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A1IGV8 (AAGAR_THASX) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 27. 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
Alternative name(s):
AgaraseA33
Gene names
Name:agaA33
OrganismThalassomonas agarivorans
Taxonomic identifier349064 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesColwelliaceaeThalassomonas

Protein attributes

Sequence length1463 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. Hydrolyzes agarose, agarohexaose, neoagarohexaose and porphyran. Hydrolysis of porphyran by this enzyme improves its antioxidant activity. Does not hydrolyze kappa-carrageenan, iota-carrageenen or lambda-carrageenan. Ref.1 Ref.2

Catalytic activity

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

Cofactor

Calcium. Ref.2

Subunit structure

Monomer. Ref.2

Sequence similarities

Belongs to the glycosyl hydrolase 96 family. UniProtKB Q9LAP7

Contains 1 CBM6 (carbohydrate binding type-6) domain.

Biophysicochemical properties

pH dependence:

Optimum pH is 8.5. Active between pH 4.5 and 9.5, stable between pH 6.5 and 10.5. Ref.1 Ref.2

Temperature dependence:

Optimum temperature is 45 degrees Celsius. Stable up to 40 degrees Celsius. Ref.1 Ref.2

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Potential
Propeptide28 – 684657 Ref.1
PRO_0000397928
Chain685 – 1463779Alpha-agarase Ref.1
PRO_0000397929

Regions

Domain701 – 832132CBM6

Sequences

Sequence LengthMass (Da)Tools
A1IGV8 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: ADCB23F68C299BEC

FASTA1,463158,250
        10         20         30         40         50         60 
MITSSKKIVS AMLSTSLWIG VASAAYAETT NVEAEGYSTI GGTYQDGNPQ PINIYSVNGV 

        70         80         90        100        110        120 
QAINFVNRGD FAEYDVSVST AGEYSIEYLI GTSIASGSAV EISVLVDGNW QSAGSTNVPL 

       130        140        150        160        170        180 
GQWDNFQALA ANNNISLAQG TNRIKITGAG THDWQWNLDA FSLTLVTPEN PDNPDNPDNP 

       190        200        210        220        230        240 
DDGNTGQPGT PFTIEMEAFD ATGSDDPRAQ GMVIGERGYP EDKHTVVDSN QTTDWVDYNI 

       250        260        270        280        290        300 
NFPVSGNYRI EMLASGQTSH ATAILFVDNV QINEVAVDTG NQAVFLDFEL TDSTYISAGA 

       310        320        330        340        350        360 
HTIRVQSGSQ INEFSWMWFG DALTFTPLDG GSTDGDADND GVLDSVDTCP NTPAGAQVDA 

       370        380        390        400        410        420 
NGCEIIVDND TDNDGVDNSI DQCPNTPAGA QVDANGCEIV AVVDADNDGV EDSLDMCPNT 

       430        440        450        460        470        480 
PAGAPVNGQG CADSQLDADN DGVSDDIDQC PSTPAGSVVD GTGCIVVTPP ADSDNDGVVD 

       490        500        510        520        530        540 
TLDMCPNTAA GLTVDSQGCA LSQLDSDNDG VTDDIDQCAN TPSGETANAT GCSSSQEGGG 

       550        560        570        580        590        600 
TDPDTPQPGL LYGELAGAMN VSDTNPNWER TTDLLQTEDS VKGNTTEVYT GFIYDADGHI 

       610        620        630        640        650        660 
SFYEHIDDSV RLYIDGVLVL SNDSWEASSQ TTDLNLTPGT HEIELRIGNA DGGSGAVDGI 

       670        680        690        700        710        720 
GFGIDVDGGT NFVHPSTLSE SIFTSVGEET GNPDLEQEGD IIVELESFVF TSTNGRVGSD 

       730        740        750        760        770        780 
SVEGFSPTAT GVNWVTNGDY GDYMVTFEEP GTYGAYITIS AANDGSYGAR VDVDGWPVAW 

       790        800        810        820        830        840 
GYFGGTGSWD VSSENLLYGG TFVVEQAGEK VVRVEAIGGS DWQWSGDRVR FTRLGDVTAI 

       850        860        870        880        890        900 
PSPIYNPDDH FVAEIQGPQT DVTYLKKPVE IPANKKVLKS DVWYTYPQNR ELEGYDNFGA 

       910        920        930        940        950        960 
TGAFWGHPPE HDFYDDTVIM DWAVDAVYAF QAEGYEYTAR GEFDWGYGWF TEYTTNPQPH 

       970        980        990       1000       1010       1020 
YVRTLDDRNV RMTFMGYLSH DGYNNNWLSN HSPAFVPFMK SQVDQILKAN PDKLMFDTQT 

      1030       1040       1050       1060       1070       1080 
NSTRSTDMRD FGGDFSPYAM ENFRVWLSKK YSTGELAALG INDINSFDYG DFLRAQGVTH 

      1090       1100       1110       1120       1130       1140 
TSWSNAGDTL SGNIPLQEDY IYFNRDVWNQ KFAEVLDYIR QQQPDIEIGA STHLFESRGY 

      1150       1160       1170       1180       1190       1200 
VFNENLTFLS GELNLGARTT ISELPTNILV HLKGAQAVDK TLVYFPYPWE FDELRLQDAP 

      1210       1220       1230       1240       1250       1260 
RFGRGWVAQA YAYGGLFSIP ANVWVGGEVW TWSPGADNYR DIYLFVRAQA DLLDDYTSYS 

      1270       1280       1290       1300       1310       1320 
KVGLVHAMYS SMKAGFIDGG NQIQSSTKLL TEGNINFDLL VFGDEGYPVV PRPEDFDKFD 

      1330       1340       1350       1360       1370       1380 
HIFFDGDEQY LTAEQQALLD QQGDKVRHIG QRGTVSGIEI TVSISGTESN ETVSAVSRIH 

      1390       1400       1410       1420       1430       1440 
ETDAAAPYVV HLVNRPFAGG VTPTLNNVEV AIPQSYFPEV VTGATLHLPD GTSTSLTLST 

      1450       1460 
NADGDVVLPV NNLEVWGILE LAH 

« Hide

References

[1]"Hyperproduction and application of alpha-agarase to enzymatic enhancement of antioxidant activity of porphyran."
Hatada Y., Ohta Y., Horikoshi K.
J. Agric. Food Chem. 54:9895-9900(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 685-696; 1181-1188 AND 1291-1298, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: JAMB-A33.
[2]"Purification and characterization of a novel alpha-agarase from a Thalassomonas sp."
Ohta Y., Hatada Y., Miyazaki M., Nogi Y., Ito S., Horikoshi K.
Curr. Microbiol. 50:212-216(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1289-1298, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
Strain: JAMB-A33.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB211981 Genomic DNA. Translation: BAF44076.1.

3D structure databases

ProteinModelPortalA1IGV8.
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-16654.
BRENDA3.2.1.158. 8322.

Family and domain databases

Gene3D2.60.120.260. 3 hits.
3.90.182.10. 1 hit.
InterProIPR005084. CMB_fam6.
IPR008979. Galactose-bd-like.
IPR011658. PA14.
IPR003367. Thrombospondin_3-like_rpt.
[Graphical view]
PfamPF03422. CBM_6. 1 hit.
PF02412. TSP_3. 6 hits.
[Graphical view]
SUPFAMSSF49785. SSF49785. 3 hits.
PROSITEPS51175. CBM6. 3 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAAGAR_THASX
AccessionPrimary (citable) accession number: A1IGV8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: February 6, 2007
Last modified: October 16, 2013
This is version 27 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