GLAA_STRGU
ID GLAA_STRGU Reviewed; 727 AA.
AC B1V8K7;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 25-MAY-2022, entry version 52.
DE RecName: Full=Alpha-1,3-galactosidase A;
DE EC=3.2.1.n1 {ECO:0000269|PubMed:17401360};
DE AltName: Full=Exo-alpha-galactosidase A;
DE EC=3.2.1.22 {ECO:0000269|PubMed:17401360};
DE AltName: Full=SgGal110A;
GN Name=glaA; Synonyms=gla;
OS Streptacidiphilus griseoplanus (Streptomyces griseoplanus).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptacidiphilus.
OX NCBI_TaxID=66896;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ENZYME ACTIVITY.
RX PubMed=18227066; DOI=10.1074/jbc.m709020200;
RA Liu Q.P., Yuan H., Bennett E.P., Levery S.B., Nudelman E., Spence J.,
RA Pietz G., Saunders K., White T., Olsson M.L., Henrissat B.,
RA Sulzenbacher G., Clausen H.;
RT "Identification of a GH110 subfamily of alpha1,3-galactosidases: novel
RT enzymes for removal of the alpha3Gal xenotransplantation antigen.";
RL J. Biol. Chem. 283:8545-8554(2008).
RN [2]
RP PROTEIN SEQUENCE OF 34-77; 144-153; 273-280 AND 489-497, AND CATALYTIC
RP ACTIVITY.
RX PubMed=17401360; DOI=10.1038/nbt1298;
RA Liu Q.P., Sulzenbacher G., Yuan H., Bennett E.P., Pietz G., Saunders K.,
RA Spence J., Nudelman E., Levery S.B., White T., Neveu J.M., Lane W.S.,
RA Bourne Y., Olsson M.L., Henrissat B., Clausen H.;
RT "Bacterial glycosidases for the production of universal red blood cells.";
RL Nat. Biotechnol. 25:454-464(2007).
CC -!- FUNCTION: Alpha-galactosidase that specifically removes branched alpha-
CC 1,3-linked galactose residues present in blood group B antigens. Has no
CC activity toward linear alpha-1,3-linked galactose residues.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing branched (1->3)-alpha-D-
CC galactosidic residues, producing free D-galactose.; EC=3.2.1.n1;
CC Evidence={ECO:0000269|PubMed:17401360};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing alpha-D-galactose
CC residues in alpha-D-galactosides, including galactose
CC oligosaccharides, galactomannans and galactolipids.; EC=3.2.1.22;
CC Evidence={ECO:0000269|PubMed:17401360};
CC -!- BIOTECHNOLOGY: Specifically cleaves the branched blood group B antigen
CC at neutral pH with low consumption of recombinant enzyme. It is
CC therefore a good candidate to participate in the development of
CC universal red blood cells by removing blood group B antigen.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 110 family. A subfamily.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=The juice of life - Issue 98
CC of October 2008;
CC URL="https://web.expasy.org/spotlight/back_issues/098";
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DR EMBL; AM259273; CAJ90659.1; -; Genomic_DNA.
DR AlphaFoldDB; B1V8K7; -.
DR SMR; B1V8K7; -.
DR CAZy; GH110; Glycoside Hydrolase Family 110.
DR GO; GO:0052692; F:raffinose alpha-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.160.20.10; -; 2.
DR InterPro; IPR039448; Beta_helix.
DR InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR InterPro; IPR006626; PbH1.
DR InterPro; IPR024535; Pectate_lyase_SF_prot.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR Pfam; PF13229; Beta_helix; 1.
DR Pfam; PF12708; Pectate_lyase_3; 1.
DR SMART; SM00710; PbH1; 6.
DR SUPFAM; SSF49373; SSF49373; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycosidase; Hydrolase; Repeat.
FT CHAIN 1..727
FT /note="Alpha-1,3-galactosidase A"
FT /id="PRO_0000348460"
FT REPEAT 336..358
FT /note="PbH1 1"
FT REPEAT 461..483
FT /note="PbH1 2"
FT REPEAT 484..506
FT /note="PbH1 3"
FT REPEAT 517..538
FT /note="PbH1 4"
FT REPEAT 551..572
FT /note="PbH1 5"
FT REPEAT 574..603
FT /note="PbH1 6"
FT REGION 220..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 66
FT /note="G -> I (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="T -> G (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 492
FT /note="N -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 496
FT /note="G -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 727 AA; 78244 MW; 059E250ED79FB764 CRC64;
MGTATAQPAL RPQTSTVIGG LHGAAVLDNT GRTVIDVTDF GADPSGKADS AAAVSAAMAH
AKTVGGPTTL HFPTGTYHIW PERTPKRELY VSNTVGSDQA FRTKNIGILV EDMRDVVVDG
GGSRIVNHGF QTVFAAIRSS DVRFTNFSQT WVAPKTVDIT VADAGVVSGQ AYRIIDIPET
YDYAVEGTSV RWNGERGPAT GQPYWTGTNS FDYSQVHDPA TNRTWRTSNP VFPERHEDHR
PRRRQVRITY GDSTAPGDRG YVYQMREVTR DTPGALFWES SRVTVDHLRL GYLHGFGIVG
QLSEDIGIDS VTFKADRGSG RVTSGFADHI QMSGVKGTVR ITNSVFDNPQ DDPINIHGTY
LQATAAERET LQLRYMHNET SGFPQFYPGD TIELVDKRTM LAAPGATAKV VSVTGPTGSG
VPAGTDPDTY LRTMTVVLDR TLPAAVLAAP GDYVAENTTY TPTVEITGNT FQAVPTRGIL
VTTRRPVRIE NNRFDGMSMA SIYISSDARS WYESGPVRNV TIRGNVFDRP ASPVIFFDPT
NQDFVAGQPV HRNVLIEDND FNLTGGTILS GRGVGGLTFR DNRVERYPHL RLTGPSRALR
VGDTTTVTTD APPPSHTSPL FTFDGADDIT LANNTYGNGF NKRVNTANMD VSEITVTADG
LALNADSISS APVAVSYSSS RPKVATVDSE GVVKALSGGT TSITARATIG GVRVTSNPVK
VVVATER
