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Q9LAP7 (AAGAR_ALTAG) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-agarase

EC=3.2.1.158
Gene names
Name:agaA
OrganismAlteromonas agarilytica
Taxonomic identifier105692 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesAlteromonadaceaeAlteromonas

Protein attributes

Sequence length1429 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Alpha-agarase. Does not hydrolyze agarotetraose, agarohexaose, kappa-carrageenan, iota-carrageenan or lambda-carrageenan. Ref.2

Catalytic activity

Endohydrolysis of 1,3-alpha-L-galactosidic linkages in agarose, yielding agarotetraose as the major product. Ref.2

Cofactor

Calcium. Ref.2

Subunit structure

Homodimer. Ref.2

Sequence similarities

Belongs to the glycosyl hydrolase 96 family.

Contains 3 CBM6 (carbohydrate binding type-6) domains.

Biophysicochemical properties

pH dependence:

Optimum pH is 7.2. Active between pH 6.0 and 9.0. Ref.2

Temperature dependence:

Inactive above 60 degrees Celsius. Ref.2

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Ref.1
Chain27 – 14291403Alpha-agarase Ref.1
PRO_5000055969

Regions

Domain29 – 161133CBM6 1
Domain211 – 345135CBM6 2
Domain662 – 793132CBM6 3

Experimental info

Sequence conflict42 – 432TY → FF AA sequence Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9LAP7 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 2ADD331171CBB5DC

FASTA1,429154,671
        10         20         30         40         50         60 
MFKTKRSLLN SSIAISFAVL GVQAQAETLE LQAESFANSG GTYSDGQPNP VTIYNVNGQG 

        70         80         90        100        110        120 
AINFVNAGDY VDYNINALGG EYDIEYFVGT GVTSGPNIEV LVDVNGTWQS QGSVAVPYGS 

       130        140        150        160        170        180 
WDDFQSLTPS HTVTLPVGTS TVRLLAVGST WQWNLESFRL TQVSPVEPVG DADNDGVNDN 

       190        200        210        220        230        240 
QDLCPNSPSG VTVDNNGCQI TGGTDPGGES FVIQMEAFDS TGSDDSRAKG VIIGERGYPQ 

       250        260        270        280        290        300 
DKHTVVDSVQ TTDWVDYSIN FPSSANYSVS MLASGQTDHA TAVLYLDGTE INEVPVHTGS 

       310        320        330        340        350        360 
QADFANFQLA GSVYIASGTH TIRVQAQSST GEFSWLWFGD ALTFTNLDSD GGNGGEATQD 

       370        380        390        400        410        420 
ADNDGVLDSS DSCPNTPTGE PADVTGCSAS QLDDDNDGVS NNVDQCPNTV AGTEVDADGC 

       430        440        450        460        470        480 
EVIFADADND GIEDSQDFCP NTPAGEAVNN SGCGASQLDA DNDGVTNNID QCPNTPAGTQ 

       490        500        510        520        530        540 
VDASGCETDN GGEPGDSYYH NGQGLLFGRV DGATNFLGEE GYVANPDNYD VTTDLLETDD 

       550        560        570        580        590        600 
AIRANSTEVF RGEIYDADGH IAFYEHIDDS VRLYIDGQLV LSNDSWENSS QTTDLNLTPG 

       610        620        630        640        650        660 
WHNFELRLGN ADGGSGAVSG IGFGIDVDGG TNFVHPSNLS PSMFRASGQV VVDPILPPSG 

       670        680        690        700        710        720 
GIYIQLEDFD ETGTVGRVAS DPNDGFVKGD SNVGWVTNGD WGKYHNVFLE AGTYRAFITV 

       730        740        750        760        770        780 
STPAGGSYGA RVDIDGEPFA WGYFDSTGGW DIAAEYELYG GHLVVESTGN HTLHVEAVGG 

       790        800        810        820        830        840 
SDWQWSGDLV RLAKVSDSAV KQPRVYNPNE HIVAEIQGPA TGLQYLKTPV EIPLANKVLK 

       850        860        870        880        890        900 
SDVWYTYPQN RNLVVDGDTP YADFGATGAF WGHPPEHDFY DDTVIMDWAV NVVDDFQSEG 

       910        920        930        940        950        960 
FEYTARGEFD WGYGWFTEFT TNPQPHYVQT LDGRNVRMTF MGYLSHDGYN NNWLSNHSPA 

       970        980        990       1000       1010       1020 
FVPFMKSQVD QILKANPDKL MFDTQTNSTR STDMRTFGGD FSPYAMENFR VWLLKKYSNA 

      1030       1040       1050       1060       1070       1080 
QLVSMGINDI TSFDYGAYLR AQGITHTDWS NAGDTISGNI PMMEDFIYFN RDVWNQKFAE 

      1090       1100       1110       1120       1130       1140 
VLEYIRQQRP NIEIGASTHL FESRGYIFNE NITFLSGELN LGARTSISEL PTNILVHLKG 

      1150       1160       1170       1180       1190       1200 
AQAVDKTLAY FPYPWEFDEL RIQNAPRFGR GWVAQAYAYG GLFSIPANVW VGGEVFTWSP 

      1210       1220       1230       1240       1250       1260 
GADNYRDIYQ FVRAQANLLD GYTSYAKAGY VHAMFSSMKA GFIDGGNQVQ SSVKILTEDN 

      1270       1280       1290       1300       1310       1320 
INFDMLVFGD AGYPVVPRQA DFDKFEYIFY DGDLNYLTAE QQAVLDAQGS KVKHIGQRGT 

      1330       1340       1350       1360       1370       1380 
IAGLQINVSI NGSVSNETVS AVSRIHETDS TAPYVVHLIN RPFAGGVTPI LNNVEVAIPA 

      1390       1400       1410       1420 
SYFPQGVTSA KLHLPDGSSS TVAVSTNANG DTVVSVSNLE VWGILELAH 

« Hide

References

[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: GJ1B.
[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF121273 Genomic DNA. Translation: AAF26838.1.

3D structure databases

ProteinModelPortalQ9LAP7.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM6. Carbohydrate-Binding Module Family 6.
GH96. Glycoside Hydrolase Family 96.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-16655.
BRENDA3.2.1.158. 8321.

Family and domain databases

Gene3D2.60.120.260. 3 hits.
4.10.1080.10. 2 hits.
InterProIPR006584. 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]
PfamPF03422. CBM_6. 3 hits.
PF02412. TSP_3. 5 hits.
[Graphical view]
SMARTSM00606. CBD_IV. 1 hit.
[Graphical view]
SUPFAMSSF103647. SSF103647. 3 hits.
SSF49785. SSF49785. 3 hits.
SSF54556. SSF54556. 1 hit.
PROSITEPS51175. CBM6. 3 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAAGAR_ALTAG
AccessionPrimary (citable) accession number: Q9LAP7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: October 1, 2000
Last modified: June 11, 2014
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries