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P49008

- HEXA_PORGI

UniProt

P49008 - HEXA_PORGI

Protein

Beta-hexosaminidase

Gene

nahA

Organism
Porphyromonas gingivalis (strain ATCC BAA-308 / W83)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 2 (03 Oct 2003)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.

    GO - Molecular functioni

    1. beta-N-acetylhexosaminidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Enzyme and pathway databases

    BioCyciPGIN242619:GHX8-41-MONOMER.

    Protein family/group databases

    CAZyiGH20. Glycoside Hydrolase Family 20.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-hexosaminidase (EC:3.2.1.52)
    Alternative name(s):
    Beta-GlcNAcase
    Beta-N-acetylhexosaminidase
    Short name:
    Beta-NAHase
    N-acetyl-beta-glucosaminidase
    Gene namesi
    Name:nahA
    Ordered Locus Names:PG_0043
    OrganismiPorphyromonas gingivalis (strain ATCC BAA-308 / W83)
    Taxonomic identifieri242619 [NCBI]
    Taxonomic lineageiBacteriaBacteroidetesBacteroidiaBacteroidalesPorphyromonadaceaePorphyromonas
    ProteomesiUP000000588: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    1. cell outer membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell outer membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818PROSITE-ProRule annotationAdd
    BLAST
    Chaini19 – 777759Beta-hexosaminidasePRO_0000012016Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi19 – 191N-palmitoyl cysteineCurated
    Lipidationi19 – 191S-diacylglycerol cysteineCurated

    Keywords - PTMi

    Lipoprotein, Palmitate

    Interactioni

    Protein-protein interaction databases

    STRINGi242619.PG0043.

    Structurei

    3D structure databases

    ProteinModelPortaliP49008.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 20 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG3525.
    KOiK12373.
    OMAiVNINTHV.
    OrthoDBiEOG6DC6HQ.

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    3.30.379.10. 1 hit.
    3.90.182.10. 1 hit.
    InterProiIPR025705. Beta_hexosaminidase_sua/sub.
    IPR004867. CHB_HEX_C_dom.
    IPR029018. Chitobiase/Hex_dom_2-like.
    IPR015883. Glyco_hydro_20_cat-core.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR015882. HEX_bac_N.
    IPR011658. PA14.
    [Graphical view]
    PfamiPF03174. CHB_HEX_C. 1 hit.
    PF00728. Glyco_hydro_20. 1 hit.
    PF02838. Glyco_hydro_20b. 1 hit.
    PF07691. PA14. 1 hit.
    [Graphical view]
    PRINTSiPR00738. GLHYDRLASE20.
    SMARTiSM00758. PA14. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    SSF55545. SSF55545. 1 hit.
    PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P49008-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKRLTFGACI CCLLSLMACS QKAKQVQIPE YDKGINIIPL PMQLTESDDS    50
    FEVDDKTTIC VSAEELKPIA KLLADKLRAS ADLSLQIEIG EEPSGNAIYI 100
    GVDTALPLKE EGYMLRSDKR GVSIIGKSAH GAFYGMQTLL QLLPAEVESS 150
    NEVLLPMTVP GVEIKDEPAF GYRGFMLDVC RHFLSVEDIK KHIDIMAMFK 200
    INRFHWHLTE DQAWRIEIKK YPRLTEVGST RTEGDGTQYS GFYTQEQVRD 250
    IVQYASDRFI TVIPEIEMPG HAMAALAAYP QLACFPREFK PRIIWGVEQD 300
    VYCAGKDSVF RFISDVIDEV APLFPGTYFH IGGDECPKDR WKACSLCQKR 350
    MRDNGLKDEH ELQSYFIKQA EKVLQKHGKR LIGWDEILEG GLAPSATVMS 400
    WRGEDGGIAA ANMNHDVIMT PGSGGLYLDH YQGDPTVEPV AIGGYAPLEQ 450
    VYAYNPLPKE LPADKHRYVL GAQANLWAEY LYTSERYDYQ AYPRLLAVAE 500
    LTWTPLAKKD FADFCRRLDN ACVRLDMHGI NYHIPLPEQP GGSSDFIAFT 550
    DKAKLTFTTS RPMKMVYTLD ETEPTLTSTP YTVPLEFAQT GLLKIRTVTA 600
    GGKMSPVRRI RVEKQPFNMS MEVPAPKPGL TIRTAYGDLY DVPDLQQVAS 650
    WEVGTVSSLE EIMHGKEKIT SPEVLERRVV EATGYVLIPE DGVYEFSTEN 700
    NEFWIDNVKL IDNVGEVKKF SRRNSSRALQ KGYHPIKTIW VGAIQGGWPT 750
    YWNYSRVMIR LKGEEKFKPI SSDMLFQ 777
    Length:777
    Mass (Da):87,661
    Last modified:October 3, 2003 - v2
    Checksum:iD0A55D2C2FFAD864
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti258 – 2581R → H in CAA55582. (PubMed:7881557)Curated
    Sequence conflicti265 – 2651E → M in CAA55582. (PubMed:7881557)Curated
    Sequence conflicti282 – 2832LA → FR in CAA55582. (PubMed:7881557)Curated
    Sequence conflicti575 – 5751T → S in CAA55582. (PubMed:7881557)Curated
    Sequence conflicti747 – 7471G → A in CAA55582. (PubMed:7881557)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X78979 Genomic DNA. Translation: CAA55582.1.
    AE015924 Genomic DNA. Translation: AAQ65295.1.
    RefSeqiNP_904396.1. NC_002950.2.

    Genome annotation databases

    EnsemblBacteriaiAAQ65295; AAQ65295; PG_0043.
    GeneIDi2552216.
    KEGGipgi:PG0043.
    PATRICi22977240. VBIPorGin134034_0039.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X78979 Genomic DNA. Translation: CAA55582.1 .
    AE015924 Genomic DNA. Translation: AAQ65295.1 .
    RefSeqi NP_904396.1. NC_002950.2.

    3D structure databases

    ProteinModelPortali P49008.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 242619.PG0043.

    Protein family/group databases

    CAZyi GH20. Glycoside Hydrolase Family 20.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAQ65295 ; AAQ65295 ; PG_0043 .
    GeneIDi 2552216.
    KEGGi pgi:PG0043.
    PATRICi 22977240. VBIPorGin134034_0039.

    Phylogenomic databases

    eggNOGi COG3525.
    KOi K12373.
    OMAi VNINTHV.
    OrthoDBi EOG6DC6HQ.

    Enzyme and pathway databases

    BioCyci PGIN242619:GHX8-41-MONOMER.

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    3.30.379.10. 1 hit.
    3.90.182.10. 1 hit.
    InterProi IPR025705. Beta_hexosaminidase_sua/sub.
    IPR004867. CHB_HEX_C_dom.
    IPR029018. Chitobiase/Hex_dom_2-like.
    IPR015883. Glyco_hydro_20_cat-core.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR015882. HEX_bac_N.
    IPR011658. PA14.
    [Graphical view ]
    Pfami PF03174. CHB_HEX_C. 1 hit.
    PF00728. Glyco_hydro_20. 1 hit.
    PF02838. Glyco_hydro_20b. 1 hit.
    PF07691. PA14. 1 hit.
    [Graphical view ]
    PRINTSi PR00738. GLHYDRLASE20.
    SMARTi SM00758. PA14. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    SSF55545. SSF55545. 1 hit.
    PROSITEi PS51257. PROKAR_LIPOPROTEIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and expression in Escherichia coli of the nahA gene from Porphyromonas gingivalis indicates that beta-N-acetylhexosaminidase is an outer-membrane-associated lipoprotein."
      Lovatt A., Roberts I.S.
      Microbiology 140:3399-3406(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC BAA-308 / W83.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-308 / W83.

    Entry informationi

    Entry nameiHEXA_PORGI
    AccessioniPrimary (citable) accession number: P49008
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: October 3, 2003
    Last modified: October 1, 2014
    This is version 110 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3