ID A0A1V4E7L0_9ACTN Unreviewed; 588 AA.
AC A0A1V4E7L0;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Pyruvate oxidase {ECO:0000313|EMBL:OPG08922.1};
GN ORFNames=B1L11_27210 {ECO:0000313|EMBL:OPG08922.1};
OS Microbispora sp. GKU 823.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Microbispora.
OX NCBI_TaxID=1652100 {ECO:0000313|EMBL:OPG08922.1, ECO:0000313|Proteomes:UP000190255};
RN [1] {ECO:0000313|EMBL:OPG08922.1, ECO:0000313|Proteomes:UP000190255}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GKU 823 {ECO:0000313|EMBL:OPG08922.1,
RC ECO:0000313|Proteomes:UP000190255};
RA Kruasuwan W.;
RT "Draft genome sequence of sugarcane root-associated plant growth promoting
RT Microbispora sp. GKU 823.";
RL Submitted (FEB-2017) 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:OPG08922.1}.
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; MWJN01000058; OPG08922.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4E7L0; -.
DR OrthoDB; 4959782at2; -.
DR Proteomes; UP000190255; 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:OPG08922.1};
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; 63928 MW; 0E2350B0086715BA CRC64;
MTEIVGESLA RRLVEWGVDT IFGLPGDGIN GLVEGFRRHR EKLRFILVHH EEAAAFMATG
YAKATGRLGV CAATSGPGAI HLLNGLYDAK LDHVPVLALT GMQETSVLGT HYQQEVHLDR
VYQDLAAYNL MITNPQQMPG VVDLAVRNAL AKRTVSHLTF PNDIQVAPAS EDPYRHVGPG
SPPASLPTCA LPPLRPVEED LTRAAEVLRQ GERIAMLVGV GARHAREEVL AVAEKLASPI
VKTLPGKFVV PDDHPLTTGG LGLLGTAPSE ELMEECDTLF MVGTSFPYAK YLPPDGQARV
VQIDADPTLL GIRRPTEAPV AADARLALQA LLPMLEPAKD RSFLEKYQRK MDAWREEMKA
LQDPSRDPIA PQYLMACVDE AASGDAILTC DSGTIATWAA RHWTIRGGRE FYLSGNLATM
APGLPYAIGM QHAFPGRQVI AFVGDGGFAM LMADFLTAVR HDLPIKVVIN NNNSYGQILW
EQIILGYPEY AVRHRQPEAD FSAWARACGA YGAKIKDPKD LPGAIREALA HDGPALVDCD
VNPNEPPMPG KVKYEQAKHF TEAFLRGQPH KAGVLATVAR DKINQLLS
//
