Q97DP6 (PAGL_CLOAB) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phospho-alpha-glucosidase pagL
EC=3.2.1.-

Gene names

Name:	pagL
Ordered Locus Names:	CA_C3426

Organism

Clostridium acetobutylicum

Taxonomic identifier

1488 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	445 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Phospho-alpha-glucosidase that catalyzes the hydrolysis of p-nitrophenyl-alpha-D-glucopyranoside 6-phosphate, but is not able to cleave 'natural' phospho-alpha-glucosides produced via the phosphoenolpyruvate-dependent sugar phosphotransferase system (PEP-PTS).
Cofactor	Binds 1 NAD per subunit. Binds 1 manganese ion per subunit.
Subunit structure	Homotetramer.
Induction	By maltose and methyl-alpha-D-glucoside.
Sequence similarities	Belongs to the glycosyl hydrolase 4 family.
Biophysicochemical properties	Kinetic parameters: KM=58.3 µM for p-nitrophenyl-alpha-D-glucopyranoside 6-phosphate Ref.2 Vmax=4.4 µmol/min/mg enzyme with p-nitrophenyl 6-phospho-alpha-D-glucoside as substrate

Ontologies

Keywords
Ligand	Manganese Metal-binding NAD
Molecular function	Glycosidase Hydrolase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	hydrolase activity, hydrolyzing O-glycosyl compounds Inferred from electronic annotation. Source: InterPro 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 – 445	445	Phospho-alpha-glucosidase pagL		PRO_0000169865
Regions
	Nucleotide binding	4 – 71	68	NAD By similarity
Sites
	Active site	172	1	Proton donor By similarity
	Active site	264	1	Proton acceptor By similarity
	Metal binding	171	1	Manganese By similarity
	Metal binding	201	1	Manganese By similarity
	Binding site	94	1	Substrate By similarity
	Binding site	148	1	Substrate By similarity
	Binding site	284	1	Substrate By similarity
	Site	110	1	Increases basicity of active site Tyr By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q97DP6 [UniParc]. Last modified October 1, 2001. Version 1. Checksum: 49FA5F7EE968BF39	FASTA	445	51,156
	10 20 30 40 50 60 MKKYSICIVG GGSRYTPDML AMLCNQKERF PLRKIVLYDN ESERQETVGN YAKILFKEYY 70 80 90 100 110 120 PELEEVIWTT DEKEAFEDID FALMQIRAGR LKMREKDEKI SLKHGCLGQE TCGAGGFAYG 130 140 150 160 170 180 LRSVPAVIDL IKSIRTYSPK CWILNYSNPA AIVAEATKRV FPNDYRIINI CDMPIAIMDI 190 200 210 220 230 240 YAAVLGLKRR DLEPKYFGLN HFGWFTHILD KKTGENYLPK LREILKTPVD VQTEPLFQEK 250 260 270 280 290 300 SWKSTFEFMS QMINDYDEYL PNTYLQYYLY PAKMRNKENP EYTRANEVMD GNEKETYERM 310 320 330 340 350 360 HKIISLGKIH GTKYELTSDV GCHAEYIVDL ATAIANNTNE IFLIITENKG TINNVSKDMM 370 380 390 400 410 420 VEVPCRVGSN GVEPLVVGSI PAFYKGLMEN QYAYEKLSVD ACLEGSYQKA LQALVLNRTV 430 440 VNTDVAKELL KDLIEANKGY WNELH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genome sequence and comparative analysis of the solvent-producing bacterium Clostridium acetobutylicum." Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R., Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F., Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V., Smith D.R. J. Bacteriol. 183:4823-4838(2001) [PubMed: 11466286] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787.
[2]	"Genes malh and pagl of Clostridium acetobutylicum ATCC 824 encode NAD+- and Mn2+-dependent phospho-alpha-glucosidase(s)." Thompson J., Hess S., Pikis A. J. Biol. Chem. 279:1553-1561(2004) [PubMed: 14570887] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-29, CHARACTERIZATION, KINETIC PARAMETERS. Strain: ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE001437 Genomic DNA. Translation: AAK81356.1.
PIR	A97321.
RefSeq	NP_350016.1. NC_003030.1.
3D structure databases
ProteinModelPortal	Q97DP6.
ModBase	Search...
Protein family/group databases
CAZy	GH4. Glycoside Hydrolase Family 4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1119608.
GenomeReviews	Gene locus CA_C3426 in contig AE001437_GR.
KEGG	cac:CA_C3426.
NMPDR	fig|272562.1.peg.3545.
PATRIC	32041289. VBICloAce74127_3608.
Phylogenomic databases
HOGENOM	HBG511715.
OMA	NDYDEYL.
PhylomeDB	Q97DP6.
ProtClustDB	CLSK880767.
Enzyme and pathway databases
BioCyc	CACE272562:CAC3426-MONOMER.
BRENDA	3.2.1.122. 1452.
Family and domain databases
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]
Gene3D	G3DSA:3.90.110.10. lact_mal_DH. 1 hit. G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KO	K01222.
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

PAGL_CLOAB

Accession

Primary (citable) accession number: Q97DP6

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 15, 2005
Last sequence update:	October 1, 2001
Last modified:	January 25, 2012
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program