P38939 (APU_THEP3) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Amylopullulanase

Alternative name(s):
Alpha-amylase/pullulanase

Including the following 2 domains:

1. Alpha-amylase
   EC=3.2.1.1
   Alternative name(s):
   1,4-alpha-D-glucan glucanohydrolase
2. Pullulanase
   EC=3.2.1.41
   Alternative name(s):
   1,4-alpha-D-glucan glucanohydrolase
   Alpha-dextrin endo-1,6-alpha-glucosidase

Gene names

Name:	apu
Ordered Locus Names:	Teth39_2173

Organism

Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) (Clostridium thermohydrosulfuricum) [Complete proteome] [HAMAP]

Taxonomic identifier

340099 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Thermoanaerobacterales › Thermoanaerobacteriaceae › Thermoanaerobacter

Protein attributes

Sequence length	1481 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	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.
Cofactor	Binds 1 calcium ion per subunit By similarity.
Subunit structure	Monomer.
Sequence similarities	Belongs to the glycosyl hydrolase 13 family. Contains 1 CBM20 (carbohydrate binding type-20) domain. Contains 2 fibronectin type-III domains.
Sequence caution	The sequence ABY95795.1 differs from that shown. Reason: Frameshift at position 1477.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Domain	Repeat Signal
Ligand	Calcium Metal-binding
Molecular function	Glycosidase Hydrolase
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	alpha-amylase activity Inferred from electronic annotation. Source: EC carbohydrate binding Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW 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 – 31	31	Potential
	Chain	32 – 1481	1450	Amylopullulanase		PRO_0000001322
Regions
	Domain	924 – 1013	90	Fibronectin type-III 1
	Domain	1156 – 1249	94	Fibronectin type-III 2
	Domain	1250 – 1357	108	CBM20
Sites
	Active site	628	1	Nucleophile By similarity
	Active site	657	1	Proton donor By similarity
	Metal binding	398	1	Calcium By similarity
	Metal binding	400	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	403	1	Calcium By similarity
	Metal binding	404	1	Calcium By similarity
	Metal binding	449	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	451	1	Calcium By similarity
	Binding site	524	1	Substrate By similarity
	Binding site	626	1	Substrate By similarity
	Binding site	797	1	Substrate By similarity
	Site	734	1	Transition state stabilizer By similarity
Experimental info
	Mutagenesis	628	1	D → N or E: Loss of function. Ref.2
	Mutagenesis	657	1	E → Q or D: Loss of function. Ref.2
	Mutagenesis	734	1	D → Q or E: Loss of function. Ref.2
	Sequence conflict	185	1	G → R no nucleotide entry Ref.1
	Sequence conflict	185	1	G → R in AAA23201. Ref.2
	Sequence conflict	264 – 265	2	SP → FA no nucleotide entry Ref.1
	Sequence conflict	264 – 265	2	SP → FA in AAA23201. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P38939 [UniParc]. Last modified May 20, 2008. Version 2. Checksum: F9CE0B0BFEF892D3	FASTA	1,481	166,230
	10 20 30 40 50 60 MFKRRTLGFL LSFLLIYTAV FGSMPVQFAK AETDTAPAIA NVVGDFQSKI GDSDWNINSD 70 80 90 100 110 120 KTVMTYKGNG FYEFTTPVAL PAGDYEYKVA LNHSWEGGGV PSQGNLSLHL DSDSVVTFYY 130 140 150 160 170 180 NYNTSSVTDS TKYTPIPEEK LPRIVGTIQS AIGAGDDWKP ETSTAIMRDY KFNNVYEYTA 190 200 210 220 230 240 NVPKGYYEFK VTLGPSWDIN YGLNGEQNGP NIPLNVAYDT KITFYYDSVS HNIWTDYNPP 250 260 270 280 290 300 LTGPDNNIYY DDLKHDTHDP FFRSPFGAIK TGDTVTLRIQ AKNHDLESAK ISYWDDIKKT 310 320 330 340 350 360 RTEVPMYKIG QSPDGQYEYW EVKLSFDYPT RIWYYFILKD GTKTAYYGDN DEQLGGVGKA 370 380 390 400 410 420 TDTVNKDFEL TVYDKNLDTP DWMKGAVMYQ IFPDRFYNGD PLNDRLKEYS RGFDPVEYHD 430 440 450 460 470 480 DWYDLPDNPN DKDKPGYTGD GIWNNDFFGG DLQGINDKLD YLKNLGISVI YLNPIFQSPS 490 500 510 520 530 540 NHRYDTTDYT KIDELLGDLD TFKTLMKEAH ARGIKVILDG VFNHTSDDSI YFDRYGKYLD 550 560 570 580 590 600 NELGAYQAWK QGDQSKSPYG DWYEIKPDGT YEGWWGFDSL PVIRQINGSE YNVKSWADFI 610 620 630 640 650 660 INNPNAISKY WLNPDGDKDA GADGWRLDVA NEIAHDFWVH FRAAINTVKP NAPMIAELWG 670 680 690 700 710 720 DASLDLLGDS FNSVMNYLFR NAVIDFILDK QFDDGNVVHN PIDAAKLDQR LMSIYERYPL 730 740 750 760 770 780 PVFYSTMNLL GSHDTMRILT VFGYNSANEN QNSQEAKDLA VKRLKLAAIL QMGYPGMPSI 790 800 810 820 830 840 YYGDEAGQSG GKDPDNRRTF SWGREDKDLQ DFFKKVVNIR NENQVLKTGD LETLYANGDV 850 860 870 880 890 900 YAFGRRIING KDVFGNSYPD SVAIVVINKG EAKSVQIDTT KFVRDGVAFT DALSGKTYTV 910 920 930 940 950 960 RDGQIVVEVV ALDGAILISD PGQNLTAPQP ITDLKAVSGN GQVDLSWSAV DRAVSYNIYR 970 980 990 1000 1010 1020 STVKGGLYEK IASNVTQITY IDTDVTNGLK YVYSVTAVDS DGNESALSNE VEAYPAFSIG 1030 1040 1050 1060 1070 1080 WAGNMNQVDT HVIGVNNPVE VYAEIWAEGL TDKPGQGENM IAQLGYRYIG DGGQDATRNK 1090 1100 1110 1120 1130 1140 VEGVEINKDW TWVDARYVGD SGNNDKYMAK FVPDMVGTWE YIMRFSSNQG QDWTYTKGPD 1150 1160 1170 1180 1190 1200 GKTDEAKQFI VVPSNDVEPP TALGLQQPGI ESSRVTLNWS LSTDNVAIYG YEIYKSLSET 1210 1220 1230 1240 1250 1260 GPFVKIATVA DTVYNYVDTD VVNGKVYYYK VVAVDTSFNR TASNIVKATP DIIPIKVIFN 1270 1280 1290 1300 1310 1320 VTVPDYTPDD GANIAGNFHD AFWNPSAHQM TKTGPNTYSI TLTLNEGTQL EYKYARGSWD 1330 1340 1350 1360 1370 1380 KVEKGEYGEE IANRKITVVN QGSNTMVVND TVQRWRDLPI YIYSPKDNTT VDANTNEIEI 1390 1400 1410 1420 1430 1440 KGNTYKGAKV TINDESFVQQ ENGVFTKVVP LEYGVNTTKI HVEPSGDKNN ELTKDITITV 1450 1460 1470 1480 IREEPVQEKE PTPTPESEPA PMPEPQPTPT PEPQPSAIMA L

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Substrate competition and specificity at the active site of amylopullulanase from Clostridium thermohydrosulfuricum." Mathupala S.P., Saha B.C., Zeikus J.G. Biochem. Biophys. Res. Commun. 166:126-132(1990) [PubMed: 2302196] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Sequencing of the amylopullulanase (apu) gene of Thermoanaerobacter ethanolicus 39E, and identification of the active site by site-directed mutagenesis." Mathupala S.P., Lowe S.E., Podkovyrov S.M., Zeikus J.G. J. Biol. Chem. 268:16332-16344(1993) [PubMed: 8344920] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 625-630, MUTAGENESIS OF ASP-628; GLU-657 AND ASP-734.
[3]	"Complete sequence of Thermoanaerobacter pseudethanolicus 39E." Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Bruce D., Goodwin L., Saunders E., Brettin T., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L. , Kyrpides N., Lykidis A., Hemme C., Fields M.W., He Z., Zhou J., Richardson P. Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 33223 / 39E.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M97665 Genomic DNA. Translation: AAA23201.1. CP000924 Genomic DNA. Translation: ABY95795.1. Frameshift.
PIR	S28669.
RefSeq	YP_001666131.1. NC_010321.1.
3D structure databases
ProteinModelPortal	P38939.
ModBase	Search...
Protein-protein interaction databases
STRING	P38939.
Protein family/group databases
CAZy	CBM20. Carbohydrate-Binding Module Family 20. CBM34. Carbohydrate-Binding Module Family 34. GH13. Glycoside Hydrolase Family 13.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5873743.
GenomeReviews	Gene locus Teth39_2173 in contig CP000924_GR.
KEGG	tpd:Teth39_2173.
PATRIC	23889175. VBIThePse6203_2274.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG313883.
OMA	GWANLQW.
ProtClustDB	CLSK932660.
Enzyme and pathway databases
BioCyc	TPSE340099:TETH39_2173-MONOMER.
Family and domain databases
InterPro	IPR006048. A-amylase_b_C. IPR015902. Alpha_amylase. IPR013784. Carb-bd-like_fold. IPR002044. CBM_fam20. IPR003961. Fibronectin_type3. 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_subgr_catalytic. IPR017853. Glycoside_hydrolase_SF. IPR013783. Ig-like_fold. IPR014756. Ig_E-set. [Graphical view]
Gene3D	G3DSA:2.60.40.1180. Glyco_hydro_13_b. 1 hit. G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit. G3DSA:2.60.40.10. Ig-like_fold. 4 hits.
PANTHER	PTHR10357. Alpha_amylase. 1 hit.
Pfam	PF00128. Alpha-amylase. 1 hit. PF02903. Alpha-amylase_N. 1 hit. PF00041. fn3. 2 hits. [Graphical view]
SMART	SM00642. Aamy. 1 hit. SM00632. Aamy_C. 1 hit. SM01065. CBM_2. 1 hit. SM00060. FN3. 2 hits. [Graphical view]
SUPFAM	SSF49452. CBD_4. 1 hit. SSF49265. FN_III-like. 2 hits. SSF51445. Glyco_hydro_cat. 1 hit. SSF81296. Ig_E-set. 1 hit.
PROSITE	PS51166. CBM20. 1 hit. PS50853. FN3. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

APU_THEP3

Accession

Primary (citable) accession number: P38939
Secondary accession number(s): B0K7X5

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	May 20, 2008
Last modified:	January 25, 2012
This is version 96 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program