POXB_LACPL
ID POXB_LACPL Reviewed; 603 AA.
AC P37063; F9ULE3;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 25-MAR-2003, sequence version 3.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Pyruvate oxidase;
DE EC=1.2.3.3;
DE AltName: Full=Pyruvic oxidase;
DE Short=POX;
GN Name=pox5; OrderedLocusNames=lp_3589;
OS Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
OS (Lactobacillus plantarum).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=220668;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P.,
RA Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J.,
RA Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M.,
RA Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M.,
RA Siezen R.J.;
RT "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1;
RX PubMed=22156394; DOI=10.1128/jb.06275-11;
RA Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M.,
RA Kleerebezem M., van Hijum S.A.;
RT "Complete resequencing and reannotation of the Lactobacillus plantarum
RT WCFS1 genome.";
RL J. Bacteriol. 194:195-196(2012).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.5 AND 2.1 ANGSTROMS) OF WILD-TYPE AND MUTANT.
RX PubMed=8145244; DOI=10.1006/jmbi.1994.1233;
RA Muller Y.A., Schumacher G., Rudolph R., Schulz G.E.;
RT "The refined structures of a stabilized mutant and of wild-type pyruvate
RT oxidase from Lactobacillus plantarum.";
RL J. Mol. Biol. 237:315-335(1994).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX PubMed=8438155; DOI=10.1126/science.8438155;
RA Muller Y.A., Schulz G.E.;
RT "Structure of the thiamine- and flavin-dependent enzyme pyruvate oxidase.";
RL Science 259:965-967(1993).
CC -!- FUNCTION: Important for the aerobic growth. Decarboxylates pyruvate in
CC four steps. The energy released is partially stored in acetyl
CC phosphate.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + O2 + phosphate + pyruvate = acetyl phosphate + CO2 +
CC H2O2; Xref=Rhea:RHEA:20848, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:22191, ChEBI:CHEBI:43474; EC=1.2.3.3;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Note=Binds 1 FAD per subunit.;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Note=Binds 1 Mg(2+) ion per subunit.;
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Note=Binds 1 thiamine pyrophosphate per subunit.;
CC -!- SUBUNIT: Homotetramer.
CC -!- DOMAIN: Each monomer is divided into three domains, each of which
CC contains a six-stranded parallel beta sheet surrounded by alpha
CC helices.
CC -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR EMBL; AL935263; CCC80550.1; -; Genomic_DNA.
DR RefSeq; WP_003646223.1; NC_004567.2.
DR RefSeq; YP_004891064.1; NC_004567.2.
DR PDB; 1POW; X-ray; 2.50 A; A/B=9-593.
DR PDB; 1POX; X-ray; 2.10 A; A/B=9-593.
DR PDB; 1Y9D; X-ray; 2.20 A; A/B/C/D=1-603.
DR PDB; 2EZ4; X-ray; 2.03 A; A/B=1-603.
DR PDB; 2EZ8; X-ray; 1.96 A; A/B=1-603.
DR PDB; 2EZ9; X-ray; 1.60 A; A/B=1-603.
DR PDB; 2EZT; X-ray; 2.29 A; A/B=1-603.
DR PDB; 2EZU; X-ray; 2.16 A; A/B=1-603.
DR PDB; 6HAF; X-ray; 1.30 A; A/B=1-603.
DR PDBsum; 1POW; -.
DR PDBsum; 1POX; -.
DR PDBsum; 1Y9D; -.
DR PDBsum; 2EZ4; -.
DR PDBsum; 2EZ8; -.
DR PDBsum; 2EZ9; -.
DR PDBsum; 2EZT; -.
DR PDBsum; 2EZU; -.
DR PDBsum; 6HAF; -.
DR AlphaFoldDB; P37063; -.
DR SMR; P37063; -.
DR STRING; 220668.lp_3589; -.
DR DrugBank; DB01987; Cocarboxylase.
DR DrugBank; DB03147; Flavin adenine dinucleotide.
DR EnsemblBacteria; CCC80550; CCC80550; lp_3589.
DR KEGG; lpl:lp_3589; -.
DR PATRIC; fig|220668.9.peg.2994; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_0_9; -.
DR OMA; AANWYAR; -.
DR PhylomeDB; P37063; -.
DR BioCyc; LPLA220668:G1GW0-3037-MON; -.
DR BRENDA; 1.2.3.3; 2849.
DR SABIO-RK; P37063; -.
DR EvolutionaryTrace; P37063; -.
DR Proteomes; UP000000432; 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 InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
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-bd_C.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52467; SSF52467; 1.
DR SUPFAM; SSF52518; SSF52518; 2.
DR TIGRFAMs; TIGR02720; pyruv_oxi_spxB; 1.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 1: Evidence at protein level;
KW 3D-structure; FAD; Flavoprotein; Magnesium; Metal-binding; Oxidoreductase;
KW Reference proteome; Thiamine pyrophosphate.
FT CHAIN 1..603
FT /note="Pyruvate oxidase"
FT /id="PRO_0000090818"
FT REGION 1..191
FT /note="Core"
FT REGION 192..342
FT /note="FAD-binding"
FT REGION 343..603
FT /note="Thiamine pyrophosphate binding"
FT BINDING 447
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 474
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 476
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:6HAF"
FT HELIX 13..23
FT /evidence="ECO:0007829|PDB:6HAF"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:6HAF"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:6HAF"
FT HELIX 38..46
FT /evidence="ECO:0007829|PDB:6HAF"
FT TURN 47..50
FT /evidence="ECO:0007829|PDB:6HAF"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:6HAF"
FT HELIX 59..73
FT /evidence="ECO:0007829|PDB:6HAF"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:6HAF"
FT HELIX 85..88
FT /evidence="ECO:0007829|PDB:6HAF"
FT HELIX 91..99
FT /evidence="ECO:0007829|PDB:6HAF"
FT STRAND 104..110
FT /evidence="ECO:0007829|PDB:6HAF"
FT TURN 113..117
FT /evidence="ECO:0007829|PDB:6HAF"
FT HELIX 127..130
FT /evidence="ECO:0007829|PDB:6HAF"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:6HAF"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:6HAF"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:1Y9D"
FT HELIX 146..160
FT /evidence="ECO:0007829|PDB:6HAF"
FT STRAND 162..169
FT /evidence="ECO:0007829|PDB:6HAF"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:6HAF"
FT STRAND 175..178
FT /evidence="ECO:0007829|PDB:6HAF"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:6HAF"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:6HAF"
FT HELIX 199..211
FT /evidence="ECO:0007829|PDB:6HAF"
FT STRAND 213..219
FT /evidence="ECO:0007829|PDB:6HAF"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:6HAF"
FT HELIX 227..237
FT /evidence="ECO:0007829|PDB:6HAF"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:6HAF"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:6HAF"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:1Y9D"
FT STRAND 263..266
FT /evidence="ECO:0007829|PDB:6HAF"
FT HELIX 268..276
FT /evidence="ECO:0007829|PDB:6HAF"
FT STRAND 278..284
FT /evidence="ECO:0007829|PDB:6HAF"
FT TURN 288..298
FT /evidence="ECO:0007829|PDB:6HAF"
FT STRAND 300..307
FT /evidence="ECO:0007829|PDB:6HAF"
FT HELIX 309..311
FT /evidence="ECO:0007829|PDB:6HAF"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:6HAF"
FT STRAND 319..324
FT /evidence="ECO:0007829|PDB:6HAF"
FT HELIX 326..335
FT /evidence="ECO:0007829|PDB:6HAF"
FT HELIX 344..364
FT /evidence="ECO:0007829|PDB:6HAF"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:6HAF"
FT HELIX 373..383
FT /evidence="ECO:0007829|PDB:6HAF"
FT STRAND 389..392
FT /evidence="ECO:0007829|PDB:6HAF"
FT HELIX 396..404
FT /evidence="ECO:0007829|PDB:6HAF"
FT STRAND 412..414
FT /evidence="ECO:0007829|PDB:6HAF"
FT TURN 422..424
FT /evidence="ECO:0007829|PDB:1POW"
FT HELIX 425..435
FT /evidence="ECO:0007829|PDB:6HAF"
FT STRAND 441..446
FT /evidence="ECO:0007829|PDB:6HAF"
FT HELIX 447..453
FT /evidence="ECO:0007829|PDB:6HAF"
FT HELIX 454..456
FT /evidence="ECO:0007829|PDB:6HAF"
FT HELIX 457..462
FT /evidence="ECO:0007829|PDB:6HAF"
FT STRAND 468..473
FT /evidence="ECO:0007829|PDB:6HAF"
FT HELIX 478..487
FT /evidence="ECO:0007829|PDB:6HAF"
FT STRAND 494..496
FT /evidence="ECO:0007829|PDB:6HAF"
FT HELIX 502..508
FT /evidence="ECO:0007829|PDB:6HAF"
FT STRAND 512..516
FT /evidence="ECO:0007829|PDB:6HAF"
FT HELIX 519..521
FT /evidence="ECO:0007829|PDB:6HAF"
FT HELIX 522..532
FT /evidence="ECO:0007829|PDB:6HAF"
FT TURN 533..535
FT /evidence="ECO:0007829|PDB:6HAF"
FT STRAND 538..543
FT /evidence="ECO:0007829|PDB:6HAF"
FT TURN 559..561
FT /evidence="ECO:0007829|PDB:6HAF"
FT HELIX 564..574
FT /evidence="ECO:0007829|PDB:6HAF"
FT HELIX 582..588
FT /evidence="ECO:0007829|PDB:6HAF"
SQ SEQUENCE 603 AA; 66111 MW; 71BEDD006EEB0FBE CRC64;
MVMKQTKQTN ILAGAAVIKV LEAWGVDHLY GIPGGSINSI MDALSAERDR IHYIQVRHEE
VGAMAAAADA KLTGKIGVCF GSAGPGGTHL MNGLYDARED HVPVLALIGQ FGTTGMNMDT
FQEMNENPIY ADVADYNVTA VNAATLPHVI DEAIRRAYAH QGVAVVQIPV DLPWQQIPAE
DWYASANSYQ TPLLPEPDVQ AVTRLTQTLL AAERPLIYYG IGARKAGKEL EQLSKTLKIP
LMSTYPAKGI VADRYPAYLG SANRVAQKPA NEALAQADVV LFVGNNYPFA EVSKAFKNTR
YFLQIDIDPA KLGKRHKTDI AVLADAQKTL AAILAQVSER ESTPWWQANL ANVKNWRAYL
ASLEDKQEGP LQAYQVLRAV NKIAEPDAIY SIDVGDINLN ANRHLKLTPS NRHITSNLFA
TMGVGIPGAI AAKLNYPERQ VFNLAGDGGA SMTMQDLATQ VQYHLPVINV VFTNCQYGFI
KDEQEDTNQN DFIGVEFNDI DFSKIADGVH MQAFRVNKIE QLPDVFEQAK AIAQHEPVLI
DAVITGDRPL PAEKLRLDSA TSSAADIEAF KQRYEAQDLQ PLSTYLKQFG LDDLQHQIGQ
GGF
