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
//