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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)DescriptionActionsGraphical viewLength
    Binding sitei225Heme (covalent; via 2 links)3 Publications1
    Active sitei226Proton acceptorPROSITE-ProRule annotationBy similarity1
    Metal bindingi227CalciumPROSITE-ProRule annotation3 Publications1
    Metal bindingi301CalciumPROSITE-ProRule annotation3 Publications1
    Metal bindingi303Calcium; via carbonyl oxygenPROSITE-ProRule annotation3 Publications1
    Metal bindingi305CalciumPROSITE-ProRule annotation3 Publications1
    Metal bindingi307CalciumPROSITE-ProRule annotation3 Publications1
    Sitei372Transition state stabilizerPROSITE-ProRule annotationBy similarity1
    Binding sitei375Heme (covalent; via 2 links)3 Publications1
    Metal bindingi468Iron (heme axial ligand)1

    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
    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)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 22Sequence analysisAdd BLAST22
    PropeptideiPRO_000042488823 – 100By similarityAdd BLAST78
    ChainiPRO_0000424889101 – 712LactoperoxidaseBy similarityAdd BLAST612

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Glycosylationi106N-linked (GlcNAc...)Sequence analysis1
    Disulfide bondi123 ↔ 284PROSITE-ProRule annotation3 Publications
    Disulfide bondi132 ↔ 145PROSITE-ProRule annotation3 Publications
    Glycosylationi212N-linked (GlcNAc...)3 Publications1
    Disulfide bondi246 ↔ 256PROSITE-ProRule annotation3 Publications
    Disulfide bondi250 ↔ 274PROSITE-ProRule annotation3 Publications
    Modified residuei315Phosphoserine2 Publications1
    Glycosylationi322N-linked (GlcNAc...)3 Publications1
    Disulfide bondi354 ↔ 365PROSITE-ProRule annotation3 Publications
    Glycosylationi358N-linked (GlcNAc...)3 Publications1
    Glycosylationi449N-linked (GlcNAc...)3 Publications1
    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

    1712
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi141 – 143Combined sources3
    Beta strandi146 – 150Combined sources5
    Turni151 – 154Combined sources4
    Beta strandi156 – 159Combined sources4
    Beta strandi171 – 173Combined sources3
    Helixi192 – 199Combined sources8
    Beta strandi209 – 214Combined sources6
    Helixi215 – 228Combined sources14
    Beta strandi238 – 240Combined sources3
    Turni241 – 243Combined sources3
    Helixi244 – 249Combined sources6
    Helixi266 – 271Combined sources6
    Beta strandi273 – 275Combined sources3
    Beta strandi282 – 284Combined sources3
    Beta strandi286 – 288Combined sources3
    Beta strandi296 – 298Combined sources3
    Beta strandi302 – 305Combined sources4
    Helixi307 – 310Combined sources4
    Helixi314 – 319Combined sources6
    Helixi353 – 357Combined sources5
    Turni358 – 361Combined sources4
    Turni371 – 374Combined sources4
    Helixi377 – 400Combined sources24
    Helixi406 – 427Combined sources22
    Helixi429 – 434Combined sources6
    Helixi435 – 437Combined sources3
    Helixi438 – 441Combined sources4
    Helixi460 – 463Combined sources4
    Helixi464 – 470Combined sources7
    Beta strandi473 – 476Combined sources4
    Beta strandi482 – 484Combined sources3
    Beta strandi486 – 488Combined sources3
    Beta strandi490 – 492Combined sources3
    Helixi493 – 496Combined sources4
    Helixi501 – 504Combined sources4
    Turni505 – 507Combined sources3
    Helixi510 – 518Combined sources9
    Beta strandi519 – 522Combined sources4
    Helixi532 – 535Combined sources4
    Beta strandi541 – 543Combined sources3
    Beta strandi545 – 548Combined sources4
    Helixi550 – 560Combined sources11
    Helixi566 – 572Combined sources7
    Helixi581 – 587Combined sources7
    Helixi591 – 601Combined sources11
    Helixi604 – 606Combined sources3
    Helixi609 – 615Combined sources7
    Beta strandi620 – 624Combined sources5
    Helixi626 – 641Combined sources16
    Helixi655 – 661Combined sources7
    Helixi666 – 673Combined sources8
    Beta strandi678 – 685Combined sources8
    Turni689 – 692Combined sources4
    Beta strandi693 – 695Combined sources3
    Helixi696 – 698Combined sources3
    Helixi705 – 707Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    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.
    OrthoDBiEOG091G0236.

    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)DescriptionActionsGraphical viewLength
    Sequence conflicti206E → D in ADZ95997 (Ref. 2) Curated1
    Sequence conflicti340G → R in ADZ95997 (Ref. 2) Curated1
    Sequence conflicti362R → H in ADZ95997 (Ref. 2) Curated1
    Sequence conflicti403H → Q in ADZ95997 (Ref. 2) Curated1
    Sequence conflicti405N → D in ADZ95997 (Ref. 2) Curated1
    Sequence conflicti421I → V in ADZ95997 (Ref. 2) Curated1
    Sequence conflicti513T → V in ADZ95997 (Ref. 2) Curated1
    Sequence conflicti664F → M in ADZ95997 (Ref. 2) Curated1
    Sequence conflicti698T → A in ADZ95997 (Ref. 2) Curated1

    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
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    PTM databases

    iPTMnetiA5JUY8.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    GeneIDi102405711.

    Organism-specific databases

    CTDi4025.

    Phylogenomic databases

    HOVERGENiHBG000071.
    OrthoDBiEOG091G0236.

    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...

    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: November 2, 2016
    This is version 62 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.