ID G9ZSY5_9LACO Unreviewed; 581 AA.
AC G9ZSY5;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Putative pyruvate oxidase {ECO:0000313|EMBL:EHL95702.1};
GN ORFNames=HMPREF9103_02902 {ECO:0000313|EMBL:EHL95702.1};
OS Lentilactobacillus parafarraginis F0439.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lentilactobacillus.
OX NCBI_TaxID=797515 {ECO:0000313|EMBL:EHL95702.1, ECO:0000313|Proteomes:UP000004625};
RN [1] {ECO:0000313|EMBL:EHL95702.1, ECO:0000313|Proteomes:UP000004625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0439 {ECO:0000313|EMBL:EHL95702.1,
RC ECO:0000313|Proteomes:UP000004625};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2011) 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:EHL95702.1}.
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DR EMBL; AGEY01000197; EHL95702.1; -; Genomic_DNA.
DR RefSeq; WP_008215058.1; NZ_JH415059.1.
DR AlphaFoldDB; G9ZSY5; -.
DR STRING; 797515.HMPREF9103_02902; -.
DR PATRIC; fig|797515.3.peg.2648; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_0_9; -.
DR Proteomes; UP000004625; 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:EHL95702.1};
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..322
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 382..532
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 581 AA; 63663 MW; 3174FA3CED10D166 CRC64;
MATITAGHAL AKVLVSWDID HIYGITADSI NNTVDGLYQE RDHLKYIQVR HEEVGSLAAT
ADAKLTGKVG VSFGSAGPGA THMFNGLYDA KMDHAPVVAI IGQSATPIMN TYFFQEMDQD
PMFSDVTDFH KQVTNPDQIP YVMDEAIRYA YQTKGPAVVI IPDNLSGETI DFEPYHTAKV
LKSATTPAVD DSAVDAVYEL ISKAKHPVLW VGLGMKDARE EVVHFSEKFS VPVLSTAPST
GIMPTDHPNF MGSRGRLGTK PAFEVTQAAD LIILAGTNYP FSRFLPKGIK FVQINNSVAD
LGKQRDIDLT VLADAKPFFA KLNQKGAAMP ATPFLKAAQQ DKKNWDAWLN KVADDDQSGL
NPEAVIRAIK DHSDDDAVFG LDVGNNLMWS IRQLPFNHDQ KLSMSAWFGT MGYALPASIA
AKLSYPDRQV FSISGDGGFS MVMQDLLTQV QYQLPIVNVV LENKAFGYIQ HEKITANQEP
YGIHFIGADW AGFADSMGAI GIKVTDRESL AQAFTKVQDL QAAGNTKPIL IDAKVKNQDP
VDTSFMPIDP EQFDRATIDT YTAQSNLFDQ PPFSELLKNE S
//
