GenomeNet

Database: UniProt
Entry: H1LG65_9LACO
LinkDB: H1LG65_9LACO
Original site: H1LG65_9LACO 
ID   H1LG65_9LACO            Unreviewed;       586 AA.
AC   H1LG65;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   SubName: Full=Pyruvate oxidase {ECO:0000313|EMBL:EHO51077.1};
GN   ORFNames=HMPREF9104_01591 {ECO:0000313|EMBL:EHO51077.1};
OS   Lentilactobacillus kisonensis F0435.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lentilactobacillus.
OX   NCBI_TaxID=797516 {ECO:0000313|EMBL:EHO51077.1, ECO:0000313|Proteomes:UP000005025};
RN   [1] {ECO:0000313|EMBL:EHO51077.1, ECO:0000313|Proteomes:UP000005025}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0435 {ECO:0000313|EMBL:EHO51077.1,
RC   ECO:0000313|Proteomes:UP000005025};
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:EHO51077.1}.
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; AGRJ01000152; EHO51077.1; -; Genomic_DNA.
DR   RefSeq; WP_008856766.1; NZ_JH591039.1.
DR   AlphaFoldDB; H1LG65; -.
DR   STRING; 797516.HMPREF9104_01591; -.
DR   PATRIC; fig|797516.3.peg.1414; -.
DR   HOGENOM; CLU_013748_3_0_9; -.
DR   OrthoDB; 4494979at2; -.
DR   Proteomes; UP000005025; Unassembled WGS sequence.
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:EHO51077.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005025};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          6..121
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          195..323
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          384..531
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   586 AA;  64220 MW;  745A08611C5DA969 CRC64;
     MVEKISGSDA VLKVLEQWGV KHIYGLPGGS FDSTMNAIHN QQDKITYIQV RHEEAGAIAA
     SATAKLTGKV GVCFGSAGPG AVHLLNGLYD AKSDGVPVVA LVAQVPTNRM NMDFFQAMDE
     EPIFDDVAVW NRTAMTAEAL PRMVDEAIRQ AYMKHGVSVL TIPKDLGWAQ IDDTYRPNVK
     SLQTPNYPIP DSTAISKAVQ LIKAAQAPMI YFGIGARNAV PELKQAAKKF KMPLVSSVLA
     KGILPDNYPA YLGSTGRVAP KPGVEVGFST DLILWVGNDV PFSIFLFNKH AKVIQIDIES
     EKLGKHRHND VSILADAKSA LEAIINAGDA RKPSPFYQAA LADKQNWEDW QDSFKDDSEL
     PIRPEPIFDV LNKTASGNAI FAVDVGNVNI NFERLLNMHD NQKWATSGIY ATMGFALPAS
     IAAKLTYPDR DVYSLSGDGG FAMLMEELMV QVKYGLHIVN IIFSNETLGF IQAEQTDDTH
     QPLSGVGLPA TNWAEVAKGM GAVSYTVRTK DDMQKAISAS KDTNKPVVID VKLTHAMPLT
     TQHMFIDPSW QDKNEVVNFV EKYDAQALKP FSDFLKEAEK RQPQHN
//
DBGET integrated database retrieval system