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P36905

- APU_THESA

UniProt

P36905 - APU_THESA

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Protein
Amylopullulanase
Gene
apu
Organism
Thermoanaerobacterium saccharolyticum
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Catalytic activityi

Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.
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.

Cofactori

Binds 1 calcium ion per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi401 – 4011Calcium By similarity
Metal bindingi403 – 4031Calcium; via carbonyl oxygen By similarity
Metal bindingi406 – 4061Calcium By similarity
Metal bindingi407 – 4071Calcium By similarity
Metal bindingi452 – 4521Calcium; via carbonyl oxygen By similarity
Metal bindingi454 – 4541Calcium By similarity
Binding sitei527 – 5271Substrate By similarity
Binding sitei627 – 6271Substrate By similarity
Active sitei629 – 6291Nucleophile By similarity
Active sitei658 – 6581Proton donor By similarity
Sitei735 – 7351Transition state stabilizer By similarity
Binding sitei798 – 7981Substrate By similarity

GO - Molecular functioni

  1. alpha-amylase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW
  3. pullulanase activity Source: UniProtKB-EC
Complete GO annotation...

GO - Biological processi

  1. carbohydrate metabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Calcium, Metal-binding

Protein family/group databases

CAZyiCBM20. Carbohydrate-Binding Module Family 20.
CBM34. Carbohydrate-Binding Module Family 34.
GH13. Glycoside Hydrolase Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
Amylopullulanase
Alternative name(s):
Alpha-amylase/pullulanase
Including the following 2 domains:
Alpha-amylase (EC:3.2.1.1)
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase
Pullulanase (EC:3.2.1.41)
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase
Alpha-dextrin endo-1,6-alpha-glucosidase
Gene namesi
Name:apu
OrganismiThermoanaerobacterium saccharolyticum
Taxonomic identifieri28896 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacterales Family III. Incertae SedisThermoanaerobacterium

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3535 Reviewed prediction
Add
BLAST
Chaini36 – 12791244Amylopullulanase
PRO_0000001324Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP36905.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini930 – 102293Fibronectin type-III 1
Add
BLAST
Domaini1158 – 125295Fibronectin type-III 2
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Repeat, Signal

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR006048. A-amylase_b_C.
IPR003961. Fibronectin_type3.
IPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR004185. Glyco_hydro_13_lg-like_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 1 hit.
PfamiPF00128. Alpha-amylase. 1 hit.
PF02903. Alpha-amylase_N. 1 hit.
PF00041. fn3. 2 hits.
[Graphical view]
SMARTiSM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
SM00060. FN3. 2 hits.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 2 hits.
SSF51445. SSF51445. 2 hits.
SSF81296. SSF81296. 1 hit.
PROSITEiPS50853. FN3. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P36905-1 [UniParc]FASTAAdd to Basket

« Hide

MYKKLFTKKF ISFVMSLLLV LTAAFSSMPF HNVYAADNAS VVANIVGDFQ     50
DQLGDSNWNI DSNITIMQYV GNGLYEFTTP TQLKAGSYQY KVALNHSWNG 100
GGVPSQGNLT LNLTNDSYVT FWFDYNTQSV TDSTKYTPIS NDKLPRLVGT 150
IQSAIGAGKD WDPGTSTAIM IDDNFDNVYS YTAHIPKGDY QYKVTLGNTW 200
AENYGANGVQ DGSNIQLSVA NDADITFFYD ANTHNIWTNY SPTLTGLDNN 250
IYYDDLKHDT HDPFFRNPFG AIKVGQTVTL RIQAKNHDLE SARISYWDDI 300
NKTRTELPMT RIGESPDGNY EYWEIKLSFD HPTRIWYYFI LKDGTKTAYY 350
GDNDDQLGGL GKATDTVNKD FELTVYDKNF DTNDWMKGAV MYQIFPDRFY 400
NGDTSNDHAK TLSRGNDPIE FHNDWNDLPD NPNNAGTPGY TGDGIWSNDF 450
FGGDLKGIDD KLDYLKGLGV SVIYLNPIFE SPSNHKYDTA DYTKIDEMFG 500
TTQDFEKLMS DAHAKGINII LDGVFNHTSD DSIYFNRYGK YPDLGAYQDW 550
KDGNQSLSPY GDWYTINSDG TYECWWGYDS LPVIKSLNGS EYNVTSWANF 600
IINDKNAISK YWLNPDENLN DGADGWRLDV ENEVAHDFWT HFRDAINTVK 650
PEAPMIAENW GDASLDLLGD SFNSVMNYQF RNDIIDFLIG QSFDDGNGQH 700
NPIDAAKLDQ RLMSIYERYP LPAFYSTMNL LGSHDTMSIL TVFGYNSADP 750
NENSDAAKRL AEQKLKLATI LQMGYPGMAD IYYGDEAGVS GGKDPDDRRT 800
FPWGNEDTAL QDFFKNVSSI RNNNQVLKTG DLETLYAQND VYAIGRRIIN 850
GKDAFGNSYP DSAAIVAINR SNSDQQITID TTKFLRDGVA FKDLINGDKS 900
YTINGGQITI NIPAMSGVML ISDDGQDLTA PQVPSNVVAT SGNGKVDLSW 950
SQSDGATGYN IYRSSVEGGL YEKIASNVTG TTFEDTNVTN GLKYVYAISA 1000
VDELGNESEM SIDTVAYPAY PIGWVGNLTQ VVDNHVISVS NPTEDIYAEV 1050
WADGLTNSTG QGPNMIAQLG YKYVGGTVND SVYGSVYNSV YGVDDSDFTW 1100
VNAQYVGDIG NNDQYKASLH LINRSMGYLM RFSDNQGQSW TTTDTLSFYV 1150
VPSDDLIKPT APILNQPGVE SSRVSLTWSP STDNVGIYNY EIYRSDGGTF 1200
NKIATVSNEV YNYVDTSVIN GTTYSYKVVA ADPSFNRTES NVVTIKPDVV 1250
PIKVTFNVTV PDYTPNSVNL AGTFPNATW 1279
Length:1,279
Mass (Da):142,431
Last modified:February 1, 1995 - v2
Checksum:i095CCBCA391624DD
GO

Sequence cautioni

The sequence AAA19800.1 differs from that shown. Reason: Contaminating sequence. Vector contamination at the C-terminus, a segment of 9 residues, which seems to originate from a puc-type vector.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L07762 Unassigned DNA. Translation: AAA19800.1. Sequence problems.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L07762 Unassigned DNA. Translation: AAA19800.1 . Sequence problems.

3D structure databases

ProteinModelPortali P36905.
ModBasei Search...

Protein family/group databases

CAZyi CBM20. Carbohydrate-Binding Module Family 20.
CBM34. Carbohydrate-Binding Module Family 34.
GH13. Glycoside Hydrolase Family 13.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 2.60.40.10. 3 hits.
2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProi IPR006048. A-amylase_b_C.
IPR003961. Fibronectin_type3.
IPR015902. Glyco_hydro_13.
IPR013780. Glyco_hydro_13_b.
IPR006047. Glyco_hydro_13_cat_dom.
IPR004185. Glyco_hydro_13_lg-like_dom.
IPR006589. Glyco_hydro_13_sub_cat_dom.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view ]
PANTHERi PTHR10357. PTHR10357. 1 hit.
Pfami PF00128. Alpha-amylase. 1 hit.
PF02903. Alpha-amylase_N. 1 hit.
PF00041. fn3. 2 hits.
[Graphical view ]
SMARTi SM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
SM00060. FN3. 2 hits.
[Graphical view ]
SUPFAMi SSF49265. SSF49265. 2 hits.
SSF51445. SSF51445. 2 hits.
SSF81296. SSF81296. 1 hit.
PROSITEi PS50853. FN3. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Cloning and sequencing of the Thermoanaerobacterium saccharolyticum B6A-RI apu gene and purification and characterization of the amylopullulanase from Escherichia coli."
    Ramesh M.V., Podkovyrov S.M., Lowe S.E., Zeikus J.G.
    Appl. Environ. Microbiol. 60:94-101(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 49915 / DSM 7060 / B6A-RI.
  2. Robison K.
    Unpublished observations (NOV-1994)
    Cited for: IDENTIFICATION OF PROBABLE VECTOR CONTAMINATION.

Entry informationi

Entry nameiAPU_THESA
AccessioniPrimary (citable) accession number: P36905
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: February 1, 1995
Last modified: January 22, 2014
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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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