Pullulanase precursor - Thermotoga maritima

Preferred order of sections

Names and origin

Protein names

Recommended name:
Pullulanase
EC=3.2.1.41

Alternative name(s):
Alpha-dextrin endo-1,6-alpha-glucosidase
Pullulan 6-glucanohydrolase

Gene names

Name:	pulA
Ordered Locus Names:	TM_1845

Organism

Thermotoga maritima

Taxonomic identifier

2336 [NCBI]

Taxonomic lineage

Bacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga

Protein attributes

Sequence length	843 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	Hydrolysis of (1->6)-alpha-D-glucosidic linkages in pullulan, amylopectin and glycogen, and in the alpha- and beta-limit dextrins of amylopectin and glycogen.
Sequence similarities	Belongs to the glycosyl hydrolase 13 family.

Ontologies

Keywords
Domain	Signal
Molecular function	Glycosidase Hydrolase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	carbohydrate binding Inferred from electronic annotation. Source: InterPro cation binding Inferred from electronic annotation. Source: InterPro pullulanase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

19

Potential

Chain

20 – 843

824

Pullulanase

PRO_0000001428

Sites

Active site

535

1

Nucleophile By similarity

Active site

564

1

Proton donor By similarity

Site

652

1

Transition state stabilizer By similarity

Secondary structure

1

.

843

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

O33840 [UniParc].

Last modified June 1, 1998. Version 2.
Checksum: C42DDE233D54FE77
Show »

FASTA

843

96,262

        10         20         30         40         50         60 
MKTKLWLLLV LLLSALIFSE TTIVVHYHRY DGKYDGWNLW IWPVEPVSQE GKAYQFTGED 

        70         80         90        100        110        120 
DFGKVAVVKL PMDLTKVGII VRLNEWQAKD VAKDRFIEIK DGKAEVWILQ GVEEIFYEKP 

       130        140        150        160        170        180 
DTSPRIFFAQ ARSNKVIEAF LTNPVDTKKK ELFKVTVDGK EIPVSRVEKA DPTDIDVTNY 

       190        200        210        220        230        240 
VRIVLSESLK EEDLRKDVEL IIEGYKPARV IMMEILDDYY YDGELGAVYS PEKTIFRVWS 

       250        260        270        280        290        300 
PVSKWVKVLL FKNGEDTEPY QVVNMEYKGN GVWEAVVEGD LDGVFYLYQL ENYGKIRTTV 

       310        320        330        340        350        360 
DPYSKAVYAN SKKSAVVNLA RTNPEGWEND RGPKIEGYED AIIYEIHIAD ITGLENSGVK 

       370        380        390        400        410        420 
NKGLYLGLTE ENTKGPGGVT TGLSHLVELG VTHVHILPFF DFYTGDELDK DFEKYYNWGY 

       430        440        450        460        470        480 
DPYLFMVPEG RYSTDPKNPH TRIREVKEMV KALHKHGIGV IMDMVFPHTY GIGELSAFDQ 

       490        500        510        520        530        540 
TVPYYFYRID KTGAYLNESG CGNVIASERP MMRKFIVDTV TYWVKEYHID GFRFDQMGLI 

       550        560        570        580        590        600 
DKKTMLEVER ALHKIDPTII LYGEPWGGWG APIRFGKSDV AGTHVAAFND EFRDAIRGSV 

       610        620        630        640        650        660 
FNPSVKGFVM GGYGKETKIK RGVVGSINYD GKLIKSFALD PEETINYAAC HDNHTLWDKN 

       670        680        690        700        710        720 
YLAAKADKKK EWTEEELKNA QKLAGAILLT SQGVPFLHGG QDFCRTKNFN DNSYNAPISI 

       730        740        750        760        770        780 
NGFDYERKLQ FIDVFNYHKG LIKLRKEHPA FRLKNAEEIK KHLEFLPGGR RIVAFMLKDH 

       790        800        810        820        830        840 
AGGDPWKDIV VIYNGNLEKT TYKLPEGKWN VVVNSQKAGT EVIETVEGTI ELDPLSAYVL 


YRE

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and analysis of genes for amylolytic enzymes of the hyperthermophilic bacterium Thermotoga maritima." Bibel M., Brettl C., Gosslar U., Kriegshaeuser G., Liebl W. FEMS Microbiol. Lett. 158:9-15(1998) [PubMed: 9453151] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[2]	"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima." Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. Fraser C.M. Nature 399:323-329(1999) [PubMed: 10360571] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ001087 Genomic DNA. Translation: CAA04522.1.
AE000512 Genomic DNA. Translation: AAD36907.1.

PIR

H72204.

RefSeq

NP_229641.1. NC_000853.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2J71	X-ray	1.69	A	20-120	[»]
2J72	X-ray	1.49	A/B	20-120	[»]
2J73	X-ray	1.40	A/B	20-120	[»]

ProteinModelPortal

O33840.

SMR

O33840. Positions 18-120.

ModBase

Search...

Protein family/group databases

CAZy

CBM41. Carbohydrate-Binding Module Family 41.
CBM48. Carbohydrate-Binding Module Family 48.
GH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

897812.

GenomeReviews

Gene locus TM_1845 in contig AE000512_GR.

KEGG

tma:TM1845.

NMPDR

fig|243274.1.peg.1825.

PATRIC

23938679. VBITheMar51294_1866.

TIGR

TM_1845.

Phylogenomic databases

HOGENOM

HBG697609.

OMA

MHKLSSS.

PhylomeDB

O33840.

ProtClustDB

CLSK2300390.

Enzyme and pathway databases

BioCyc

TMAR243274:TM_1845-MONOMER.

Family and domain databases

InterPro

IPR015902. Alpha_amylase.
IPR006047. Glyco_hydro_13_cat_dom.
IPR004193. Glyco_hydro_13_N.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR005323. PUD.
IPR011840. PulA_typeI.
[Graphical view]

Gene3D

G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
G3DSA:2.60.40.10. Ig-like_fold. 1 hit.

KO

K01200.

PANTHER

PTHR10357. Alpha_amylase. 1 hit.

Pfam

PF00128. Alpha-amylase. 2 hits.
PF02922. CBM_48. 1 hit.
PF03714. PUD. 1 hit.
[Graphical view]

SUPFAM

SSF51445. Glyco_hydro_cat. 1 hit.
SSF81296. Ig_E-set. 1 hit.

TIGRFAMs

TIGR02104. PulA_typeI. 1 hit.

ProtoNet

Search...

Entry information

Entry name

PULA_THEMA

Accession

Primary (citable) accession number: O33840

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	June 1, 1998
Last modified:	January 25, 2012
This is version 97 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families