Reviewed, UniProtKB/Swiss-Prot P16950 (APU_THETY)

Names and origin

Protein names

Recommended name:
    Amylopullulanase
Alternative name(s):
    Alpha-amylase/pullulanase
Including the following 2 domains:
    1- Recommended name:
            Alpha-amylase
              EC=3.2.1.1
        Alternative name(s):
            1,4-alpha-D-glucan glucanohydrolase
    2- Recommended name:
            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

Organism

Thermoanaerobacter thermohydrosulfuricus (Clostridium thermohydrosulfuricum)

Taxonomic identifier

1516 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Thermoanaerobacterales › Thermoanaerobacteriaceae › Thermoanaerobacter

Protein attributes

Sequence length	1475 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 oligosaccharides and polysaccharides. 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.
Sequence similarities	Belongs to the glycosyl hydrolase 13 family. Contains 1 CBM20 (carbohydrate binding type-20) domain. Contains 2 fibronectin type-III domains.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Domain	Repeat Signal
Ligand	Calcium Metal-binding
Molecular function	Glycosidase Hydrolase
Technical term	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 calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW carbohydrate 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 – 31	31	Ref.2
	Chain	32 – 1475	1444	Amylopullulanase		PRO_0000001323
Regions
	Domain	925 – 1014	90	Fibronectin type-III 1
	Domain	1161 – 1254	94	Fibronectin type-III 2
	Domain	1255 – 1362	108	CBM20
Sites
	Active site	629	1	Nucleophile By similarity
	Active site	658	1	Proton donor By similarity
	Active site	735	1	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

Sequences

	Sequence		Length	Mass (Da)
	P16950-1 [UniParc]. Last modified August 1, 1990. Version 1. Checksum: 3476C414110BE376	FASTA	1,475	165,631
	10 20 30 40 50 60 MFKRRALGFL LAFLLVFTAV FGSMPMEFAK AETDTAPAIA NVVGNFQSKL GDSDWNINSD 70 80 90 100 110 120 KTIMTYKGNG FYEFTTPVAL PAGDYEYKVA LNHSWEGGGV PSQGNLSFHL DSDSVVTFYY 130 140 150 160 170 180 NYNTSSITDS TKYTPIPEDK LPRLVGTIQP AIGAGDDWKP ETSTAIMRDY KFNNVYEYTA 190 200 210 220 230 240 NVPKGNYEFK VTLGPSWDIN YGLNGEQNGP NIPLNVAYDT KITFYYDSVS HNIWTDYNPP 250 260 270 280 290 300 LTGPDNNIYY DDLRHDTHDP FFRSPFGAIK TGDTVTLRIQ AKNHDIESAK ISYWDDIKKT 310 320 330 340 350 360 RIEVPMYRIG QSPDGKYEYW EVKLSFDHPT RIWYYFILKD GTKTAYYGDN DEQLGGVGKA 370 380 390 400 410 420 TDTENKDFEL TVYDKNLDTP DWMKGSVMYQ IFPDRFFNGD SSNDHLKKYS RGFDPVEYHS 430 440 450 460 470 480 NWYELPDNPN DKNKLGYTGD GIWSNDFFGG DLKGIDDKLD YLKSLGISVI YLNPIFQSPS 490 500 510 520 530 540 NHRYDTTDYT KIDELLGDLS TFKKLMEDAH AKGIKVILDG VFNHTSDDSI YFDRYGKYLN 550 560 570 580 590 600 TGVLGAYQAW KQGDQSKSPY GDWYEIKPDG TYEGWWGFDS LPVIRQINGS EYNVKSWADF 610 620 630 640 650 660 IINNPNAISK YWLNPDGDKN VGADGWRLDV ANEVAHDFWV HFRGAINTVK PNAPMVAENW 670 680 690 700 710 720 NDASLDLLGD SFNSVMNYLF RNAVIDFILD KSFDDGNVVH NPIDAAKLDQ RLMSIYERYP 730 740 750 760 770 780 LPVFYSTMNL LGSHDTMRIL TVFGYNSADE NQNSQAAKDL AVKRLKLAAI LQMGYPGMPS 790 800 810 820 830 840 IYYGDEAGQS GGKDPDNRRT FPWGREDTDL QTFFKKVVNI RNENQVLKTG DLETLYANGD 850 860 870 880 890 900 VYAFGRRIIN GKDTFGKSYP DSVAIVVINK GDAKQVSIDT TKFIRDGVAF TDALSGKTYT 910 920 930 940 950 960 VQDGKIVVEV GSMDGAILIS DTGQNLTAPQ PITDLKAVSG NGKVDLSWSV VDKAVSYNIY 970 980 990 1000 1010 1020 RSTVKGGLYE KIASNVTQIT YTDTEVTNGL KYVYAVTAVD NDGNESALSN EVEAYPAFPI 1030 1040 1050 1060 1070 1080 GWAGNMNQVN THVIGVNNPV EVYAEVWAQG LTDKPGQGEN MIAQLGYRYI GDTVGDAVYN 1090 1100 1110 1120 1130 1140 AVYNKVEGVE ISKDWTWVDA QYVGDSGNND KYMAKFVPDM VGTWEYIMRF SSNQGHDWTY 1150 1160 1170 1180 1190 1200 TKGPDGKTDE AKQFTVVPSN DVETPTAPVL QQPGIESSRV TLNWSPSADD VAIFGYEIYK 1210 1220 1230 1240 1250 1260 SSSETGPFIK IATVSDSVYN YVDTDVVNGN VYYYKVVAVD TSYNRTASNT VKATPDIIPI 1270 1280 1290 1300 1310 1320 KVTFNVTIPD YTPDDGVNIA GNFPDAFWNP NANQMTKAGS NTYSITLTLN EGTQIEYKYA 1330 1340 1350 1360 1370 1380 RGSWDKVEKG EYGNEIDNRK ITVVNQGSNT MVVNDTVQRW RDVPIYIYSP KDKTIVDANT 1390 1400 1410 1420 1430 1440 SEIEIKGNTY KGAKVTINDE SFVQQENGVF TKVVPLEYGV NTIKIHVEPS GDKNNELTKD 1450 1460 1470 ITITVTREKP ARRQNLLLLH QQKQQNHLKK YHKAK

References

[1]	"Nucleotide sequence of the alpha-amylase-pullulanase gene from Clostridium thermohydrosulfuricum." Melasniemi H., Paloheimo M., Hemioe L. J. Gen. Microbiol. 136:447-454(1990) [PubMed: 2391488] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: E101-69.
[2]	"Purification and some properties of the extracellular alpha-amylase-pullulanase produced by Clostridium thermohydrosulfuricum." Melasniemi H. Biochem. J. 250:813-818(1988) [PubMed: 3260488] [Abstract] Cited for: PROTEIN SEQUENCE OF 32-39. Strain: E101-69.
[3]	"Proposed acquisition of an animal protein domain by bacteria." Bork P., Doolittle R.F. Proc. Natl. Acad. Sci. U.S.A. 89:8990-8994(1992) [PubMed: 1409594] [Abstract] Cited for: DOMAINS FIBRONECTIN TYPE-III.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M28471 Genomic DNA. Translation: AAA23205.1.
PIR	A44765.
3D structure databases
HSSP	HSSP built from PDB template 1JI1 based on UniProtKB Q60053.
ModBase	Search...
Protein family/group databases
CAZy	CBM20. Carbohydrate-Binding Module Family 20. CBM34. Carbohydrate-Binding Module Family 34. GH13. Glycoside Hydrolase Family 13.
Enzyme and pathway databases
BRENDA	3.2.1.1. 290446. 3.2.1.41. 290446.
Family and domain databases
InterPro	IPR006048. A-amylase_b_C. IPR008957. Fibronectin_typ-III-like_fold. IPR003961. FN_III. IPR006047. Glyco_hydro_13_cat. IPR004185. Glyco_hydro_13_lg-like. IPR006589. Glyco_hydro_13_sub_cat. IPR002044. Glyco_hydro_carb-bd. IPR013781. Glyco_hydro_sg_catalytic. IPR013783. Ig-like_fold. [Graphical view]
Gene3D	G3DSA:2.60.40.30. FN_III-like. 2 hits. G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit. G3DSA:2.60.40.10. Ig-like_fold. 1 hit.
Pfam	PF00128. Alpha-amylase. 1 hit. PF02903. Alpha-amylase_N. 1 hit. PF00686. CBM_20. 1 hit. PF00041. fn3. 2 hits. [Graphical view]
SMART	SM00642. Aamy. 1 hit. SM00632. Aamy_C. 1 hit. SM00060. FN3. 2 hits. [Graphical view]
PROSITE	PS51166. CBM20. 1 hit. PS50853. FN3. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

APU_THETY

Accession

Primary (citable) accession number: P16950

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	August 1, 1990
Last modified:	June 16, 2009
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)