Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Pyruvate oxidase

Gene

pox5

Organism
Lactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Important for the aerobic growth. Decarboxylates pyruvate in four steps. The energy released is partially stored in acetyl phosphate.

Catalytic activityi

Pyruvate + phosphate + O2 = acetyl phosphate + CO2 + H2O2.

Cofactori

Protein has several cofactor binding sites:
  • FADNote: Binds 1 FAD per subunit.
  • Mg2+Note: Binds 1 Mg2+ ion per subunit.
  • thiamine diphosphateNote: Binds 1 thiamine pyrophosphate per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi447 – 4471Magnesium
Metal bindingi474 – 4741Magnesium
Metal bindingi476 – 4761Magnesium

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, Magnesium, Metal-binding, Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciLPLA220668-WGS:GSPK-3037-MONOMER.
BRENDAi1.2.3.3. 2849.
SABIO-RKP37063.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate oxidase (EC:1.2.3.3)
Alternative name(s):
Pyruvic oxidase
Short name:
POX
Gene namesi
Name:pox5
Ordered Locus Names:lp_3589
OrganismiLactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
Taxonomic identifieri220668 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus
Proteomesi
  • UP000000432 Componenti: Chromosome

Pathology & Biotechi

Chemistry

DrugBankiDB03147. Flavin adenine dinucleotide.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 603603Pyruvate oxidasePRO_0000090818Add
BLAST

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

STRINGi220668.lp_3589.

Structurei

Secondary structure

1
603
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 123Combined sources
Helixi13 – 2311Combined sources
Beta strandi28 – 314Combined sources
Helixi35 – 373Combined sources
Helixi38 – 469Combined sources
Turni47 – 504Combined sources
Beta strandi51 – 555Combined sources
Helixi59 – 7315Combined sources
Beta strandi77 – 815Combined sources
Helixi85 – 884Combined sources
Helixi91 – 999Combined sources
Beta strandi104 – 1107Combined sources
Turni113 – 1175Combined sources
Helixi127 – 1304Combined sources
Turni131 – 1333Combined sources
Beta strandi135 – 1395Combined sources
Turni143 – 1453Combined sources
Helixi146 – 16015Combined sources
Beta strandi162 – 1698Combined sources
Helixi172 – 1743Combined sources
Beta strandi175 – 1784Combined sources
Turni179 – 1813Combined sources
Helixi186 – 1883Combined sources
Helixi199 – 21113Combined sources
Beta strandi213 – 2197Combined sources
Helixi221 – 2233Combined sources
Helixi227 – 23711Combined sources
Beta strandi241 – 2433Combined sources
Helixi245 – 2473Combined sources
Beta strandi258 – 2614Combined sources
Beta strandi263 – 2664Combined sources
Helixi268 – 2769Combined sources
Beta strandi278 – 2847Combined sources
Turni288 – 29811Combined sources
Beta strandi300 – 3078Combined sources
Helixi309 – 3113Combined sources
Beta strandi314 – 3163Combined sources
Beta strandi319 – 3246Combined sources
Helixi326 – 33510Combined sources
Helixi344 – 36421Combined sources
Beta strandi368 – 3703Combined sources
Helixi373 – 38311Combined sources
Beta strandi389 – 3924Combined sources
Helixi396 – 4049Combined sources
Beta strandi412 – 4143Combined sources
Turni422 – 4243Combined sources
Helixi425 – 43511Combined sources
Beta strandi441 – 4466Combined sources
Helixi447 – 4537Combined sources
Helixi454 – 4563Combined sources
Helixi457 – 4626Combined sources
Beta strandi468 – 4736Combined sources
Helixi478 – 48710Combined sources
Beta strandi494 – 4963Combined sources
Helixi502 – 5087Combined sources
Beta strandi512 – 5165Combined sources
Helixi519 – 5213Combined sources
Helixi522 – 53211Combined sources
Turni533 – 5353Combined sources
Beta strandi538 – 5436Combined sources
Turni559 – 5613Combined sources
Helixi564 – 57411Combined sources
Helixi582 – 5887Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1POWX-ray2.50A/B9-593[»]
1POXX-ray2.10A/B9-593[»]
1Y9DX-ray2.20A/B/C/D1-603[»]
2EZ4X-ray2.03A/B1-603[»]
2EZ8X-ray1.96A/B1-603[»]
2EZ9X-ray1.60A/B1-603[»]
2EZTX-ray2.29A/B1-603[»]
2EZUX-ray2.16A/B1-603[»]
ProteinModelPortaliP37063.
SMRiP37063. Positions 9-593.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP37063.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 191191CoreAdd
BLAST
Regioni192 – 342151FAD-bindingAdd
BLAST
Regioni343 – 603261Thiamine pyrophosphate bindingAdd
BLAST

Domaini

Each monomer is divided into three domains, each of which contains a six-stranded parallel beta sheet surrounded by alpha helices.

Sequence similaritiesi

Belongs to the TPP enzyme family.Curated

Phylogenomic databases

eggNOGiENOG4105C7K. Bacteria.
COG0028. LUCA.
HOGENOMiHOG000258444.
KOiK00158.
OMAiLFRECSV.

Family and domain databases

Gene3Di3.40.50.1220. 1 hit.
3.40.50.970. 2 hits.
InterProiIPR029035. DHS-like_NAD/FAD-binding_dom.
IPR014092. Pyruvate_oxidase.
IPR029061. THDP-binding.
IPR012000. Thiamin_PyroP_enz_cen_dom.
IPR012001. Thiamin_PyroP_enz_TPP-bd_dom.
IPR000399. TPP-bd_CS.
IPR011766. TPP_enzyme-bd_C.
[Graphical view]
PfamiPF02775. TPP_enzyme_C. 1 hit.
PF00205. TPP_enzyme_M. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
[Graphical view]
SUPFAMiSSF52467. SSF52467. 1 hit.
SSF52518. SSF52518. 2 hits.
TIGRFAMsiTIGR02720. pyruv_oxi_spxB. 1 hit.
PROSITEiPS00187. TPP_ENZYMES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P37063-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVMKQTKQTN ILAGAAVIKV LEAWGVDHLY GIPGGSINSI MDALSAERDR
60 70 80 90 100
IHYIQVRHEE VGAMAAAADA KLTGKIGVCF GSAGPGGTHL MNGLYDARED
110 120 130 140 150
HVPVLALIGQ FGTTGMNMDT FQEMNENPIY ADVADYNVTA VNAATLPHVI
160 170 180 190 200
DEAIRRAYAH QGVAVVQIPV DLPWQQIPAE DWYASANSYQ TPLLPEPDVQ
210 220 230 240 250
AVTRLTQTLL AAERPLIYYG IGARKAGKEL EQLSKTLKIP LMSTYPAKGI
260 270 280 290 300
VADRYPAYLG SANRVAQKPA NEALAQADVV LFVGNNYPFA EVSKAFKNTR
310 320 330 340 350
YFLQIDIDPA KLGKRHKTDI AVLADAQKTL AAILAQVSER ESTPWWQANL
360 370 380 390 400
ANVKNWRAYL ASLEDKQEGP LQAYQVLRAV NKIAEPDAIY SIDVGDINLN
410 420 430 440 450
ANRHLKLTPS NRHITSNLFA TMGVGIPGAI AAKLNYPERQ VFNLAGDGGA
460 470 480 490 500
SMTMQDLATQ VQYHLPVINV VFTNCQYGFI KDEQEDTNQN DFIGVEFNDI
510 520 530 540 550
DFSKIADGVH MQAFRVNKIE QLPDVFEQAK AIAQHEPVLI DAVITGDRPL
560 570 580 590 600
PAEKLRLDSA TSSAADIEAF KQRYEAQDLQ PLSTYLKQFG LDDLQHQIGQ

GGF
Length:603
Mass (Da):66,111
Last modified:March 25, 2003 - v3
Checksum:i71BEDD006EEB0FBE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL935263 Genomic DNA. Translation: CCC80550.1.
RefSeqiWP_003646223.1. NC_004567.2.
YP_004891064.1. NC_004567.2.

Genome annotation databases

EnsemblBacteriaiCCC80550; CCC80550; lp_3589.
GeneIDi1062065.
KEGGilpl:lp_3589.
PATRICi22252792. VBILacPla27411_2994.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL935263 Genomic DNA. Translation: CCC80550.1.
RefSeqiWP_003646223.1. NC_004567.2.
YP_004891064.1. NC_004567.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1POWX-ray2.50A/B9-593[»]
1POXX-ray2.10A/B9-593[»]
1Y9DX-ray2.20A/B/C/D1-603[»]
2EZ4X-ray2.03A/B1-603[»]
2EZ8X-ray1.96A/B1-603[»]
2EZ9X-ray1.60A/B1-603[»]
2EZTX-ray2.29A/B1-603[»]
2EZUX-ray2.16A/B1-603[»]
ProteinModelPortaliP37063.
SMRiP37063. Positions 9-593.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi220668.lp_3589.

Chemistry

DrugBankiDB03147. Flavin adenine dinucleotide.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCC80550; CCC80550; lp_3589.
GeneIDi1062065.
KEGGilpl:lp_3589.
PATRICi22252792. VBILacPla27411_2994.

Phylogenomic databases

eggNOGiENOG4105C7K. Bacteria.
COG0028. LUCA.
HOGENOMiHOG000258444.
KOiK00158.
OMAiLFRECSV.

Enzyme and pathway databases

BioCyciLPLA220668-WGS:GSPK-3037-MONOMER.
BRENDAi1.2.3.3. 2849.
SABIO-RKP37063.

Miscellaneous databases

EvolutionaryTraceiP37063.

Family and domain databases

Gene3Di3.40.50.1220. 1 hit.
3.40.50.970. 2 hits.
InterProiIPR029035. DHS-like_NAD/FAD-binding_dom.
IPR014092. Pyruvate_oxidase.
IPR029061. THDP-binding.
IPR012000. Thiamin_PyroP_enz_cen_dom.
IPR012001. Thiamin_PyroP_enz_TPP-bd_dom.
IPR000399. TPP-bd_CS.
IPR011766. TPP_enzyme-bd_C.
[Graphical view]
PfamiPF02775. TPP_enzyme_C. 1 hit.
PF00205. TPP_enzyme_M. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
[Graphical view]
SUPFAMiSSF52467. SSF52467. 1 hit.
SSF52518. SSF52518. 2 hits.
TIGRFAMsiTIGR02720. pyruv_oxi_spxB. 1 hit.
PROSITEiPS00187. TPP_ENZYMES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPOXB_LACPL
AccessioniPrimary (citable) accession number: P37063
Secondary accession number(s): F9ULE3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: March 25, 2003
Last modified: September 7, 2016
This is version 116 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.