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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

Ca2+By similarityNote: Binds 1 Ca(2+) ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi401 – 4011CalciumBy similarity
Metal bindingi403 – 4031Calcium; via carbonyl oxygenBy similarity
Metal bindingi406 – 4061CalciumBy similarity
Metal bindingi407 – 4071CalciumBy similarity
Metal bindingi452 – 4521Calcium; via carbonyl oxygenBy similarity
Metal bindingi454 – 4541CalciumBy similarity
Binding sitei527 – 5271SubstrateBy similarity
Binding sitei627 – 6271SubstrateBy similarity
Active sitei629 – 6291NucleophileBy similarity
Active sitei658 – 6581Proton donorBy similarity
Sitei735 – 7351Transition state stabilizerBy similarity
Binding sitei798 – 7981SubstrateBy similarity

GO - Molecular functioni

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

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 – 3535Sequence AnalysisAdd
BLAST
Chaini36 – 12791244AmylopullulanasePRO_0000001324Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP36905.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated
Contains 2 fibronectin type-III domains.PROSITE-ProRule annotation

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

        10         20         30         40         50
MYKKLFTKKF ISFVMSLLLV LTAAFSSMPF HNVYAADNAS VVANIVGDFQ
60 70 80 90 100
DQLGDSNWNI DSNITIMQYV GNGLYEFTTP TQLKAGSYQY KVALNHSWNG
110 120 130 140 150
GGVPSQGNLT LNLTNDSYVT FWFDYNTQSV TDSTKYTPIS NDKLPRLVGT
160 170 180 190 200
IQSAIGAGKD WDPGTSTAIM IDDNFDNVYS YTAHIPKGDY QYKVTLGNTW
210 220 230 240 250
AENYGANGVQ DGSNIQLSVA NDADITFFYD ANTHNIWTNY SPTLTGLDNN
260 270 280 290 300
IYYDDLKHDT HDPFFRNPFG AIKVGQTVTL RIQAKNHDLE SARISYWDDI
310 320 330 340 350
NKTRTELPMT RIGESPDGNY EYWEIKLSFD HPTRIWYYFI LKDGTKTAYY
360 370 380 390 400
GDNDDQLGGL GKATDTVNKD FELTVYDKNF DTNDWMKGAV MYQIFPDRFY
410 420 430 440 450
NGDTSNDHAK TLSRGNDPIE FHNDWNDLPD NPNNAGTPGY TGDGIWSNDF
460 470 480 490 500
FGGDLKGIDD KLDYLKGLGV SVIYLNPIFE SPSNHKYDTA DYTKIDEMFG
510 520 530 540 550
TTQDFEKLMS DAHAKGINII LDGVFNHTSD DSIYFNRYGK YPDLGAYQDW
560 570 580 590 600
KDGNQSLSPY GDWYTINSDG TYECWWGYDS LPVIKSLNGS EYNVTSWANF
610 620 630 640 650
IINDKNAISK YWLNPDENLN DGADGWRLDV ENEVAHDFWT HFRDAINTVK
660 670 680 690 700
PEAPMIAENW GDASLDLLGD SFNSVMNYQF RNDIIDFLIG QSFDDGNGQH
710 720 730 740 750
NPIDAAKLDQ RLMSIYERYP LPAFYSTMNL LGSHDTMSIL TVFGYNSADP
760 770 780 790 800
NENSDAAKRL AEQKLKLATI LQMGYPGMAD IYYGDEAGVS GGKDPDDRRT
810 820 830 840 850
FPWGNEDTAL QDFFKNVSSI RNNNQVLKTG DLETLYAQND VYAIGRRIIN
860 870 880 890 900
GKDAFGNSYP DSAAIVAINR SNSDQQITID TTKFLRDGVA FKDLINGDKS
910 920 930 940 950
YTINGGQITI NIPAMSGVML ISDDGQDLTA PQVPSNVVAT SGNGKVDLSW
960 970 980 990 1000
SQSDGATGYN IYRSSVEGGL YEKIASNVTG TTFEDTNVTN GLKYVYAISA
1010 1020 1030 1040 1050
VDELGNESEM SIDTVAYPAY PIGWVGNLTQ VVDNHVISVS NPTEDIYAEV
1060 1070 1080 1090 1100
WADGLTNSTG QGPNMIAQLG YKYVGGTVND SVYGSVYNSV YGVDDSDFTW
1110 1120 1130 1140 1150
VNAQYVGDIG NNDQYKASLH LINRSMGYLM RFSDNQGQSW TTTDTLSFYV
1160 1170 1180 1190 1200
VPSDDLIKPT APILNQPGVE SSRVSLTWSP STDNVGIYNY EIYRSDGGTF
1210 1220 1230 1240 1250
NKIATVSNEV YNYVDTSVIN GTTYSYKVVA ADPSFNRTES NVVTIKPDVV
1260 1270
PIKVTFNVTV PDYTPNSVNL AGTFPNATW
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.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07762 Unassigned DNA. Translation: AAA19800.1. Sequence problems.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07762 Unassigned DNA. Translation: AAA19800.1 . Sequence problems.

3D structure databases

ProteinModelPortali P36905.
ModBasei Search...
MobiDBi 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: November 26, 2014
This is version 96 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