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serotype 4
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serotype 2
D39V
serotype 2
Hungary19A-6
serotype 19A
EF3030
serotype 19F
670-6B
serotype 6B
6A-10
serotype 6A
70585
serotype 5
A026
serotype 19F
A66
serotype 3
AP200
serotype 11A
ASP0581
serotype 12F
ATCC 49619
serotype 19F
ATCC 700669
serotype 23F
BVJ1JL
serotype 1
CGSP14
serotype 14
G54
serotype 19F
HU-OH
serotype 3
Hu15
serotype 19A
Hu17
serotype 19A
INV104
serotype 1
INV200
serotype 14
JJA
serotype 14
MDRSPN001
serotype 19F
NCTC7466
serotype 2
NU83127
serotype 4
OXC141
serotype 3
P1031
serotype 1
R6
serotype 2
SP49
serotype 19A
SPN032672
serotype 1
SPN034156
serotype 3
SPN034183
serotype 3
SPN994038
serotype 3
SPN994039
serotype 3
SPNA45
serotype 3
ST556
serotype 19F
TCH8431/19A
serotype 19A
Taiwan19F-14
serotype 19F
Xen35
serotype 4
gamPNI0373
serotype 1

NCBI: 02-AUG-2013

⊟Summary[edit | edit source]

  • organism: Streptococcus pneumoniae gamPNI0373
  • locus tag: HMPREF1038_00746 [new locus tag: HMPREF1038_RS03665 ]
  • pan locus tag?: PNEUPAN001678000
  • symbol: spxB
  • pan gene symbol?: spxB
  • synonym:
  • product: pyruvate oxidase

⊟Genome View[edit | edit source]

⊟Gene[edit | edit source]

⊟General[edit | edit source]

  • type: CDS
  • locus tag: HMPREF1038_00746 [new locus tag: HMPREF1038_RS03665 ]
  • symbol: spxB
  • product: pyruvate oxidase
  • replicon: chromosome
  • strand: +
  • coordinates: 684566..686341
  • length: 1776
  • essential: unknown

⊟Accession numbers[edit | edit source]

⊟Phenotype[edit | edit source]

Share your knowledge and add information here. [edit]

⊟DNA sequence[edit | edit source]

  • 1
    61
    121
    181
    241
    301
    361
    421
    481
    541
    601
    661
    721
    781
    841
    901
    961
    1021
    1081
    1141
    1201
    1261
    1321
    1381
    1441
    1501
    1561
    1621
    1681
    1741
    ATGACTCAAGGGAAAATTACTGCATCTGCAGCAATGCTTAACGTATTGAAAACATGGGGC
    GTAGATACAATCTACGGTATCCCATCAGGAACACTCAGCTCATTGATGGACGCTTTGGCT
    GAAGACAAAGATATCCGCTTCTTACAAGTTCGCCACGAAGAGACAGGTGCTCTTGCAGCG
    GTTATGCAAGCTAAATTCGGCGGCTCAATCGGGGTTGCAGTTGGTTCAGGTGGTCCAGGT
    GCGACTCACTTGATTAACGGTGTTTACGATGCAGCTATGGATAACACTCCATTCCTAGCG
    ATCCTTGGATCACGTCCAGTTAACGAATTGAACATGGATGCTTTCCAAGAGCTTAACCAA
    AACCCAATGTACAACGGTATCGCTGTTTACAACAAACGTGTAGCTTACGCTGAGCAATTG
    CCAAAAGTAATTGACGAAGCCTGCCGTGCTGCAGTTTCTAAAAAAGGTCCAGCTGTTGTT
    GAAATTCCAGTAAACTTCGGTTTCCAAGAAATCGATGAAAACTCATACTACGGTTCAGGT
    TCATACGAACGCTCATTCATCGCTCCTGCTTTGAACGAAGTTGAAATCGACAAAGCTGTT
    GAAATCTTGAACAATGCTGAACGCCCAGTTATCTATGCTGGATTTGGTGGTGTTAAAGCT
    GGTGAAGTGATTACTGAATTGTCACGTAAAATCAAAGCACCAATCATCACAACTGGTAAA
    AACTTTGAAGCTTTCGAATGGAACTATGAAGGTTTGACAGGTTCTGCTTACCGTGTTGGT
    TGGAAACCAGCCAACGAAGTGGTCTTTGAAGCAGACACAGTTCTTTTCCTTGGTTCAAAC
    TTCCCATTTGCTGAAGTTTACGAAGCATTCAAGAACACTGAAAAATTCATCCAAGTCGAT
    ATCGACCCTTACAAACTTGGTAAACGTCATGCCCTTGACGCTTCAATCCTTGGTGATGCT
    GGTCAAGCAGCTAAAGCTATCCTTGACAAAGTAAACCCAGTTGAATCAACTCCATGGTGG
    CGTGCAAACGTTAAGAACAACCAAAACTGGCGTGATTACATGAACAAACTCGAAGGTAAA
    ACTGAGGGTGAATTGCAATTGTATCAAGTTTACAATGCAATCAACAAACATGCTGATCAA
    GACGCTATCTACTCAATCGACGTAGGTAACACTACTCAAACATCTACTCGTCACCTTCAC
    ATGACACCTAAGAACATGTGGCGTACATCTCCACTCTTTGCGACAATGGGTATTGCCCTT
    CCTGGTGGTATCGCTGCTAAGAAAGACAATCCAGATCGCCAAGTATGGAACATCATGGGT
    GACGGAGCATTCAACATGTGCTACCCAGACGTTATCACAAACGTTCAATACGACCTTCCA
    GTTATCAACCTTGTCTTCTCAAATGCTGAGTACGGCTTCATCAAGAACAAATACGAAGAT
    ACAAACAAACACTTGTTTGGTGTAGACTTCACAAACGCTGACTACGCTAAAATTGCGGAA
    GCTCAAGGAGCTGTTGGATTCACAGTTGACCGTATCGAAGACATCGATGCAGTTGTTGCA
    GAAGCTGTTAAATTGAACAAAGAAGGTAAAACTGTTGTCATCGATGCTCGCATCACTCAA
    CACCGTCCACTTCCAGTAGAAGTACTTGAATTGGATCCAAAACTTCACTCAGAAGAAGCT
    ATCAAAGCCTTCAAGGAAAAATACGAAGCAGAAGAACTCGTACCATTCCGTCTCTTCTTG
    GAAGAAGAAGGATTGCAATCACGCGCAATTAAATAA
    60
    120
    180
    240
    300
    360
    420
    480
    540
    600
    660
    720
    780
    840
    900
    960
    1020
    1080
    1140
    1200
    1260
    1320
    1380
    1440
    1500
    1560
    1620
    1680
    1740
    1776

⊟Protein[edit | edit source]

⊟General[edit | edit source]

  • locus tag: HMPREF1038_00746 [new locus tag: HMPREF1038_RS03665 ]
  • symbol: SpxB
  • description: pyruvate oxidase
  • length: 591
  • theoretical pI: 4.80988
  • theoretical MW: 65265.5
  • GRAVY: -0.235871

⊟Function[edit | edit source]

  • reaction:
    EC 1.2.3.3?  ExPASy
    Pyruvate oxidase Pyruvate + phosphate + O2 = acetyl phosphate + CO2 + H2O2
  • TIGRFAM:
    Metabolism Energy metabolism Aerobic pyruvate oxidase (TIGR02720; EC 1.2.3.3; HMM-score: 1008.1)
    and 13 more
    Metabolism Amino acid biosynthesis Pyruvate family acetolactate synthase, large subunit, biosynthetic type (TIGR00118; EC 2.2.1.6; HMM-score: 269.2)
    Metabolism Central intermediary metabolism Other sulfoacetaldehyde acetyltransferase (TIGR03457; EC 2.3.3.15; HMM-score: 263)
    glyoxylate carboligase (TIGR01504; EC 4.1.1.47; HMM-score: 192.5)
    Metabolism Energy metabolism Fermentation acetolactate synthase, catabolic (TIGR02418; EC 2.2.1.6; HMM-score: 191.7)
    Metabolism Energy metabolism Sugars 3,5/4-trihydroxycyclohexa-1,2-dione hydrolase (TIGR04377; EC 3.7.1.-; HMM-score: 140.5)
    Cellular processes Cellular processes Detoxification oxalyl-CoA decarboxylase (TIGR03254; EC 4.1.1.8; HMM-score: 132.1)
    indolepyruvate/phenylpyruvate decarboxylase (TIGR03394; EC 4.1.1.43,4.1.1.74; HMM-score: 79.6)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Menaquinone and ubiquinone 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase (TIGR00173; EC 2.2.1.9; HMM-score: 37.7)
    Metabolism Central intermediary metabolism Other indolepyruvate decarboxylase (TIGR03393; EC 4.1.1.74; HMM-score: 27)
    Metabolism Biosynthesis of cofactors, prosthetic groups, and carriers Other sulfopyruvate decarboxylase, alpha subunit (TIGR03845; EC 4.1.1.79; HMM-score: 20.4)
    Metabolism Energy metabolism Methanogenesis sulfopyruvate decarboxylase, alpha subunit (TIGR03845; EC 4.1.1.79; HMM-score: 20.4)
    formylmethanofuran dehydrogenase subunit B (TIGR03129; EC 1.2.99.5; HMM-score: 12.5)
    phosphonopyruvate decarboxylase (TIGR03297; EC 4.1.1.82; HMM-score: 10.9)
  • TheSEED  :
    • Pyruvate oxidase (EC 1.2.3.3)
    Carbohydrates Central carbohydrate metabolism Pyruvate metabolism II: acetyl-CoA, acetogenesis from pyruvate  Pyruvate oxidase (EC 1.2.3.3)
  • PFAM:
    THDP-binding (CL0254) TPP_enzyme_N; Thiamine pyrophosphate enzyme, N-terminal TPP binding domain (PF02776; HMM-score: 136)
    TPP_enzyme_C; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain (PF02775; HMM-score: 118.2)
    and 2 more
    FAD_DHS (CL0085) TPP_enzyme_M; Thiamine pyrophosphate enzyme, central domain (PF00205; HMM-score: 91.4)
    THDP-binding (CL0254) POR_N; Pyruvate flavodoxin/ferredoxin oxidoreductase, thiamine diP-bdg (PF01855; HMM-score: 26.2)

⊟Structure, modifications & cofactors[edit | edit source]

  • domains:
  • modifications:
  • cofactors:
  • effectors:

⊟Localization[edit | edit source]

  • PSORTb: Cytoplasmic Membrane
    • Cytoplasmic Score: 0.17
    • Cytoplasmic Membrane Score: 9.51
    • Cellwall Score: 0.16
    • Extracellular Score: 0.15
    • Internal Helices: 0
  • SignalP: no predicted signal peptide
    • SP(Sec/SPI): 0.056912
    • TAT(Tat/SPI): 0.005212
    • LIPO(Sec/SPII): 0.005244
  • predicted transmembrane helices (TMHMM): 0

⊟Accession numbers[edit | edit source]

  • GI:
  • RefSeq: AFS42812 NCBI
  • UniProt:

⊟Protein sequence[edit | edit source]

  • MTQGKITASAAMLNVLKTWGVDTIYGIPSGTLSSLMDALAEDKDIRFLQVRHEETGALAAVMQAKFGGSIGVAVGSGGPGATHLINGVYDAAMDNTPFLAILGSRPVNELNMDAFQELNQNPMYNGIAVYNKRVAYAEQLPKVIDEACRAAVSKKGPAVVEIPVNFGFQEIDENSYYGSGSYERSFIAPALNEVEIDKAVEILNNAERPVIYAGFGGVKAGEVITELSRKIKAPIITTGKNFEAFEWNYEGLTGSAYRVGWKPANEVVFEADTVLFLGSNFPFAEVYEAFKNTEKFIQVDIDPYKLGKRHALDASILGDAGQAAKAILDKVNPVESTPWWRANVKNNQNWRDYMNKLEGKTEGELQLYQVYNAINKHADQDAIYSIDVGNTTQTSTRHLHMTPKNMWRTSPLFATMGIALPGGIAAKKDNPDRQVWNIMGDGAFNMCYPDVITNVQYDLPVINLVFSNAEYGFIKNKYEDTNKHLFGVDFTNADYAKIAEAQGAVGFTVDRIEDIDAVVAEAVKLNKEGKTVVIDARITQHRPLPVEVLELDPKLHSEEAIKAFKEKYEAEELVPFRLFLEEEGLQSRAIK

⊟Experimental data[edit | edit source]

  • protein localization:
  • interaction partners:

⊟Expression & Regulation[edit | edit source]

⊟Operon[edit | edit source]

⊟Regulation[edit | edit source]

  • regulator:

⊟Expression data[edit | edit source]

⊟Biological Material[edit | edit source]

⊟Mutants[edit | edit source]

⊟Expression vector[edit | edit source]

⊟lacZ fusion[edit | edit source]

⊟GFP fusion[edit | edit source]

⊟two-hybrid system[edit | edit source]

⊟FLAG-tag construct[edit | edit source]

⊟Antibody[edit | edit source]

⊟Other Information[edit | edit source]

You are kindly invited to share additional interesting facts.

⊟Literature[edit | edit source]

⊟References[edit | edit source]

⊟Relevant publications[edit | edit source]

Christopher D Pericone, Sunny Park, James A Imlay, Jeffrey N Weiser
Factors contributing to hydrogen peroxide resistance in Streptococcus pneumoniae include pyruvate oxidase (SpxB) and avoidance of the toxic effects of the fenton reaction.
J Bacteriol: 2003, 185(23);6815-25
[PubMed:14617646] [WorldCat.org] [DOI] (P p)Gili Regev-Yochay, Krzysztof Trzcinski, Claudette M Thompson, Marc Lipsitch, Richard Malley
SpxB is a suicide gene of Streptococcus pneumoniae and confers a selective advantage in an in vivo competitive colonization model.
J Bacteriol: 2007, 189(18);6532-9
[PubMed:17631628] [WorldCat.org] [DOI] (P p)Patrick Bättig, Kathrin Mühlemann
Influence of the spxB gene on competence in Streptococcus pneumoniae.
J Bacteriol: 2008, 190(4);1184-9
[PubMed:18065543] [WorldCat.org] [DOI] (I p)Smirla Ramos-Montañez, Ho-Ching Tiffany Tsui, Kyle J Wayne, Jordan L Morris, Lindsey E Peters, Faming Zhang, Krystyna M Kazmierczak, Lok-To Sham, Malcolm E Winkler
Polymorphism and regulation of the spxB (pyruvate oxidase) virulence factor gene by a CBS-HotDog domain protein (SpxR) in serotype 2 Streptococcus pneumoniae.
Mol Microbiol: 2008, 67(4);729-46
[PubMed:18179423] [WorldCat.org] [DOI] (P p)Hiroaki Taniai, Ken-ichiro Iida, Masanori Seki, Mitsumasa Saito, Susumu Shiota, Hiroaki Nakayama, Shin-ichi Yoshida
Concerted action of lactate oxidase and pyruvate oxidase in aerobic growth of Streptococcus pneumoniae: role of lactate as an energy source.
J Bacteriol: 2008, 190(10);3572-9
[PubMed:18344365] [WorldCat.org] [DOI] (I p)Sandra M Carvalho, Vahid Farshchi Andisi, Henrik Gradstedt, Jolanda Neef, Oscar P Kuipers, Ana R Neves, Jetta J E Bijlsma
Pyruvate oxidase influences the sugar utilization pattern and capsule production in Streptococcus pneumoniae.
PLoS One: 2013, 8(7);e68277
[PubMed:23844180] [WorldCat.org] [DOI] (I e)Haley Echlin, Matthew W Frank, Amy Iverson, Ti-Cheng Chang, Michael D L Johnson, Charles O Rock, Jason W Rosch
Pyruvate Oxidase as a Critical Link between Metabolism and Capsule Biosynthesis in Streptococcus pneumoniae.
PLoS Pathog: 2016, 12(10);e1005951
[PubMed:27760231] [WorldCat.org] [DOI] (I e)Joseph C Bryant, Ridge C Dabbs, Katie L Oswalt, Lindsey R Brown, Jason W Rosch, Keun S Seo, Janet R Donaldson, Larry S McDaniel, Justin A Thornton
Pyruvate oxidase of Streptococcus pneumoniae contributes to pneumolysin release.
BMC Microbiol: 2016, 16(1);271
[PubMed:27829373] [WorldCat.org] [DOI] (I e)B Spellerberg, D R Cundell, J Sandros, B J Pearce, I Idanpaan-Heikkila, C Rosenow, H R Masure
Pyruvate oxidase, as a determinant of virulence in Streptococcus pneumoniae.
Mol Microbiol: 1996, 19(4);803-13
[PubMed:8820650] [WorldCat.org] [DOI] (P p)

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