Alpha-glucosidase - Bacteroides thetaiotaomicron

Preferred order of sections

Names and origin

Protein names

Submitted name:
Alpha-glucosidase EMBL AAC44671.1

Gene names

Name:

susB EMBL AAC44671.1

Organism

Bacteroides thetaiotaomicron EMBL AAC44671.1

Taxonomic identifier

818 [NCBI]

Taxonomic lineage

Bacteria › Bacteroidetes › Bacteroidia › Bacteroidales › Bacteroidaceae › Bacteroides

Protein attributes

Sequence length	738 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Ontologies

Keywords
Ligand	Calcium PDB 2D73 PDB 2JKA PDB 2JKE PDB 2JKP PDB 2ZQ0 Metal-binding PDB 2D73 PDB 2JKA PDB 2JKE PDB 2JKP PDB 2ZQ0
Technical term	3D-structure PDB 2D73 PDB 2JKA PDB 2JKE PDB 2JKP PDB 2ZQ0
Gene Ontology (GO)
Molecular function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Sites

Metal binding

194

1

Calcium PDB 2D73 PDB 2JKA PDB 2JKE PDB 2JKP PDB 2ZQ0

Metal binding

508

1

Calcium PDB 2D73 PDB 2JKA PDB 2JKE PDB 2JKP PDB 2ZQ0

Metal binding

526

1

Calcium PDB 2D73 PDB 2JKA PDB 2JKE PDB 2JKP PDB 2ZQ0

Metal binding

532

1

Calcium PDB 2D73 PDB 2JKA PDB 2JKE PDB 2JKP PDB 2ZQ0

Sequences

Sequence

Length

Mass (Da)

Tools

P71094 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 2BFE87C3552C9A12
Show »

FASTA

738

84,378

        10         20         30         40         50         60 
MKKRKILSLI AFLCISFIAN AQQKLTSPDN NLVMTFQVDS KGAPTYELTY KNKVVIKPST 

        70         80         90        100        110        120 
LGLELKKEDN TRTDFDWVDR RDLTKLDSKT NLYDGFEVKD TQTATFDETW QPVWGEEKEI 

       130        140        150        160        170        180 
RNHYNELAVT LYQPMNDRSI VIRFRLFNDG LGFRYEFPQQ KSLNYFVIKE EHSQFGMNGD 

       190        200        210        220        230        240 
HIAFWIPGDY DTQEYDYTIS RLSEIRGLMK EAITPNSSQT PFSQTGVQTA LMMKTDDGLY 

       250        260        270        280        290        300 
INLHEAALVD YSCMHLNLDD KNMVFESWLT PDAKGDKGYM QTPCNTPWRT IIVSDDARNI 

       310        320        330        340        350        360 
LASRITLNLN EPCKIADAAS WVKPVKYIGV WWDMITGKGS WAYTDELTSV KLGETDYSKT 

       370        380        390        400        410        420 
KPNGKHSANT ANVKRYIDFA AAHGFDAVLV EGWNEGWEDW FGNSKDYVFD FVTPYPDFDV 

       430        440        450        460        470        480 
KEIHRYAARK GIKMMMHHET SASVRNYERH MDKAYQFMAD NGYNSVKSGY VGNIIPRGEH 

       490        500        510        520        530        540 
HYGQWMNNHY LYAVKKAADY KIMVNAHEAT RPTGICRTYP NLIGNESARG TEYESFGGNK 

       550        560        570        580        590        600 
VYHTTILPFT RLVGGPMDYT PGIFETHCNK MNPANNSQVR STIARQLALY VTMYSPLQMA 

       610        620        630        640        650        660 
ADIPENYERF MDAFQFIKDV ALDWDETNYL EAEPGEYITI ARKAKDTDDW YVGCTAGENG 

       670        680        690        700        710        720 
HTSKLVFDFL TPGKQYIATV YADAKDADWK ENPQAYTIKK GILTNKSKLN LHAANGGGYA 

       730 
ISIKEVKDKS EAKGLKRL

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References

[1]	"Contribution of a neopullulanase, a pullulanase, and an alpha-glucosidase to growth of Bacteroides thetaiotaomicron on starch." D'Elia J.N., Salyers A.A. J. Bacteriol. 178:7173-7179(1996) [PubMed: 8955399] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: 5482 EMBL AAC44671.1.
[2]	D'Elia J., Salyers A. Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: 5482 EMBL AAC44671.1.
[3]	"Structural and functional analysis of a glycoside hydrolase family 97 enzyme from Bacteroides thetaiotaomicron." Kitamura M., Okuyama M., Tanzawa F., Mori H., Kitago Y., Watanabe N., Kimura A., Tanaka I., Yao M. J. Biol. Chem. 283:36328-36337(2008) [PubMed: 18981178] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 22-738 IN COMPLEX WITH CALCIUM.
[4]	"Divergence of catalytic mechanism within a glycosidase family provides insight into evolution of carbohydrate metabolism by human gut flora." Gloster T.M., Turkenburg J.P., Potts J.R., Henrissat B., Davies G.J. Chem. Biol. 15:1058-1067(2008) [PubMed: 18848471] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 22-738 IN COMPLEX WITH CALCIUM.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U66897 Genomic DNA. Translation: AAC44671.1.

RefSeq

NP_812614.1. NC_004663.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2D73	X-ray	1.60	A/B	22-738	[»]
2JKA	X-ray	1.90	A/B	22-738	[»]
2JKE	X-ray	1.70	A/B	22-738	[»]
2JKP	X-ray	1.99	A/B	22-738	[»]
2ZQ0	X-ray	1.60	A/B	22-738	[»]

ProteinModelPortal

P71094.

SMR

P71094. Positions 22-738.

ModBase

Search...

Protein family/group databases

CAZy

GH97. Glycoside Hydrolase Family 97.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

1072064.

GenomeReviews

Gene locus BT_3703 in contig AE015928_GR.

KEGG

bth:BT_3703.

NMPDR

fig|226186.1.peg.3701.

PATRIC

21062407. VBIBacThe70966_3763.

Phylogenomic databases

HOGENOM

HBG612373.

OMA

ANVKRYI.

PhylomeDB

P71094.

ProtClustDB

CLSK903536.

Family and domain databases

InterPro

IPR019563. Glycoside_hydrolase_97.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]

Pfam

PF10566. Glyco_hydro_97. 1 hit.
[Graphical view]

SUPFAM

SSF51445. Glyco_hydro_cat. 1 hit.

ProtoNet

Search...

Entry information

Entry name

P71094_BACT4

Accession

Primary (citable) accession number: P71094
Secondary accession number(s): Q7C3Z2

Entry history

Integrated into UniProtKB/TrEMBL:	February 1, 1997
Last sequence update:	February 1, 1997
Last modified:	January 25, 2012
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)