRQVV AFVGDGGFAM LMADFITAVR EELPIKVVIN NNNAYGQILW
     EQIELGYPEY AVRHLQPETD FSTWARGCGA HGEKVKDPAR VADAVREAFA SPGPALVDVD
     VNPNEPPIPG TIEFKQAKAF TEAFLRGQPH KAETVTTIVK DKIREWTS
//
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