ID A0A367FE85_9ACTN Unreviewed; 588 AA.
AC A0A367FE85;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Pyruvate oxidase {ECO:0000313|EMBL:RCG28634.1};
GN ORFNames=DQ384_23110 {ECO:0000313|EMBL:RCG28634.1};
OS Sphaerisporangium album.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Sphaerisporangium.
OX NCBI_TaxID=509200 {ECO:0000313|EMBL:RCG28634.1, ECO:0000313|Proteomes:UP000253094};
RN [1] {ECO:0000313|EMBL:RCG28634.1, ECO:0000313|Proteomes:UP000253094}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCTCC AA 208026 {ECO:0000313|EMBL:RCG28634.1,
RC ECO:0000313|Proteomes:UP000253094};
RA Li L.;
RT "Sphaerisporangium craniellae sp. nov., isolated from a marine sponge in
RT the South China Sea.";
RL Submitted (JUN-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:RCG28634.1}.
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DR EMBL; QOIL01000013; RCG28634.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367FE85; -.
DR OrthoDB; 4959782at2; -.
DR Proteomes; UP000253094; 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:RCG28634.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000253094};
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 201..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"
FT REGION 178..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 588 AA; 63651 MW; 152A3333794C2330 CRC64;
MTEIVGESVA RRLVEWGVDT IFGLPGDGIN GLMEGFRRHR ARLRFVLVHH EEAAAFMATG
YAKATGRLGV CAATSGPGAI HLMNGLYDAK LDHAPVLALT GMQETSVLGT YYQQEVHLDR
LFQDLASYNL MVTNPQQVPG VVDLAVRDAL SKRTVAHLSF PNDIQVAPVT EDPYRHVGPG
APSRSVPVYS RPPLPPAEED LDRAADTLNA GRKVAVFAGA GARDARAEVL AVAERLASPI
VKTLPGKPVV PDDHPMTTGV LGLLGTKPSE EIMRECDTLL MVGASFPYAT FLPEPGAARV
VQIDADPSLI GLRLPVEAPV AGDARLALER LLPRLKGGAD PSFLRKYQRK AQAWRADMKA
LEDPSRHPIA PQYLMGCVDQ AATGDAILTC DSGTIATWAA RHWTIRGGRD FYLSGNLATM
APGLPYAIGM QHAFPGRQVI AFVGDGGFAM LMAEFLTAVR NQLPIKVVIC NNNAYAQILW
EQIVLGYPEY SVRHRQPEAD FSAWARACGA YGAKVDSPHE LPRAIRAALA HDGPALVDCD
VNPNEPPMPG KVTYEQAKAF TEAFLRGQPH KREILVTVAR DKINELRS
//
