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Protein

Lactoperoxidase

Gene

LPO

Organism
Bubalus bubalis (Domestic water buffalo)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Antimicrobial agent which utilizes hydrogen peroxide and thiocyanate (SCN) to generate the antimicrobial substance hypothiocyanous acid (HOSCN). May protect the udder from infection and promote growth in newborn calves. Inhibits growth of the following bacterial species: E.coli, K.pneumoniae, P.aeruginosa, S.sonnei, S.saphrophyticus, S.epidermidis, and S.dysenteriae.1 Publication

Catalytic activityi

2 phenolic donor + H2O2 = 2 phenoxyl radical of the donor + 2 H2O.2 Publications

Cofactori

Protein has several cofactor binding sites:
  • Ca2+PROSITE-ProRule annotation1 PublicationNote: Binds 1 Ca2+ ion per heterodimer.PROSITE-ProRule annotation1 Publication
  • heme bPROSITE-ProRule annotation1 PublicationNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group covalently per heterodimer.PROSITE-ProRule annotation1 Publication

Kineticsi

  1. KM=0.82 mM for 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) (at 60 degrees Celsius)1 Publication
  2. KM=0.77 mM for 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) (at 25 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is 6.1 Publication

    Temperature dependencei

    Optimum temperature is 60 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei225 – 2251Heme (covalent; via 2 links)3 Publications
    Active sitei226 – 2261Proton acceptorPROSITE-ProRule annotationBy similarity
    Metal bindingi227 – 2271CalciumPROSITE-ProRule annotation3 Publications
    Metal bindingi301 – 3011CalciumPROSITE-ProRule annotation3 Publications
    Metal bindingi303 – 3031Calcium; via carbonyl oxygenPROSITE-ProRule annotation3 Publications
    Metal bindingi305 – 3051CalciumPROSITE-ProRule annotation3 Publications
    Metal bindingi307 – 3071CalciumPROSITE-ProRule annotation3 Publications
    Sitei372 – 3721Transition state stabilizerPROSITE-ProRule annotationBy similarity
    Binding sitei375 – 3751Heme (covalent; via 2 links)3 Publications
    Metal bindingi468 – 4681Iron (heme axial ligand)

    GO - Molecular functioni

    • calcium ion binding Source: UniProtKB
    • heme binding Source: InterPro
    • thiocyanate peroxidase activity Source: UniProtKB

    GO - Biological processi

    • antibacterial humoral response Source: UniProtKB
    • hydrogen peroxide catabolic process Source: UniProtKB
    • response to oxidative stress Source: InterPro
    • thiocyanate metabolic process Source: GOC
    Complete GO annotation...

    Keywords - Molecular functioni

    Antibiotic, Antimicrobial, Oxidoreductase, Peroxidase

    Keywords - Biological processi

    Hydrogen peroxide

    Keywords - Ligandi

    Calcium, Heme, Iron, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    LactoperoxidaseImported (EC:1.11.1.72 Publications)
    Short name:
    LPO2 Publications
    Short name:
    WBLP1 Publication
    Gene namesi
    Name:LPOImported
    OrganismiBubalus bubalis (Domestic water buffalo)
    Taxonomic identifieri89462 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBubalus

    Subcellular locationi

    GO - Cellular componenti

    • extracellular space Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Sequence analysisAdd
    BLAST
    Propeptidei23 – 10078By similarityPRO_0000424888Add
    BLAST
    Chaini101 – 712612LactoperoxidaseBy similarityPRO_0000424889Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi106 – 1061N-linked (GlcNAc...)Sequence analysis
    Disulfide bondi123 ↔ 284PROSITE-ProRule annotation3 Publications
    Disulfide bondi132 ↔ 145PROSITE-ProRule annotation3 Publications
    Glycosylationi212 – 2121N-linked (GlcNAc...)3 Publications
    Disulfide bondi246 ↔ 256PROSITE-ProRule annotation3 Publications
    Disulfide bondi250 ↔ 274PROSITE-ProRule annotation3 Publications
    Modified residuei315 – 3151Phosphoserine2 Publications
    Glycosylationi322 – 3221N-linked (GlcNAc...)3 Publications
    Disulfide bondi354 ↔ 365PROSITE-ProRule annotation3 Publications
    Glycosylationi358 – 3581N-linked (GlcNAc...)3 Publications
    Glycosylationi449 – 4491N-linked (GlcNAc...)3 Publications
    Disulfide bondi573 ↔ 630PROSITE-ProRule annotation3 Publications
    Disulfide bondi671 ↔ 696PROSITE-ProRule annotation3 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    PTM databases

    iPTMnetiA5JUY8.

    Expressioni

    Tissue specificityi

    Mammary gland; milk.2 Publications

    Structurei

    Secondary structure

    1
    712
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi141 – 1433Combined sources
    Beta strandi146 – 1505Combined sources
    Turni151 – 1544Combined sources
    Beta strandi156 – 1594Combined sources
    Beta strandi171 – 1733Combined sources
    Helixi192 – 1998Combined sources
    Beta strandi209 – 2146Combined sources
    Helixi215 – 22814Combined sources
    Beta strandi238 – 2403Combined sources
    Turni241 – 2433Combined sources
    Helixi244 – 2496Combined sources
    Helixi266 – 2716Combined sources
    Beta strandi273 – 2753Combined sources
    Beta strandi282 – 2843Combined sources
    Beta strandi286 – 2883Combined sources
    Beta strandi296 – 2983Combined sources
    Beta strandi302 – 3054Combined sources
    Helixi307 – 3104Combined sources
    Helixi314 – 3196Combined sources
    Helixi353 – 3575Combined sources
    Turni358 – 3614Combined sources
    Turni371 – 3744Combined sources
    Helixi377 – 40024Combined sources
    Helixi406 – 42722Combined sources
    Helixi429 – 4346Combined sources
    Helixi435 – 4373Combined sources
    Helixi438 – 4414Combined sources
    Helixi460 – 4634Combined sources
    Helixi464 – 4707Combined sources
    Beta strandi473 – 4764Combined sources
    Beta strandi482 – 4843Combined sources
    Beta strandi486 – 4883Combined sources
    Beta strandi490 – 4923Combined sources
    Helixi493 – 4964Combined sources
    Helixi501 – 5044Combined sources
    Turni505 – 5073Combined sources
    Helixi510 – 5189Combined sources
    Beta strandi519 – 5224Combined sources
    Helixi532 – 5354Combined sources
    Beta strandi541 – 5433Combined sources
    Beta strandi545 – 5484Combined sources
    Helixi550 – 56011Combined sources
    Helixi566 – 5727Combined sources
    Helixi581 – 5877Combined sources
    Helixi591 – 60111Combined sources
    Helixi604 – 6063Combined sources
    Helixi609 – 6157Combined sources
    Beta strandi620 – 6245Combined sources
    Helixi626 – 64116Combined sources
    Helixi655 – 6617Combined sources
    Helixi666 – 6738Combined sources
    Beta strandi678 – 6858Combined sources
    Turni689 – 6924Combined sources
    Beta strandi693 – 6953Combined sources
    Helixi696 – 6983Combined sources
    Helixi705 – 7073Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2GJMX-ray2.75A130-712[»]
    2O86X-ray2.80A118-712[»]
    2Z5ZX-ray3.50A118-712[»]
    3ERHX-ray2.40A118-712[»]
    3FAQX-ray2.70A118-712[»]
    3FNLX-ray2.48A118-712[»]
    4Y55X-ray2.10A118-712[»]
    ProteinModelPortaliA5JUY8.
    SMRiA5JUY8. Positions 130-712.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiA5JUY8.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peroxidase family. XPO subfamily.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOVERGENiHBG000071.

    Family and domain databases

    Gene3Di1.10.640.10. 1 hit.
    InterProiIPR010255. Haem_peroxidase.
    IPR019791. Haem_peroxidase_animal.
    IPR029587. LPO.
    [Graphical view]
    PANTHERiPTHR11475:SF67. PTHR11475:SF67. 1 hit.
    PfamiPF03098. An_peroxidase. 1 hit.
    [Graphical view]
    PRINTSiPR00457. ANPEROXIDASE.
    SUPFAMiSSF48113. SSF48113. 1 hit.
    PROSITEiPS50292. PEROXIDASE_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    A5JUY8-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MWVCLQLPVF LASVTLFEVA ASDTIAQAAS TTTISDAVSK VKIQVNKAFL
    60 70 80 90 100
    DSRTRLKTTL SSEAPTTQQL SEYFKHAKGQ TRTAIRNGQV WEESFKRLRR
    110 120 130 140 150
    DTTLTNVTDP SLDLTALSWE VGCGAPVPLV KCDENSPYRT ITGDCNNRRS
    160 170 180 190 200
    PALGAANRAL ARWLPAEYED GLALPFGWTQ RKTRNGFRVP LAREVSNKIV
    210 220 230 240 250
    GYLDEEGVLD QNRSLLFMQW GQIVDHDLDF APETELGSNE HSKTQCEEYC
    260 270 280 290 300
    IQGDNCFPIM FPKNDPKLKT QGKCMPFFRA GFVCPTPPYQ SLAREQINAV
    310 320 330 340 350
    TSFLDASLVY GSEPSLASRL RNLSSPLGLM AVNQEAWDHG LAYLPFNNKK
    360 370 380 390 400
    PSPCEFINTT ARVPCFLAGD FRASEQILLA TAHTLLLREH NRLARELKKL
    410 420 430 440 450
    NPHWNGEKLY QEARKILGAF IQIITFRDYL PIVLGSEMQK WIPPYQGYNN
    460 470 480 490 500
    SVDPRISNVF TFAFRFGHME VPSTVSRLDE NYQPWGPEAE LPLHTLFFNT
    510 520 530 540 550
    WRIIKDGGID PLTRGLLAKK SKLMNQDKMV TSELRNKLFQ PTHKIHGFDL
    560 570 580 590 600
    AAINLQRCRD HGMPGYNSWR GFCGLSQPKT LKGLQTVLKN KILAKKLMDL
    610 620 630 640 650
    YKTPDNIDIW IGGNAEPMVE RGRVGPLLAC LLGRQFQQIR DGDRFWWENP
    660 670 680 690 700
    GVFTEKQRDS LQKFSFSRLI CDNTHITKVP LHAFQANNYP HDFVDCSTVD
    710
    KLDLSPWASR EN
    Length:712
    Mass (Da):80,698
    Last modified:June 26, 2007 - v1
    Checksum:i426BF93704E7309B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti206 – 2061E → D in ADZ95997 (Ref. 2) Curated
    Sequence conflicti340 – 3401G → R in ADZ95997 (Ref. 2) Curated
    Sequence conflicti362 – 3621R → H in ADZ95997 (Ref. 2) Curated
    Sequence conflicti403 – 4031H → Q in ADZ95997 (Ref. 2) Curated
    Sequence conflicti405 – 4051N → D in ADZ95997 (Ref. 2) Curated
    Sequence conflicti421 – 4211I → V in ADZ95997 (Ref. 2) Curated
    Sequence conflicti513 – 5131T → V in ADZ95997 (Ref. 2) Curated
    Sequence conflicti664 – 6641F → M in ADZ95997 (Ref. 2) Curated
    Sequence conflicti698 – 6981T → A in ADZ95997 (Ref. 2) Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    EF580919 mRNA. Translation: ABQ45486.1.
    HQ285238 mRNA. Translation: ADZ95997.1.
    RefSeqiNP_001277812.1. NM_001290883.1.

    Genome annotation databases

    GeneIDi102405711.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    EF580919 mRNA. Translation: ABQ45486.1.
    HQ285238 mRNA. Translation: ADZ95997.1.
    RefSeqiNP_001277812.1. NM_001290883.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2GJMX-ray2.75A130-712[»]
    2O86X-ray2.80A118-712[»]
    2Z5ZX-ray3.50A118-712[»]
    3ERHX-ray2.40A118-712[»]
    3FAQX-ray2.70A118-712[»]
    3FNLX-ray2.48A118-712[»]
    4Y55X-ray2.10A118-712[»]
    ProteinModelPortaliA5JUY8.
    SMRiA5JUY8. Positions 130-712.
    ModBaseiSearch...
    MobiDBiSearch...

    PTM databases

    iPTMnetiA5JUY8.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    GeneIDi102405711.

    Organism-specific databases

    CTDi4025.

    Phylogenomic databases

    HOVERGENiHBG000071.

    Miscellaneous databases

    EvolutionaryTraceiA5JUY8.

    Family and domain databases

    Gene3Di1.10.640.10. 1 hit.
    InterProiIPR010255. Haem_peroxidase.
    IPR019791. Haem_peroxidase_animal.
    IPR029587. LPO.
    [Graphical view]
    PANTHERiPTHR11475:SF67. PTHR11475:SF67. 1 hit.
    PfamiPF03098. An_peroxidase. 1 hit.
    [Graphical view]
    PRINTSiPR00457. ANPEROXIDASE.
    SUPFAMiSSF48113. SSF48113. 1 hit.
    PROSITEiPS50292. PEROXIDASE_3. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    1. Kushwaha G.S., Baskar Singh S., Sheikh I.A., Ethayathulla A.S., Sharma S., Srinivasan A., Singh T.P.
      Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Mammary glandImported.
    2. "Cloning and sequencing of Bubalus bubalis lactoperoxidase gene."
      Pradeep M.A., Kaushik J.K., Mohanty A.K.
      Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Purification of lactoperoxidase from creek-water buffalo milk and investigation of kinetic and antibacterial properties."
      Ozdemir H., Hacibeyoglu H.I., Uslu H.
      Prep. Biochem. Biotechnol. 32:143-155(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    4. "Crystal structure of Buffalo lactoperoxidase at 2.75A resolution."
      Sheikh I.A., Ethayathulla A.S., Singh A.K., Singh N., Sharma S., Singh T.P.
      Submitted (MAR-2006) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 130-712 IN COMPLEX WITH THIOCYANATE; CALCIUM AND HEME, CALCIUM-BINDING SITES, GLYCOSYLATION AT ASN-212; ASN-322; ASN-358 AND ASN-449, DISULFIDE BONDS.
    5. "Crystal structure of the complex of buffalo Lactoperoxidase with fluoride ion at 3.5A resolution."
      Sheikh I.A., Jain R., Singh N., Sharma S., Bhushan A., Kaur P., Srinivasan A., Singh T.P.
      Submitted (JUL-2007) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 118-712 IN COMPLEX WITH CALCIUM AND HEME, CALCIUM-BINDING SITES, PHOSPHORYLATION AT SER-315, GLYCOSYLATION AT ASN-212; ASN-322; ASN-358 AND ASN-449, DISULFIDE BONDS.
    6. "Structural evidence of substrate specificity in mammalian peroxidases: structure of the thiocyanate complex with lactoperoxidase and its interactions at 2.4 A resolution."
      Sheikh I.A., Singh A.K., Singh N., Sinha M., Singh S.B., Bhushan A., Kaur P., Srinivasan A., Sharma S., Singh T.P.
      J. Biol. Chem. 284:14849-14856(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 118-712 IN COMPLEXES WITH THIOCYANATE; CYANIDE; CALCIUM AND HEME, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, CALCIUM-BINDING SITES, PHOSPHORYLATION AT SER-315, GLYCOSYLATION AT ASN-212; ASN-322; ASN-358 AND ASN-449, DISULFIDE BONDS.

    Entry informationi

    Entry nameiPERL_BUBBU
    AccessioniPrimary (citable) accession number: A5JUY8
    Secondary accession number(s): F2X043
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 22, 2014
    Last sequence update: June 26, 2007
    Last modified: January 20, 2016
    This is version 58 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    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.