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Protein

Amylopullulanase

Gene

apu

Organism
Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) (Clostridium thermohydrosulfuricum)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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.1 Publication

Cofactori

Ca2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi245 – 2451Calcium 1By similarity
Metal bindingi247 – 2471Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi285 – 2851Calcium 1By similarity
Metal bindingi340 – 3401Calcium 1By similarity
Metal bindingi398 – 3981Calcium 2By similarity
Metal bindingi400 – 4001Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi403 – 4031Calcium 2By similarity
Metal bindingi404 – 4041Calcium 2By similarity
Metal bindingi449 – 4491Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi451 – 4511Calcium 2By similarity
Binding sitei524 – 5241SubstrateBy similarity
Binding sitei626 – 6261SubstrateBy similarity
Active sitei628 – 6281Nucleophile1 Publication
Active sitei657 – 6571Proton donor1 Publication
Sitei734 – 7341Transition state stabilizerBy similarity
Binding sitei793 – 7931SubstrateBy similarity
Binding sitei797 – 7971SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BioCyciTPSE340099:GH4W-2228-MONOMER.

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:3.2.1.411 Publication)
Alternative name(s):
1,4-alpha-D-glucan glucanohydrolase
Alpha-dextrin endo-1,6-alpha-glucosidase
Gene namesi
Name:apu
Ordered Locus Names:Teth39_2173
OrganismiThermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) (Clostridium thermohydrosulfuricum)
Taxonomic identifieri340099 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacteraceaeThermoanaerobacter
Proteomesi
  • UP000002156 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi628 – 6281D → N or E: Loss of function. 1 Publication
Mutagenesisi657 – 6571E → Q or D: Loss of function. 1 Publication
Mutagenesisi734 – 7341D → Q or E: Loss of function. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3131Sequence analysisAdd
BLAST
Chaini32 – 14811450AmylopullulanasePRO_0000001322Add
BLAST

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi340099.Teth39_2173.

Structurei

3D structure databases

ProteinModelPortaliP38939.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini927 – 101892Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini1159 – 125597Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini1250 – 1357108CBM20PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni733 – 7342Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the glycosyl hydrolase 13 family.Curated
Contains 1 CBM20 (carbohydrate binding type-20) domain.PROSITE-ProRule annotation
Contains 2 fibronectin type-III domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG4105C9C. Bacteria.
COG0366. LUCA.
COG3103. LUCA.
HOGENOMiHOG000037518.
OMAiWSNDFFG.

Family and domain databases

Gene3Di2.60.40.10. 4 hits.
2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR031319. A-amylase_C.
IPR013784. Carb-bd-like_fold.
IPR002044. CBM_fam20.
IPR003961. FN3_dom.
IPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR004185. Glyco_hydro_13_lg-like_dom.
IPR013780. Glyco_hydro_b.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 3 hits.
PfamiPF00128. Alpha-amylase. 1 hit.
PF02903. Alpha-amylase_N. 1 hit.
[Graphical view]
SMARTiSM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
SM01065. CBM_2. 1 hit.
SM00060. FN3. 2 hits.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 2 hits.
SSF49452. SSF49452. 1 hit.
SSF51445. SSF51445. 2 hits.
SSF81296. SSF81296. 1 hit.
PROSITEiPS51166. CBM20. 1 hit.
PS50853. FN3. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P38939-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFKRRTLGFL LSFLLIYTAV FGSMPVQFAK AETDTAPAIA NVVGDFQSKI
60 70 80 90 100
GDSDWNINSD KTVMTYKGNG FYEFTTPVAL PAGDYEYKVA LNHSWEGGGV
110 120 130 140 150
PSQGNLSLHL DSDSVVTFYY NYNTSSVTDS TKYTPIPEEK LPRIVGTIQS
160 170 180 190 200
AIGAGDDWKP ETSTAIMRDY KFNNVYEYTA NVPKGYYEFK VTLGPSWDIN
210 220 230 240 250
YGLNGEQNGP NIPLNVAYDT KITFYYDSVS HNIWTDYNPP LTGPDNNIYY
260 270 280 290 300
DDLKHDTHDP FFRSPFGAIK TGDTVTLRIQ AKNHDLESAK ISYWDDIKKT
310 320 330 340 350
RTEVPMYKIG QSPDGQYEYW EVKLSFDYPT RIWYYFILKD GTKTAYYGDN
360 370 380 390 400
DEQLGGVGKA TDTVNKDFEL TVYDKNLDTP DWMKGAVMYQ IFPDRFYNGD
410 420 430 440 450
PLNDRLKEYS RGFDPVEYHD DWYDLPDNPN DKDKPGYTGD GIWNNDFFGG
460 470 480 490 500
DLQGINDKLD YLKNLGISVI YLNPIFQSPS NHRYDTTDYT KIDELLGDLD
510 520 530 540 550
TFKTLMKEAH ARGIKVILDG VFNHTSDDSI YFDRYGKYLD NELGAYQAWK
560 570 580 590 600
QGDQSKSPYG DWYEIKPDGT YEGWWGFDSL PVIRQINGSE YNVKSWADFI
610 620 630 640 650
INNPNAISKY WLNPDGDKDA GADGWRLDVA NEIAHDFWVH FRAAINTVKP
660 670 680 690 700
NAPMIAELWG DASLDLLGDS FNSVMNYLFR NAVIDFILDK QFDDGNVVHN
710 720 730 740 750
PIDAAKLDQR LMSIYERYPL PVFYSTMNLL GSHDTMRILT VFGYNSANEN
760 770 780 790 800
QNSQEAKDLA VKRLKLAAIL QMGYPGMPSI YYGDEAGQSG GKDPDNRRTF
810 820 830 840 850
SWGREDKDLQ DFFKKVVNIR NENQVLKTGD LETLYANGDV YAFGRRIING
860 870 880 890 900
KDVFGNSYPD SVAIVVINKG EAKSVQIDTT KFVRDGVAFT DALSGKTYTV
910 920 930 940 950
RDGQIVVEVV ALDGAILISD PGQNLTAPQP ITDLKAVSGN GQVDLSWSAV
960 970 980 990 1000
DRAVSYNIYR STVKGGLYEK IASNVTQITY IDTDVTNGLK YVYSVTAVDS
1010 1020 1030 1040 1050
DGNESALSNE VEAYPAFSIG WAGNMNQVDT HVIGVNNPVE VYAEIWAEGL
1060 1070 1080 1090 1100
TDKPGQGENM IAQLGYRYIG DGGQDATRNK VEGVEINKDW TWVDARYVGD
1110 1120 1130 1140 1150
SGNNDKYMAK FVPDMVGTWE YIMRFSSNQG QDWTYTKGPD GKTDEAKQFI
1160 1170 1180 1190 1200
VVPSNDVEPP TALGLQQPGI ESSRVTLNWS LSTDNVAIYG YEIYKSLSET
1210 1220 1230 1240 1250
GPFVKIATVA DTVYNYVDTD VVNGKVYYYK VVAVDTSFNR TASNIVKATP
1260 1270 1280 1290 1300
DIIPIKVIFN VTVPDYTPDD GANIAGNFHD AFWNPSAHQM TKTGPNTYSI
1310 1320 1330 1340 1350
TLTLNEGTQL EYKYARGSWD KVEKGEYGEE IANRKITVVN QGSNTMVVND
1360 1370 1380 1390 1400
TVQRWRDLPI YIYSPKDNTT VDANTNEIEI KGNTYKGAKV TINDESFVQQ
1410 1420 1430 1440 1450
ENGVFTKVVP LEYGVNTTKI HVEPSGDKNN ELTKDITITV IREEPVQEKE
1460 1470 1480
PTPTPESEPA PMPEPQPTPT PEPQPSAIMA L
Length:1,481
Mass (Da):166,230
Last modified:May 20, 2008 - v2
Checksum:iF9CE0B0BFEF892D3
GO

Sequence cautioni

The sequence ABY95795 differs from that shown. Reason: Frameshift at position 1477. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti185 – 1851G → R no nucleotide entry (PubMed:2302196).Curated
Sequence conflicti185 – 1851G → R in AAA23201 (PubMed:8344920).Curated
Sequence conflicti264 – 2652SP → FA no nucleotide entry (PubMed:2302196).Curated
Sequence conflicti264 – 2652SP → FA in AAA23201 (PubMed:8344920).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M97665 Genomic DNA. Translation: AAA23201.1.
CP000924 Genomic DNA. Translation: ABY95795.1. Frameshift.
PIRiS28669.

Genome annotation databases

EnsemblBacteriaiABY95795; ABY95795; Teth39_2173.
KEGGitpd:Teth39_2173.
PATRICi23889175. VBIThePse6203_2274.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M97665 Genomic DNA. Translation: AAA23201.1.
CP000924 Genomic DNA. Translation: ABY95795.1. Frameshift.
PIRiS28669.

3D structure databases

ProteinModelPortaliP38939.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi340099.Teth39_2173.

Protein family/group databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABY95795; ABY95795; Teth39_2173.
KEGGitpd:Teth39_2173.
PATRICi23889175. VBIThePse6203_2274.

Phylogenomic databases

eggNOGiENOG4105C9C. Bacteria.
COG0366. LUCA.
COG3103. LUCA.
HOGENOMiHOG000037518.
OMAiWSNDFFG.

Enzyme and pathway databases

BioCyciTPSE340099:GH4W-2228-MONOMER.

Family and domain databases

Gene3Di2.60.40.10. 4 hits.
2.60.40.1180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR031319. A-amylase_C.
IPR013784. Carb-bd-like_fold.
IPR002044. CBM_fam20.
IPR003961. FN3_dom.
IPR015902. Glyco_hydro_13.
IPR006047. Glyco_hydro_13_cat_dom.
IPR004185. Glyco_hydro_13_lg-like_dom.
IPR013780. Glyco_hydro_b.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
[Graphical view]
PANTHERiPTHR10357. PTHR10357. 3 hits.
PfamiPF00128. Alpha-amylase. 1 hit.
PF02903. Alpha-amylase_N. 1 hit.
[Graphical view]
SMARTiSM00642. Aamy. 1 hit.
SM00632. Aamy_C. 1 hit.
SM01065. CBM_2. 1 hit.
SM00060. FN3. 2 hits.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 2 hits.
SSF49452. SSF49452. 1 hit.
SSF51445. SSF51445. 2 hits.
SSF81296. SSF81296. 1 hit.
PROSITEiPS51166. CBM20. 1 hit.
PS50853. FN3. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAPU_THEP3
AccessioniPrimary (citable) accession number: P38939
Secondary accession number(s): B0K7X5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: May 20, 2008
Last modified: September 7, 2016
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.