Unreviewed, UniProtKB/TrEMBL Q9LIR6 (Q9LIR6_ARATH)

Names and origin

Protein names

Recommended name:
    Beta-amylase RuleBase RU000509V3
    EC=3.2.1.2

Gene names

Ordered Locus Names:

At3g23920 TAIR At3g23920

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	575 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains. RuleBase RU000509V3
Sequence similarities	Belongs to the glycosyl hydrolase 14 family. RuleBase RU004157V1

Ontologies

Keywords
Biological process	Carbohydrate metabolism Polysaccharide degradation RuleBase RU000509V3
Molecular function	Glycosidase RuleBase RU000509V3 Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	starch catabolic process Inferred from mutant phenotype. Source: TAIR
Molecular function	beta-amylase activity Inferred from electronic annotation. Source: InterPro cation binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	Q9LIR6-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: CDCF1007217789A0	FASTA	575	63,762
	10 20 30 40 50 60 MALNLSHQLG VLAGTPIKSG EMTDSSLLSI SPPSARMMTP KAMNRNYKAH GTDPSPPMSP 70 80 90 100 110 120 ILGATRADLS VACKAFAVEN GIGTIEEQRT YREGGIGGKK EGGGGVPVFV MMPLDSVTMG 130 140 150 160 170 180 NTVNRRKAMK ASLQALKSAG VEGIMIDVWW GLVEKESPGT YNWGGYNELL ELAKKLGLKV 190 200 210 220 230 240 QAVMSFHQCG GNVGDSVTIP LPQWVVEEVD KDPDLAYTDQ WGRRNHEYIS LGADTLPVLK 250 260 270 280 290 300 GRTPVQCYAD FMRAFRDNFK HLLGETIVEI QVGMGPAGEL RYPSYPEQEG TWKFPGIGAF 310 320 330 340 350 360 QCYDKYSLSS LKAAAETYGK PEWGSTGPTD AGHYNNWPED TQFFKKEGGG WNSEYGDFFL 370 380 390 400 410 420 SWYSQMLLDH GERILSSAKS IFENMGVKIS VKIAGIHWHY GTRSHAPELT AGYYNTRFRD 430 440 450 460 470 480 GYLPIAQMLA RHNAIFNFTC IEMRDHEQPQ DALCAPEKLV NQVALATLAA EVPLAGENAL 490 500 510 520 530 540 PRYDDYAHEQ ILKASALNLD QNNEGEPREM CAFTYLRMNP ELFQADNWGK FVAFVKKMGE 550 560 570 GRDSHRCREE VEREAEHFVH VTQPLVQEAA VALTH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC clones." Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S. DNA Res. 7:217-221(2000) [PubMed: 10907853] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[2]	Kaneko T., Kato T., Sato S., Nakamura Y., Asamizu E., Tabata S. Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE.
[3]	"Site-specific phosphorylation profiling of Arabidopsis proteins by mass spectrometry and peptide chip analysis." de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E., Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H. J. Proteome Res. 7:2458-2470(2008) [PubMed: 18433157] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[4]	"Arabidopsis Open Reading Frame (ORF) Clones." Yamada K., Banh J., Chan M.M., Chang C.H., Chang E., Dale J.M., Deng J.M., Goldsmith A.D., Lee J.M., Onodera C.S., Quach H.L., Tang C., Toriumi M., Wu H.C., Yamamura Y., Yu G., Bowser L., Carninci P. , Chen H., Cheuk R., Hayashizaki Y., Ishida J., Jones T., Kamiya A., Karlin-Neumann G., Kawai J., Kim C., Lam B., Lin J., Meyers M.C., Miranda M., Narusaka M., Nguyen M., Palm C.J., Sakurai T., Satou M., Seki M., Shinn P., Southwick A., Shinozaki K., Davis R.W., Ecker J.R., Theologis A. Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE.
[5]	"Arabidopsis cDNA clones." Cheuk R., Chen H., Kim C.J., Meyers M.C., Banh J., Bowser L., Carninci P., Chang E., Dale J.M., Goldsmith A.D., Hayashizaki Y., Ishida J., Jones T., Kamiya A., Karlin-Neumann G., Kawai J., Lam B., Lee J.M. , Lin J., Miranda M., Narusaka M., Nguyen M., Onodera C.S., Palm C.J., Quach H.L., Sakurai T., Satou M., Seki M., Southwick A., Tang C.C., Toriumi M., Wu H.C., Yamada K., Yamamura Y., Yu G., Yu S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE.
[6]	"Arabidopsis Full Length cDNA Clones." Yamada K., Liu S.X., Sakano H., Pham P.K., Banh J., Chung M.K., Goldsmith A.D., Lee J.M., Quach H.L., Toriumi M., Yu G., Bowser L., Carninci P., Chen H., Cheuk R., Hayashizaki Y., Ishida J., Jones T. , Kamiya A., Karlin-Neumann G., Kawai J., Kim C., Lam B., Lin J., Miranda M., Narusaka M., Nguyen M., Palm C.J., Sakurai T., Satou M., Seki M., Shinn P., Southwick A., Shinozaki K., Davis R.W., Ecker J.R., Theologis A. Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE.
[7]	"Arabidopsis cDNA clones." Shinn P., Chen H., Cheuk R., Kim C.J., Meyers M.C., Banh J., Bowser L., Carninci P., Chung M.K., Goldsmith A.D., Hayashizaki Y., Ishida J., Jones T., Kamiya A., Karlin-Neumann G., Kawai J., Lam B., Lee J.M. , Lin J., Liu S.X., Miranda M., Narusaka M., Nguyen M., Palm C.J., Pham P.K., Quach H.L., Sakano H., Sakurai T., Satou M., Seki M., Southwick A., Toriumi M., Yamada K., Yu G., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF367293 mRNA. Translation: AAK56281.1. AY074393 mRNA. Translation: AAL67089.1. AY078046 mRNA. Translation: AAL77747.1. AY096517 mRNA. Translation: AAM20167.1. AP001297 Genomic DNA. Translation: BAB03009.1.
IPI	IPI00518242.
RefSeq	NP_189034.1.
UniGene	At.8278
3D structure databases
HSSP	HSSP built from PDB template 1B1Y based on UniProtKB P16098.
ModBase	Search...
Protein family/group databases
CAZy	GH14. Glycoside Hydrolase Family 14.
Proteomic databases
PRIDE	Q9LIR6.
Genome annotation databases
GeneID	821975.
KEGG	ath:AT3G23920.
NMPDR	fig|3702.1.peg.14650.
Organism-specific databases
TAIR	At3g23920.
Phylogenomic databases
OMA	Q9LIR6. DKDQDLA.
Enzyme and pathway databases
BRENDA	3.2.1.2. 302.
Gene expression databases
ArrayExpress	Q9LIR6.
Family and domain databases
InterPro	IPR001554. Glyco_hydro_14. IPR018238. Glyco_hydro_14_CS. IPR001371. Glyco_hydro_14B_pln. IPR013781. Glyco_hydro_sg_catalytic. [Graphical view]
Gene3D	G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
Pfam	PF01373. Glyco_hydro_14. 1 hit. [Graphical view]
PRINTS	PR00750. BETAAMYLASE. PR00842. GLHYDLASE14B.
PROSITE	PS00506. BETA_AMYLASE_1. 1 hit. PS00679. BETA_AMYLASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

Q9LIR6_ARATH

Accession

Primary (citable) accession number: Q9LIR6

Entry history

Integrated into UniProtKB/TrEMBL:	October 1, 2000
Last sequence update:	October 1, 2000
Last modified:	June 16, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)