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P0CD66

- AGLU_SULSO

UniProt

P0CD66 - AGLU_SULSO

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Protein

Alpha-glucosidase

Gene

malA

Organism
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli

Functioni

Major soluble alpha-glucosidase.By similarity

Catalytic activityi

Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-glucose residues with release of alpha-D-glucose.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei320 – 3201By similarity
Active sitei323 – 3231By similarity
Active sitei416 – 4161Proton donorBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Enzyme and pathway databases

BioCyciSSOL273057:GCH2-2839-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-glucosidase (EC:3.2.1.20)
Alternative name(s):
Maltase
Gene namesi
Name:malA
Ordered Locus Names:SSO3051
ORF Names:C23_036
OrganismiSulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Taxonomic identifieri273057 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
ProteomesiUP000001974: Chromosome

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 693693Alpha-glucosidasePRO_0000185367Add
BLAST

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 84Combined sources
Beta strandi10 – 1910Combined sources
Helixi38 – 414Combined sources
Beta strandi43 – 486Combined sources
Beta strandi51 – 577Combined sources
Beta strandi63 – 664Combined sources
Beta strandi78 – 836Combined sources
Beta strandi99 – 1013Combined sources
Beta strandi104 – 1096Combined sources
Beta strandi112 – 1187Combined sources
Beta strandi124 – 1329Combined sources
Beta strandi135 – 1439Combined sources
Beta strandi145 – 1517Combined sources
Helixi155 – 16612Combined sources
Helixi174 – 1774Combined sources
Beta strandi178 – 1825Combined sources
Helixi189 – 20113Combined sources
Beta strandi206 – 2116Combined sources
Helixi213 – 2153Combined sources
Turni226 – 2283Combined sources
Helixi232 – 24110Combined sources
Beta strandi245 – 2506Combined sources
Helixi261 – 2666Combined sources
Beta strandi276 – 2783Combined sources
Beta strandi280 – 2834Combined sources
Beta strandi286 – 2894Combined sources
Helixi296 – 31015Combined sources
Turni311 – 3133Combined sources
Beta strandi316 – 3194Combined sources
Turni322 – 3243Combined sources
Helixi328 – 33710Combined sources
Helixi348 – 3514Combined sources
Beta strandi357 – 3615Combined sources
Beta strandi364 – 3674Combined sources
Helixi368 – 3714Combined sources
Helixi372 – 3743Combined sources
Helixi375 – 38915Combined sources
Beta strandi397 – 4004Combined sources
Helixi406 – 4083Combined sources
Beta strandi411 – 4133Combined sources
Helixi421 – 43515Combined sources
Turni436 – 4383Combined sources
Beta strandi441 – 4433Combined sources
Beta strandi452 – 4554Combined sources
Helixi461 – 47010Combined sources
Turni471 – 4733Combined sources
Beta strandi477 – 4793Combined sources
Helixi490 – 4923Combined sources
Helixi495 – 52531Combined sources
Beta strandi529 – 5313Combined sources
Helixi533 – 5364Combined sources
Helixi541 – 5455Combined sources
Beta strandi550 – 5523Combined sources
Turni553 – 5553Combined sources
Beta strandi556 – 5583Combined sources
Beta strandi563 – 5675Combined sources
Beta strandi569 – 5724Combined sources
Beta strandi574 – 5796Combined sources
Turni580 – 5823Combined sources
Beta strandi585 – 5939Combined sources
Beta strandi596 – 5983Combined sources
Beta strandi600 – 61011Combined sources
Helixi611 – 6133Combined sources
Beta strandi614 – 62411Combined sources
Beta strandi630 – 6334Combined sources
Beta strandi635 – 6428Combined sources
Beta strandi644 – 6529Combined sources
Beta strandi659 – 6624Combined sources
Beta strandi667 – 6693Combined sources
Beta strandi671 – 6744Combined sources
Beta strandi677 – 69317Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2G3MX-ray2.55A/B/C/D/E/F5-693[»]
2G3NX-ray2.55A/B/C/D/E/F5-693[»]
ProteinModelPortaliP0CD66.
SMRiP0CD66. Positions 4-693.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0CD66.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 31 family.Curated

Phylogenomic databases

HOGENOMiHOG000033867.
InParanoidiP0CD66.
KOiK01187.
OMAiIIMKQAG.

Family and domain databases

Gene3Di3.20.20.70. 2 hits.
InterProiIPR013785. Aldolase_TIM.
IPR011013. Gal_mutarotase_SF_dom.
IPR000322. Glyco_hydro_31.
IPR025887. Glyco_hydro_31_N_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF13802. Gal_mutarotas_2. 1 hit.
PF01055. Glyco_hydro_31. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 2 hits.
SSF74650. SSF74650. 1 hit.
PROSITEiPS00129. GLYCOSYL_HYDROL_F31_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0CD66-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQTIKIYENK GVYKVVIGEP FPPIEFPLEQ KISSNKSLSE LGLTIVQQGN
60 70 80 90 100
KVIVEKSLDL KEHIIGLGEK AFELDRKRKR YVMYNVDAGA YKKYQDPLYV
110 120 130 140 150
SIPLFISVKD GVATGYFFNS ASKVIFDVGL EEYDKVIVTI PEDSVEFYVI
160 170 180 190 200
EGPRIEDVLE KYTELTGKPF LPPMWAFGYM ISRYSYYPQD KVVELVDIMQ
210 220 230 240 250
KEGFRVAGVF LDIHYMDSYK LFTWHPYRFP EPKKLIDELH KRNVKLITIV
260 270 280 290 300
DHGIRVDQNY SPFLSGMGKF CEIESGELFV GKMWPGTTVY PDFFREDTRE
310 320 330 340 350
WWAGLISEWL SQGVDGIWLD MNEPTDFSRA IEIRDVLSSL PVQFRDDRLV
360 370 380 390 400
TTFPDNVVHY LRGKRVKHEK VRNAYPLYEA MATFKGFRTS HRNEIFILSR
410 420 430 440 450
AGYAGIQRYA FIWTGDNTPS WDDLKLQLQL VLGLSISGVP FVGCDIGGFQ
460 470 480 490 500
GRNFAEIDNS MDLLVKYYAL ALFFPFYRSH KATDGIDTEP VFLPDYYKEK
510 520 530 540 550
VKEIVELRYK FLPYIYSLAL EASEKGHPVI RPLFYEFQDD DDMYRIEDEY
560 570 580 590 600
MVGKYLLYAP IVSKEESRLV TLPRGKWYNY WNGEIINGKS VVKSTHELPI
610 620 630 640 650
YLREGSIIPL EGDELIVYGE TSFKRYDNAE ITSSSNEIKF SREIYVSKLT
660 670 680 690
ITSEKPVSKI IVDDSKEIQV EKTMQNTYVA KINQKIRGKI NLE
Length:693
Mass (Da):80,441
Last modified:February 9, 2010 - v1
Checksum:i27BB952C0A7B3858
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006641 Genomic DNA. Translation: AAK43151.1.
PIRiH90486.
RefSeqiNP_344361.1. NC_002754.1.

Genome annotation databases

EnsemblBacteriaiAAK43151; AAK43151; SSO3051.
GeneIDi1453070.
KEGGisso:SSO3051.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006641 Genomic DNA. Translation: AAK43151.1 .
PIRi H90486.
RefSeqi NP_344361.1. NC_002754.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2G3M X-ray 2.55 A/B/C/D/E/F 5-693 [» ]
2G3N X-ray 2.55 A/B/C/D/E/F 5-693 [» ]
ProteinModelPortali P0CD66.
SMRi P0CD66. Positions 4-693.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAK43151 ; AAK43151 ; SSO3051 .
GeneIDi 1453070.
KEGGi sso:SSO3051.

Phylogenomic databases

HOGENOMi HOG000033867.
InParanoidi P0CD66.
KOi K01187.
OMAi IIMKQAG.

Enzyme and pathway databases

BioCyci SSOL273057:GCH2-2839-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0CD66.

Family and domain databases

Gene3Di 3.20.20.70. 2 hits.
InterProi IPR013785. Aldolase_TIM.
IPR011013. Gal_mutarotase_SF_dom.
IPR000322. Glyco_hydro_31.
IPR025887. Glyco_hydro_31_N_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF13802. Gal_mutarotas_2. 1 hit.
PF01055. Glyco_hydro_31. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 2 hits.
SSF74650. SSF74650. 1 hit.
PROSITEi PS00129. GLYCOSYL_HYDROL_F31_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.

Entry informationi

Entry nameiAGLU_SULSO
AccessioniPrimary (citable) accession number: P0CD66
Secondary accession number(s): O59645
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 9, 2010
Last sequence update: February 9, 2010
Last modified: November 26, 2014
This is version 34 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3