ID I9AJK0_LACPE Unreviewed; 585 AA.
AC I9AJK0;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=Pyruvate oxidase {ECO:0000313|EMBL:EIW13117.1};
DE EC=1.2.3.3 {ECO:0000313|EMBL:EIW13117.1};
GN Name=pox3 {ECO:0000313|EMBL:EIW13117.1};
GN ORFNames=KCA1_2145 {ECO:0000313|EMBL:EIW13117.1};
OS Lactiplantibacillus pentosus KCA1.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=1136177 {ECO:0000313|EMBL:EIW13117.1};
RN [1] {ECO:0000313|EMBL:EIW13117.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCA1 {ECO:0000313|EMBL:EIW13117.1};
RX PubMed=23527145;
RA Anukam K.C., Macklaim J.M., Gloor G.B., Reid G., Boekhorst J., Renckens B.,
RA van Hijum S.A., Siezen R.J.;
RT "Genome Sequence of Lactobacillus pentosus KCA1: Vaginal Isolate from a
RT Healthy Premenopausal Woman.";
RL PLoS ONE 8:E59239-E59239(2013).
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:EIW13117.1}.
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DR EMBL; AKAO01000068; EIW13117.1; -; Genomic_DNA.
DR RefSeq; WP_003639362.1; NZ_CM001538.1.
DR AlphaFoldDB; I9AJK0; -.
DR PATRIC; fig|1136177.4.peg.2082; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_0_9; -.
DR Proteomes; UP000005826; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0047112; F:pyruvate oxidase activity; IEA:UniProtKB-EC.
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 Oxidoreductase {ECO:0000313|EMBL:EIW13117.1};
KW Pyruvate {ECO:0000313|EMBL:EIW13117.1};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 8..118
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 196..324
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 386..534
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 585 AA; 64329 MW; 5EDC80D8330CCDB0 CRC64;
MAKMIEASVA MLKVLEAWDI KQIYGYAGGS FNSTMHALDV EKSRLQYVQV RHEQVGALAA
AADAKLTGKI GVAFGSAGPG AVNLLNGLYD AKEDHVPVLA LVGQVAHTNM NYDYFQEFAE
EPIFSDVAVF NRTVMTPESL PYVVDKAIRT AYRENGVAVV TIPNDFGYVE IPDENYDSAS
VPAKLRGVPE IEDDQVKTVL DMIKAAKYPV FHVGQGTRGA TEDMMALAER LQVPIIITGL
AKGVIPDSFD GNMGSAYRAA SKAADELMGI TDLVVSVGAD YSFAQIMYTT HDFKYVQIEL
DPGKFGRHHH LDFGVNGDAK VFIKRALALS EQAAPSPYYQ AAKADMADWK QYLKKLSERT
TDPLEYEQVY QEINRVAEDD AVFSMDVGDN TINSFRFLKM NPKQKLLTSA LFATMGAGVP
GAIAAKMSYP DRQAFNIAGD GAFSMVMQDL LTEVKYHLPI FNIVTSNQTL NFIKSEQEDV
PQPYYGIDLL DADFAKIAEG MGVKGIRVDH FDQLHDAFET AMAELKAGRP VLIDAKITDK
RGLPVEILDV DPAKTSDASV SAFKEKYDAN ELKPLSSYFK EFKVQ
//