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A1IGV8

- AAGAR_THASX

UniProt

A1IGV8 - AAGAR_THASX

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Protein

Alpha-agarase

Gene
agaA33
Organism
Thalassomonas agarivorans
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

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

Cofactori

Calcium.1 Publication

pH dependencei

Optimum pH is 8.5. Active between pH 4.5 and 9.5, stable between pH 6.5 and 10.5.2 Publications

Temperature dependencei

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

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
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16654.
BRENDAi3.2.1.158. 8322.

Protein family/group databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-agarase (EC:3.2.1.158)
Alternative name(s):
AgaraseA33
Gene namesi
Name:agaA33
OrganismiThalassomonas agarivorans
Taxonomic identifieri349064 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesColwelliaceaeThalassomonas

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727 Reviewed predictionAdd
BLAST
Propeptidei28 – 6846571 PublicationPRO_0000397928Add
BLAST
Chaini685 – 1463779Alpha-agarase1 PublicationPRO_0000397929Add
BLAST

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

3D structure databases

ProteinModelPortaliA1IGV8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini701 – 832132CBM6Add
BLAST

Sequence similaritiesi

Belongs to the glycosyl hydrolase 96 family.By similarity

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.120.260. 3 hits.
3.90.182.10. 1 hit.
4.10.1080.10. 2 hits.
InterProiIPR005084. CMB_fam6.
IPR008979. Galactose-bd-like.
IPR011658. PA14.
IPR003367. Thrombospondin_3-like_rpt.
IPR028974. TSP_type-3_rpt.
[Graphical view]
PfamiPF03422. CBM_6. 1 hit.
PF02412. TSP_3. 6 hits.
[Graphical view]
SUPFAMiSSF103647. SSF103647. 2 hits.
SSF49785. SSF49785. 3 hits.
PROSITEiPS51175. CBM6. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

A1IGV8-1 [UniParc]FASTAAdd to Basket

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MITSSKKIVS AMLSTSLWIG VASAAYAETT NVEAEGYSTI GGTYQDGNPQ     50
PINIYSVNGV QAINFVNRGD FAEYDVSVST AGEYSIEYLI GTSIASGSAV 100
EISVLVDGNW QSAGSTNVPL GQWDNFQALA ANNNISLAQG TNRIKITGAG 150
THDWQWNLDA FSLTLVTPEN PDNPDNPDNP DDGNTGQPGT PFTIEMEAFD 200
ATGSDDPRAQ GMVIGERGYP EDKHTVVDSN QTTDWVDYNI NFPVSGNYRI 250
EMLASGQTSH ATAILFVDNV QINEVAVDTG NQAVFLDFEL TDSTYISAGA 300
HTIRVQSGSQ INEFSWMWFG DALTFTPLDG GSTDGDADND GVLDSVDTCP 350
NTPAGAQVDA NGCEIIVDND TDNDGVDNSI DQCPNTPAGA QVDANGCEIV 400
AVVDADNDGV EDSLDMCPNT PAGAPVNGQG CADSQLDADN DGVSDDIDQC 450
PSTPAGSVVD GTGCIVVTPP ADSDNDGVVD TLDMCPNTAA GLTVDSQGCA 500
LSQLDSDNDG VTDDIDQCAN TPSGETANAT GCSSSQEGGG TDPDTPQPGL 550
LYGELAGAMN VSDTNPNWER TTDLLQTEDS VKGNTTEVYT GFIYDADGHI 600
SFYEHIDDSV RLYIDGVLVL SNDSWEASSQ TTDLNLTPGT HEIELRIGNA 650
DGGSGAVDGI GFGIDVDGGT NFVHPSTLSE SIFTSVGEET GNPDLEQEGD 700
IIVELESFVF TSTNGRVGSD SVEGFSPTAT GVNWVTNGDY GDYMVTFEEP 750
GTYGAYITIS AANDGSYGAR VDVDGWPVAW GYFGGTGSWD VSSENLLYGG 800
TFVVEQAGEK VVRVEAIGGS DWQWSGDRVR FTRLGDVTAI PSPIYNPDDH 850
FVAEIQGPQT DVTYLKKPVE IPANKKVLKS DVWYTYPQNR ELEGYDNFGA 900
TGAFWGHPPE HDFYDDTVIM DWAVDAVYAF QAEGYEYTAR GEFDWGYGWF 950
TEYTTNPQPH YVRTLDDRNV RMTFMGYLSH DGYNNNWLSN HSPAFVPFMK 1000
SQVDQILKAN PDKLMFDTQT NSTRSTDMRD FGGDFSPYAM ENFRVWLSKK 1050
YSTGELAALG INDINSFDYG DFLRAQGVTH TSWSNAGDTL SGNIPLQEDY 1100
IYFNRDVWNQ KFAEVLDYIR QQQPDIEIGA STHLFESRGY VFNENLTFLS 1150
GELNLGARTT ISELPTNILV HLKGAQAVDK TLVYFPYPWE FDELRLQDAP 1200
RFGRGWVAQA YAYGGLFSIP ANVWVGGEVW TWSPGADNYR DIYLFVRAQA 1250
DLLDDYTSYS KVGLVHAMYS SMKAGFIDGG NQIQSSTKLL TEGNINFDLL 1300
VFGDEGYPVV PRPEDFDKFD HIFFDGDEQY LTAEQQALLD QQGDKVRHIG 1350
QRGTVSGIEI TVSISGTESN ETVSAVSRIH ETDAAAPYVV HLVNRPFAGG 1400
VTPTLNNVEV AIPQSYFPEV VTGATLHLPD GTSTSLTLST NADGDVVLPV 1450
NNLEVWGILE LAH 1463
Length:1,463
Mass (Da):158,250
Last modified:February 6, 2007 - v1
Checksum:iADCB23F68C299BEC
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB211981 Genomic DNA. Translation: BAF44076.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB211981 Genomic DNA. Translation: BAF44076.1 .

3D structure databases

ProteinModelPortali A1IGV8.
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-16654.
BRENDAi 3.2.1.158. 8322.

Family and domain databases

Gene3Di 2.60.120.260. 3 hits.
3.90.182.10. 1 hit.
4.10.1080.10. 2 hits.
InterProi IPR005084. CMB_fam6.
IPR008979. Galactose-bd-like.
IPR011658. PA14.
IPR003367. Thrombospondin_3-like_rpt.
IPR028974. TSP_type-3_rpt.
[Graphical view ]
Pfami PF03422. CBM_6. 1 hit.
PF02412. TSP_3. 6 hits.
[Graphical view ]
SUPFAMi SSF103647. SSF103647. 2 hits.
SSF49785. SSF49785. 3 hits.
PROSITEi PS51175. CBM6. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiAAGAR_THASX
AccessioniPrimary (citable) accession number: A1IGV8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: February 6, 2007
Last modified: June 11, 2014
This is version 28 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

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