Q034G9 (PAGL2_LACC3) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
6-phospho-alpha-glucosidase 2
EC=3.2.1.122

Gene names

Ordered Locus Names:

LSEI_2684

Organism

Lactobacillus casei (strain ATCC 334) [Complete proteome] [HAMAP]

Taxonomic identifier

321967 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Lactobacillales › Lactobacillaceae › Lactobacillus › Lactobacillus casei group › Lactobacillus casei

Protein attributes

Sequence length	461 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	Maltose 6'-phosphate + H2O = D-glucose + D-glucose 6-phosphate.
Cofactor	Binds 1 divalent metal ion per subunit. Manganese By similarity. Binds 1 NAD+ per subunit By similarity.
Sequence similarities	Belongs to the glycosyl hydrolase 4 family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Ligand	Manganese Metal-binding NAD
Molecular function	Glycosidase Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	maltose-6'-phosphate glucosidase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW nucleotide binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 461	461	6-phospho-alpha-glucosidase 2		PRO_0000389205
Regions
	Nucleotide binding	7 – 73	67	NAD By similarity
Sites
	Active site	173	1	Proton donor By similarity
	Active site	267	1	Proton acceptor By similarity
	Metal binding	172	1	Manganese By similarity
	Metal binding	202	1	Manganese By similarity
	Binding site	96	1	Substrate By similarity
	Binding site	150	1	Substrate By similarity
	Binding site	287	1	Substrate By similarity
	Site	112	1	Increases basicity of active site Tyr By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q034G9 [UniParc]. Last modified November 14, 2006. Version 1. Checksum: F96D99955DA75E84	FASTA	461	52,030
	10 20 30 40 50 60 MNQNKQFSIV IAGGGSTYTA GIVMMLLENA ERFPLRALKL YDIDEERQAT IAEAIAIELK 70 80 90 100 110 120 EKAPAIDFTW TTDPQTAFTD VDFCFAHIRS GGYKMREQDE KIPLKHHVVG QETCGPGGIA 130 140 150 160 170 180 YGMRSIGDII ELIDFIEKYS PDCWMLNYSN PASIVAEACR RLRPDAKILN ICDMPVGTQR 190 200 210 220 230 240 RMSQIIGLQP KDLEVRYFGM NHFGWWTSVK DKAGNEYLPQ IRDYVAHHGY LTQIEVDTQH 250 260 270 280 290 300 MDASWQATHK KAQDLLAVDP HYLPNTYLKY YLYPDYVVAH SDPDYTRANE VEDGREKCVF 310 320 330 340 350 360 SAAQKIIDAG TSDVGSFPID SHASFIVDLA CAIAFNTHER MLLIVENNGA VANIDDNIMV 370 380 390 400 410 420 EVPCIVGKDG AEPLTQGKIP MFQRGMILNQ AMVEKLVVDA WINHDYQELW QALTLSKTLP 430 440 450 460 SAQVAKEVLD DLIEANREYW PELKHDEHEV HLISESAVSE I

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Comparative genomics of the lactic acid bacteria." Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V., Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V., Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M., Hawkins T. , Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A., Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W., Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y., Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R., O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T., Richardson P., Kozyavkin S., Weimer B.C., Mills D.A. Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 334.
[2]	"The sim operon facilitates the transport and metabolism of sucrose isomers in Lactobacillus casei ATCC 334." Thompson J., Jakubovics N., Abraham B., Hess S., Pikis A. J. Bacteriol. 190:3362-3373(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000423 Genomic DNA. Translation: ABJ71403.1.
RefSeq	YP_807845.1. NC_008526.1.
3D structure databases
ProteinModelPortal	Q034G9.
SMR	Q034G9. Positions 5-443.
ModBase	Search...
Protein-protein interaction databases
STRING	321967.LSEI_2684.
Protein family/group databases
CAZy	GH4. Glycoside Hydrolase Family 4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABJ71403; ABJ71403; LSEI_2684.
GeneID	4421236.
KEGG	lca:LSEI_2684.
PATRIC	22209078. VBILacCas62221_2628.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1486.
HOGENOM	HOG000239810.
KO	K01232.
OMA	GHSSAGE.
ProtClustDB	CLSK880767.
Enzyme and pathway databases
BioCyc	LCAS321967:GH4S-2605-MONOMER.
Family and domain databases
Gene3D	3.40.50.720. 1 hit. 3.90.110.10. 1 hit.
InterPro	IPR019802. GlycHydrolase_4_CS. IPR001088. Glyco_hydro_4. IPR022616. Glyco_hydro_4_C. IPR015955. Lactate_DH/Glyco_Ohase_4_C. IPR016040. NAD(P)-bd_dom. [Graphical view]
Pfam	PF02056. Glyco_hydro_4. 1 hit. PF11975. Glyco_hydro_4C. 1 hit. [Graphical view]
PRINTS	PR00732. GLHYDRLASE4.
SUPFAM	SSF56327. Lactate_DH/Glyco_hydro_4_C. 1 hit.
PROSITE	PS01324. GLYCOSYL_HYDROL_F4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PAGL2_LACC3

Accession

Primary (citable) accession number: Q034G9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 24, 2009
Last sequence update:	November 14, 2006
Last modified:	May 1, 2013
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program