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P29761

- AMYG_CLOS0

UniProt

P29761 - AMYG_CLOS0

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Protein

Glucoamylase

Gene

cga

Organism
Clostridium sp. (strain G0005)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

CGA has typical kinetic properties for a glucoamylase, but this bacterial enzyme had higher isomaltose-hydrolyzing activity than other eukaryotic glucoamylases.

Catalytic activityi

Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei342 – 3421SubstrateBy similarity
Active sitei452 – 4521Proton acceptorPROSITE-ProRule annotation
Active sitei455 – 4551Proton donorPROSITE-ProRule annotation

GO - Molecular functioni

  1. carbohydrate binding Source: InterPro
  2. glucan 1,4-alpha-glucosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. polysaccharide catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation

Enzyme and pathway databases

SABIO-RKP29761.

Protein family/group databases

CAZyiGH15. Glycoside Hydrolase Family 15.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucoamylase (EC:3.2.1.3)
Alternative name(s):
1,4-alpha-D-glucan glucohydrolase
Glucan 1,4-alpha-glucosidase
Gene namesi
Name:cga
OrganismiClostridium sp. (strain G0005)
Taxonomic identifieri72582 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Subcellular locationi

GO - Cellular componenti

  1. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121PROSITE-ProRule annotationAdd
BLAST
Chaini22 – 702681GlucoamylasePRO_0000001481Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi22 – 221N-palmitoyl cysteineCurated
Lipidationi22 – 221S-diacylglycerol cysteineCurated

Keywords - PTMi

Lipoprotein, Palmitate

Structurei

3D structure databases

ProteinModelPortaliP29761.
SMRiP29761. Positions 28-701.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 15 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di1.50.10.10. 1 hit.
2.70.98.10. 1 hit.
InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR011013. Gal_mutarotase_SF_dom.
IPR000165. Glucoamylase.
IPR006425. Glucoamylase_bac.
IPR015220. Glucodextran_N.
IPR014718. Glyco_hydro-type_carb-bd_sub.
IPR011613. Glyco_hydro_15.
[Graphical view]
PfamiPF09137. Glucodextran_N. 1 hit.
PF00723. Glyco_hydro_15. 1 hit.
[Graphical view]
SUPFAMiSSF48208. SSF48208. 1 hit.
SSF74650. SSF74650. 1 hit.
TIGRFAMsiTIGR01535. glucan_glucosid. 1 hit.
PROSITEiPS00820. GLUCOAMYLASE. 1 hit.
PS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P29761-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSRKLIKYLP LLVLASSVLS GCSNNVSSIK IDRFNNISAV NGPGEEDTWA
60 70 80 90 100
SAQKQGVGTA NNYVSKVWFT LANGAISEVY YPTIDTADVK EIKFIVTDGK
110 120 130 140 150
SFVSDETKDT ISKVEKFTDK SLGYKLVNTD KKGRYRITKE IFTDVKRNSL
160 170 180 190 200
IMKAKFEALE GSIHDYKLYL AYDPHIKNQG SYNEGYVIKA NNNEMLMAKR
210 220 230 240 250
DNVYTALSSN IGWKGYSIGY YKVNDIMTDL DENKQMTKHY DSARGNIIEG
260 270 280 290 300
AEIDLKKNSQ FEIVLSFGNS EDEAVKASIE TLSENYDSLK SAYIDEWEKY
310 320 330 340 350
CNSLNNFNGK ANSLYYNSMM ILKASEDKTN KGAYIASLSI PWGDGQGDDN
360 370 380 390 400
TGGYHLVWSR DLYHVANAFI AAGDVDSANR SLDYLAKVVK DNGMIPQNTW
410 420 430 440 450
ISGKPYWTGI QLDEQADPII LSYRLRRYDL YDSLVKPLAD FIIKMGPKTG
460 470 480 490 500
QERWEEIGGY SPATMAAEVA GLTCAAYIAE QNKDYESAQK YQEKADNWQK
510 520 530 540 550
LIDNLTYTEH GPLENGQYYI RIAGLPDPNA DFTISIANGG GVYDQKEIVD
560 570 580 590 600
PSFLELVRLG VKSPDDPKIL NTLRVVDSTI KVDTPKGPSW YRYNHDGYGE
610 620 630 640 650
PSKTELYHGA GKGRLWPLLT GERGMYEIAA GKDATPYLKA MENFANEGGI
660 670 680 690 700
ISEQVWEDTG LPTDSASPLN WAHAEYVVLF PSNIEHKVLD MPDIVYKRYV

AK
Length:702
Mass (Da):78,658
Last modified:April 1, 1993 - v1
Checksum:i955EB4D0AD569546
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D12818 Genomic DNA. Translation: BAA02251.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D12818 Genomic DNA. Translation: BAA02251.1 .

3D structure databases

ProteinModelPortali P29761.
SMRi P29761. Positions 28-701.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH15. Glycoside Hydrolase Family 15.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

SABIO-RK P29761.

Family and domain databases

Gene3Di 1.50.10.10. 1 hit.
2.70.98.10. 1 hit.
InterProi IPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR011013. Gal_mutarotase_SF_dom.
IPR000165. Glucoamylase.
IPR006425. Glucoamylase_bac.
IPR015220. Glucodextran_N.
IPR014718. Glyco_hydro-type_carb-bd_sub.
IPR011613. Glyco_hydro_15.
[Graphical view ]
Pfami PF09137. Glucodextran_N. 1 hit.
PF00723. Glyco_hydro_15. 1 hit.
[Graphical view ]
SUPFAMi SSF48208. SSF48208. 1 hit.
SSF74650. SSF74650. 1 hit.
TIGRFAMsi TIGR01535. glucan_glucosid. 1 hit.
PROSITEi PS00820. GLUCOAMYLASE. 1 hit.
PS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Molecular cloning of a glucoamylase gene from a thermophilic Clostridium and kinetics of the cloned enzyme."
    Ohnishi H., Kitamura H., Minowa T., Sakai H., Ohta T.
    Eur. J. Biochem. 207:413-418(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.

Entry informationi

Entry nameiAMYG_CLOS0
AccessioniPrimary (citable) accession number: P29761
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: October 29, 2014
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

High activity towards 1,6-glycosidic bonds.

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