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Q9LAP7

- AAGAR_ALTAG

UniProt

Q9LAP7 - AAGAR_ALTAG

Protein

Alpha-agarase

Gene

agaA

Organism
Alteromonas agarilytica
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 46 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Alpha-agarase. Does not hydrolyze agarotetraose, agarohexaose, kappa-carrageenan, iota-carrageenan or lambda-carrageenan.1 Publication

    Catalytic activityi

    Endohydrolysis of 1,3-alpha-L-galactosidic linkages in agarose, yielding agarotetraose as the major product.1 Publication

    Cofactori

    Calcium.1 Publication

    pH dependencei

    Optimum pH is 7.2. Active between pH 6.0 and 9.0.1 Publication

    Temperature dependencei

    Inactive above 60 degrees Celsius.1 Publication

    GO - Molecular functioni

    1. alpha-agarase activity Source: UniProtKB-EC
    2. calcium ion binding Source: InterPro
    3. carbohydrate binding Source: InterPro

    GO - Biological processi

    1. cell adhesion Source: InterPro
    2. polysaccharide catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Polysaccharide degradation

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-16655.
    BRENDAi3.2.1.158. 8321.

    Protein family/group databases

    CAZyiCBM6. Carbohydrate-Binding Module Family 6.
    GH96. Glycoside Hydrolase Family 96.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-agaraseImported (EC:3.2.1.158)
    Gene namesi
    Name:agaAImported
    OrganismiAlteromonas agarilytica
    Taxonomic identifieri105692 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesAlteromonadaceaeAlteromonas

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 26261 PublicationAdd
    BLAST
    Chaini27 – 14291403Alpha-agarase1 PublicationPRO_5000055969Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliQ9LAP7.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini29 – 161133CBM6 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini211 – 345135CBM6 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini662 – 793132CBM6 3PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 96 family.Sequence Analysis
    Contains 3 CBM6 (carbohydrate binding type-6) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Family and domain databases

    Gene3Di2.60.120.260. 3 hits.
    4.10.1080.10. 2 hits.
    InterProiIPR006584. Cellulose-bd_IV.
    IPR029070. Chitinase_insertion.
    IPR005084. CMB_fam6.
    IPR008979. Galactose-bd-like.
    IPR003367. Thrombospondin_3-like_rpt.
    IPR028974. TSP_type-3_rpt.
    [Graphical view]
    PfamiPF03422. CBM_6. 3 hits.
    PF02412. TSP_3. 5 hits.
    [Graphical view]
    SMARTiSM00606. CBD_IV. 1 hit.
    [Graphical view]
    SUPFAMiSSF103647. SSF103647. 3 hits.
    SSF49785. SSF49785. 3 hits.
    SSF54556. SSF54556. 1 hit.
    PROSITEiPS51175. CBM6. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9LAP7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFKTKRSLLN SSIAISFAVL GVQAQAETLE LQAESFANSG GTYSDGQPNP     50
    VTIYNVNGQG AINFVNAGDY VDYNINALGG EYDIEYFVGT GVTSGPNIEV 100
    LVDVNGTWQS QGSVAVPYGS WDDFQSLTPS HTVTLPVGTS TVRLLAVGST 150
    WQWNLESFRL TQVSPVEPVG DADNDGVNDN QDLCPNSPSG VTVDNNGCQI 200
    TGGTDPGGES FVIQMEAFDS TGSDDSRAKG VIIGERGYPQ DKHTVVDSVQ 250
    TTDWVDYSIN FPSSANYSVS MLASGQTDHA TAVLYLDGTE INEVPVHTGS 300
    QADFANFQLA GSVYIASGTH TIRVQAQSST GEFSWLWFGD ALTFTNLDSD 350
    GGNGGEATQD ADNDGVLDSS DSCPNTPTGE PADVTGCSAS QLDDDNDGVS 400
    NNVDQCPNTV AGTEVDADGC EVIFADADND GIEDSQDFCP NTPAGEAVNN 450
    SGCGASQLDA DNDGVTNNID QCPNTPAGTQ VDASGCETDN GGEPGDSYYH 500
    NGQGLLFGRV DGATNFLGEE GYVANPDNYD VTTDLLETDD AIRANSTEVF 550
    RGEIYDADGH IAFYEHIDDS VRLYIDGQLV LSNDSWENSS QTTDLNLTPG 600
    WHNFELRLGN ADGGSGAVSG IGFGIDVDGG TNFVHPSNLS PSMFRASGQV 650
    VVDPILPPSG GIYIQLEDFD ETGTVGRVAS DPNDGFVKGD SNVGWVTNGD 700
    WGKYHNVFLE AGTYRAFITV STPAGGSYGA RVDIDGEPFA WGYFDSTGGW 750
    DIAAEYELYG GHLVVESTGN HTLHVEAVGG SDWQWSGDLV RLAKVSDSAV 800
    KQPRVYNPNE HIVAEIQGPA TGLQYLKTPV EIPLANKVLK SDVWYTYPQN 850
    RNLVVDGDTP YADFGATGAF WGHPPEHDFY DDTVIMDWAV NVVDDFQSEG 900
    FEYTARGEFD WGYGWFTEFT TNPQPHYVQT LDGRNVRMTF MGYLSHDGYN 950
    NNWLSNHSPA FVPFMKSQVD QILKANPDKL MFDTQTNSTR STDMRTFGGD 1000
    FSPYAMENFR VWLLKKYSNA QLVSMGINDI TSFDYGAYLR AQGITHTDWS 1050
    NAGDTISGNI PMMEDFIYFN RDVWNQKFAE VLEYIRQQRP NIEIGASTHL 1100
    FESRGYIFNE NITFLSGELN LGARTSISEL PTNILVHLKG AQAVDKTLAY 1150
    FPYPWEFDEL RIQNAPRFGR GWVAQAYAYG GLFSIPANVW VGGEVFTWSP 1200
    GADNYRDIYQ FVRAQANLLD GYTSYAKAGY VHAMFSSMKA GFIDGGNQVQ 1250
    SSVKILTEDN INFDMLVFGD AGYPVVPRQA DFDKFEYIFY DGDLNYLTAE 1300
    QQAVLDAQGS KVKHIGQRGT IAGLQINVSI NGSVSNETVS AVSRIHETDS 1350
    TAPYVVHLIN RPFAGGVTPI LNNVEVAIPA SYFPQGVTSA KLHLPDGSSS 1400
    TVAVSTNANG DTVVSVSNLE VWGILELAH 1429
    Length:1,429
    Mass (Da):154,671
    Last modified:October 1, 2000 - v1
    Checksum:i2ADD331171CBB5DC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti42 – 432TY → FF AA sequence (PubMed:17513582)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF121273 Genomic DNA. Translation: AAF26838.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF121273 Genomic DNA. Translation: AAF26838.1 .

    3D structure databases

    ProteinModelPortali Q9LAP7.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi CBM6. Carbohydrate-Binding Module Family 6.
    GH96. Glycoside Hydrolase Family 96.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER-16655.
    BRENDAi 3.2.1.158. 8321.

    Family and domain databases

    Gene3Di 2.60.120.260. 3 hits.
    4.10.1080.10. 2 hits.
    InterProi IPR006584. Cellulose-bd_IV.
    IPR029070. Chitinase_insertion.
    IPR005084. CMB_fam6.
    IPR008979. Galactose-bd-like.
    IPR003367. Thrombospondin_3-like_rpt.
    IPR028974. TSP_type-3_rpt.
    [Graphical view ]
    Pfami PF03422. CBM_6. 3 hits.
    PF02412. TSP_3. 5 hits.
    [Graphical view ]
    SMARTi SM00606. CBD_IV. 1 hit.
    [Graphical view ]
    SUPFAMi SSF103647. SSF103647. 3 hits.
    SSF49785. SSF49785. 3 hits.
    SSF54556. SSF54556. 1 hit.
    PROSITEi PS51175. CBM6. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Alpha-agarases define a new family of glycoside hydrolases, distinct from beta-agarase families."
      Flament D., Barbeyron T., Jam M., Potin P., Czjzek M., Kloareg B., Michel G.
      Appl. Environ. Microbiol. 73:4691-4694(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 27-43 AND 802-821.
      Strain: GJ1BImported.
    2. "Purification and characterization of the alpha-agarase from Alteromonas agarlyticus (Cataldi) comb. nov., strain GJ1B."
      Potin P., Richard C., Rochas C., Kloareg B.
      Eur. J. Biochem. 214:599-607(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.

    Entry informationi

    Entry nameiAAGAR_ALTAG
    AccessioniPrimary (citable) accession number: Q9LAP7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 5, 2010
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 46 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    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