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Database: UniProt
Entry: C9A5L7_ENTCA
LinkDB: C9A5L7_ENTCA
Original site: C9A5L7_ENTCA 
ID   C9A5L7_ENTCA            Unreviewed;       577 AA.
AC   C9A5L7;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 2.
DT   24-JAN-2024, entry version 52.
DE   SubName: Full=Pyruvate oxidase {ECO:0000313|EMBL:EEV39921.2};
GN   ORFNames=ECBG_02190 {ECO:0000313|EMBL:EEV39921.2};
OS   Enterococcus casseliflavus EC20.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=565655 {ECO:0000313|EMBL:EEV39921.2, ECO:0000313|Proteomes:UP000012675};
RN   [1] {ECO:0000313|EMBL:EEV39921.2, ECO:0000313|Proteomes:UP000012675}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EC20 {ECO:0000313|EMBL:EEV39921.2,
RC   ECO:0000313|Proteomes:UP000012675};
RG   The Broad Institute Genome Sequencing Platform;
RA   Feldgarden M., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L.,
RA   Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C.,
RA   Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA   Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T.,
RA   White J., Yandava C., Gilmore M., Manson J., Palmer K., Carniol K.,
RA   Lander E., Nusbaum C., Galagan J., Birren B.;
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EEV39921.2, ECO:0000313|Proteomes:UP000012675}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EC20 {ECO:0000313|EMBL:EEV39921.2,
RC   ECO:0000313|Proteomes:UP000012675};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Russ C., Feldgarden M., Gilmore M., Manson J., Palmer K., Carniol K.,
RA   Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Enterococcus casseliflavus EC20 (899205).";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; CP004856; EEV39921.2; -; Genomic_DNA.
DR   RefSeq; WP_015509859.1; NZ_AKCC01000001.1.
DR   AlphaFoldDB; C9A5L7; -.
DR   GeneID; 15142397; -.
DR   KEGG; ecas:ECBG_02190; -.
DR   eggNOG; COG0028; Bacteria.
DR   HOGENOM; CLU_013748_3_0_9; -.
DR   Proteomes; UP000012675; Chromosome.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0047112; F:pyruvate oxidase 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; 1.10.10.940; -; 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; IPR014092; Pyruvate_oxidase.
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   NCBIfam; TIGR02720; pyruv_oxi_spxB; 1.
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:EEV39921.2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000012675};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          5..120
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          194..321
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          382..528
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   577 AA;  63240 MW;  F1DDEE002C8360D0 CRC64;
     MTKINAGTAM IKVFEAWGID HIYGIPGGSF NSTMDALYHE RQSVKYIQVR HEEAGALAAA
     ADAKLTGKVG AVFGSAGPGA THLINGLYDA QMDNVPVVAL LGQVASSSMN YNDFQEMNEN
     PMFADVSIYN RTVMSPESLP HVVDEAIKAA YKFKGVAVVT IPVDYGFAEI DEQEIATAKN
     HKTGVLQPDE EGLQAALPYF EQAKKPVLYI GQGLFGHFDA IDAFSKHFSM PIAASVLAKG
     IVPDLYENFL GFAGRVATKP ANEALAEADL IVFVGSDFPF GRRFFNPGAN FIQVDIDASK
     FGRRHQTDVS VLGDGATALR KWTEMAAPRP ADAWLKANQE NCRNWHEWRH RFDHDSQEPL
     RPEPVYREIN RIAAPDALFV TDVGNVTIHS IRHLEMTGEQ RFTTSGWFAT MGNGVPGGIA
     AQLSYPNRQV FTFSGDGGFA MQMQDIITQV KYDLPIINVV FSNDSFGFIE AEQEDTEQTK
     FGVQLAGADF GKVGEALGAK GFTVTKEEEL ASVFTQAKES HGPVVIDVKI ANERPLPVEE
     LKLDPNRFSA EEIAAFKAKY QVHDLPALSE LYVDSQE
//
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