Q42656 (AGAL_COFAR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Alpha-galactosidase EC=3.2.1.22 Alternative name(s): Alpha-D-galactoside galactohydrolase Melibiase
Organism	Coffea arabica (Arabian coffee)
Taxonomic identifier	13443 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Gentianales › Rubiaceae › Ixoroideae › Coffeeae › Coffea

Protein attributes

Sequence length	378 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)

Function	Preferentially cleaves alpha-1,3 and alpha-1,4 glycoside linkages. Involved in the hydrolysis of the galactomannan, it splits alpha-linked galactose moieties. It is particularly suitable for the hydrolysis of guar gum to a gum with improved gelling properties. Can cleave terminal alpha-1,3-linked galactose residues responsible for blood group B specificity from the surface of erythrocytes thereby converting these cells serologically to group O.
Catalytic activity	Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids.
Biotechnological use	Used to convert human blood group antigens of type B into type O, the universal donor type. Ref.2 Ref.3 Ref.4
Sequence similarities	Belongs to the glycosyl hydrolase 27 family.

Ontologies

Keywords
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	cation binding Inferred from electronic annotation. Source: InterPro raffinose alpha-galactosidase 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 – 15	15	Ref.1
	Chain	16 – 378	363	Alpha-galactosidase		PRO_0000001001
Regions
	Region	178 – 182	5	Substrate binding By similarity
Sites
	Active site	145	1	Nucleophile By similarity
	Active site	200	1	Proton donor By similarity
Amino acid modifications
	Disulfide bond	36 ↔ 68		By similarity
	Disulfide bond	116 ↔ 147		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q42656 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 9FC7610BFD760AE3	FASTA	378	41,310
	10 20 30 40 50 60 MVKSPGTEDY TRRSLLANGL GLTPPMGWNS WNHFRCNLDE KLIRETADAM VSKGLAALGY 70 80 90 100 110 120 KYINLDDCWA ELNRDSQGNL VPKGSTFPSG IKALADYVHS KGLKLGIYSD AGTQTCSKTM 130 140 150 160 170 180 PGSLGHEEQD AKTFASWGVD YLKYDNCNNN NISPKERYPI MSKALLNSGR SIFFSLCEWG 190 200 210 220 230 240 EEDPATWAKE VGNSWRTTGD IDDSWSSMTS RADMNDKWAS YAGPGGWNDP DMLEVGNGGM 250 260 270 280 290 300 TTTEYRSHFS IWALAKAPLL IGCDIRSMDG ATFQLLSNAE VIAVNQDKLG VQGNKVKTYG 310 320 330 340 350 360 DLEVWAGPLS GKRVAVALWN RGSSTATITA YWSDVGLPST AVVNARDLWA HSTEKSVKGQ 370 ISAAVDAHDS KMYVLTPQ

References

[1]	"Cloning and functional expression of a cDNA encoding coffee bean alpha-galactosidase." Zhu A., Goldstein J. Gene 140:227-231(1994) [PubMed: 8144030] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 16-34; 215-231 AND 373-378. Tissue: Seed.
[2]	"Characterization of recombinant alpha-galactosidase for use in seroconversion from blood group B to O of human erythrocytes." Zhu A., Leng L., Monahan C., Zhang Z., Hurst R., Lenny L., Goldstein J. Arch. Biochem. Biophys. 327:324-329(1996) [PubMed: 8619622] [Abstract] Cited for: BIOTECHNOLOGY.
[3]	"Transfusion to blood group A and O patients of group B RBCs that have been enzymatically converted to group O." Kruskall M.S., AuBuchon J.P., Anthony K.Y., Herschel L., Pickard C., Biehl R., Horowitz M., Brambilla D.J., Popovsky M.A. Transfusion 40:1290-1298(2000) [PubMed: 11099655] [Abstract] Cited for: BIOTECHNOLOGY.
[4]	"B to O erythrocyte conversion by the recombinant alpha-galactosidase." Zhang Y.P., Gong F., Bao G.Q., Gao H.W., Ji S.P., Tan Y.X., Li S.B., Li L.L., Wang Y.L., Xu H., Xu L.J., Tian S.G., Zhang Z.X., Lu Q.S., Qiu Y., Bai J.S., Chen J.T. Chin. Med. J. 120:1145-1150(2007) [PubMed: 17637242] [Abstract] Cited for: BIOTECHNOLOGY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L27992 mRNA. Translation: AAA33022.1.
PIR	T50781.
3D structure databases
ProteinModelPortal	Q42656.
SMR	Q42656. Positions 18-377.
ModBase	Search...
Protein family/group databases
CAZy	GH27. Glycoside Hydrolase Family 27.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR013785. Aldolase_TIM. IPR013780. Glyco_hydro_13_b. IPR002241. Glyco_hydro_27. IPR000111. Glyco_hydro_GHD. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit. G3DSA:2.60.40.1180. Glyco_hydro_13_b. 1 hit.
Pfam	PF02065. Melibiase. 1 hit. [Graphical view]
PRINTS	PR00740. GLHYDRLASE27.
SUPFAM	SSF51445. Glyco_hydro_cat. 1 hit.
PROSITE	PS00512. ALPHA_GALACTOSIDASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AGAL_COFAR

Accession

Primary (citable) accession number: Q42656

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	July 27, 2011
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program