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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)DescriptionActionsGraphical viewLength
Metal bindingi447Magnesium1
Metal bindingi474Magnesium1
Metal bindingi476Magnesium1

GO - Molecular functioni

Keywordsi

Molecular functionOxidoreductase
LigandFAD, Flavoprotein, Magnesium, Metal-binding, Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciLPLA220668:G137Z-3016-MONOMER.
BRENDAi1.2.3.3. 2849.
SABIO-RKiP37063.

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 databases

DrugBankiDB03147. Flavin adenine dinucleotide.
DB01987. Thiamin Diphosphate.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000908181 – 603Pyruvate oxidaseAdd BLAST603

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

STRINGi220668.lp_3589.

Structurei

Secondary structure

1603
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi10 – 12Combined sources3
Helixi13 – 23Combined sources11
Beta strandi28 – 31Combined sources4
Helixi35 – 37Combined sources3
Helixi38 – 46Combined sources9
Turni47 – 50Combined sources4
Beta strandi51 – 55Combined sources5
Helixi59 – 73Combined sources15
Beta strandi77 – 81Combined sources5
Helixi85 – 88Combined sources4
Helixi91 – 99Combined sources9
Beta strandi104 – 110Combined sources7
Turni113 – 117Combined sources5
Helixi127 – 130Combined sources4
Turni131 – 133Combined sources3
Beta strandi135 – 139Combined sources5
Turni143 – 145Combined sources3
Helixi146 – 160Combined sources15
Beta strandi162 – 169Combined sources8
Helixi172 – 174Combined sources3
Beta strandi175 – 178Combined sources4
Turni179 – 181Combined sources3
Helixi186 – 188Combined sources3
Helixi199 – 211Combined sources13
Beta strandi213 – 219Combined sources7
Helixi221 – 223Combined sources3
Helixi227 – 237Combined sources11
Beta strandi241 – 243Combined sources3
Helixi245 – 247Combined sources3
Beta strandi258 – 261Combined sources4
Beta strandi263 – 266Combined sources4
Helixi268 – 276Combined sources9
Beta strandi278 – 284Combined sources7
Turni288 – 298Combined sources11
Beta strandi300 – 307Combined sources8
Helixi309 – 311Combined sources3
Beta strandi314 – 316Combined sources3
Beta strandi319 – 324Combined sources6
Helixi326 – 335Combined sources10
Helixi344 – 364Combined sources21
Beta strandi368 – 370Combined sources3
Helixi373 – 383Combined sources11
Beta strandi389 – 392Combined sources4
Helixi396 – 404Combined sources9
Beta strandi412 – 414Combined sources3
Turni422 – 424Combined sources3
Helixi425 – 435Combined sources11
Beta strandi441 – 446Combined sources6
Helixi447 – 453Combined sources7
Helixi454 – 456Combined sources3
Helixi457 – 462Combined sources6
Beta strandi468 – 473Combined sources6
Helixi478 – 487Combined sources10
Beta strandi494 – 496Combined sources3
Helixi502 – 508Combined sources7
Beta strandi512 – 516Combined sources5
Helixi519 – 521Combined sources3
Helixi522 – 532Combined sources11
Turni533 – 535Combined sources3
Beta strandi538 – 543Combined sources6
Turni559 – 561Combined sources3
Helixi564 – 574Combined sources11
Helixi582 – 588Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP37063.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 191CoreAdd BLAST191
Regioni192 – 342FAD-bindingAdd BLAST151
Regioni343 – 603Thiamine pyrophosphate bindingAdd BLAST261

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.
OMAiAANWYAR.

Family and domain databases

Gene3Di3.40.50.1220. 1 hit.
InterProiView protein in InterPro
IPR029035. 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.
PfamiView protein in Pfam
PF02775. TPP_enzyme_C. 1 hit.
PF00205. TPP_enzyme_M. 1 hit.
PF02776. TPP_enzyme_N. 1 hit.
SUPFAMiSSF52467. SSF52467. 1 hit.
SSF52518. SSF52518. 2 hits.
TIGRFAMsiTIGR02720. pyruv_oxi_spxB. 1 hit.
PROSITEiView protein in PROSITE
PS00187. TPP_ENZYMES. 1 hit.

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.
PATRICifig|220668.9.peg.2994.

Similar proteinsi

Entry informationi

Entry nameiPOXB_LACPL
AccessioniPrimary (citable) accession number: P37063
Secondary accession number(s): F9ULE3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: March 25, 2003
Last modified: August 30, 2017
This is version 122 of the entry and version 3 of the sequence. See 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