GLAA_STRAW
ID GLAA_STRAW Reviewed; 625 AA.
AC Q826C5; A4Q8G4;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Alpha-1,3-galactosidase A;
DE EC=3.2.1.n1;
DE AltName: Full=Exo-alpha-galactosidase A;
DE EC=3.2.1.22;
DE AltName: Full=SaGal110A;
DE Flags: Precursor;
GN Name=glaA; OrderedLocusNames=SAV_7268;
OS Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC
OS 14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=227882;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=11572948; DOI=10.1073/pnas.211433198;
RA Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M.,
RA Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M.;
RT "Genome sequence of an industrial microorganism Streptomyces avermitilis:
RT deducing the ability of producing secondary metabolites.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL
RC 8165 / MA-4680;
RX PubMed=12692562; DOI=10.1038/nbt820;
RA Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA Sakaki Y., Hattori M., Omura S.;
RT "Complete genome sequence and comparative analysis of the industrial
RT microorganism Streptomyces avermitilis.";
RL Nat. Biotechnol. 21:526-531(2003).
RN [4]
RP 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).
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:18227066};
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:18227066};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 110 family. A subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM109953; CAJ33349.1; -; Genomic_DNA.
DR EMBL; BA000030; BAC74979.1; -; Genomic_DNA.
DR RefSeq; WP_010988663.1; NZ_JZJK01000085.1.
DR AlphaFoldDB; Q826C5; -.
DR SMR; Q826C5; -.
DR STRING; 227882.SAV_7268; -.
DR CAZy; GH110; Glycoside Hydrolase Family 110.
DR EnsemblBacteria; BAC74979; BAC74979; SAVERM_7268.
DR KEGG; sma:SAVERM_7268; -.
DR eggNOG; COG5434; Bacteria.
DR HOGENOM; CLU_017693_0_0_11; -.
DR OrthoDB; 1217730at2; -.
DR Proteomes; UP000000428; Chromosome.
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; IPR006626; PbH1.
DR InterPro; IPR024535; Pectate_lyase_SF_prot.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR Pfam; PF12708; Pectate_lyase_3; 1.
DR SMART; SM00710; PbH1; 5.
DR SUPFAM; SSF51126; SSF51126; 1.
PE 3: Inferred from homology;
KW Glycosidase; Hydrolase; Reference proteome; Repeat; Signal.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..625
FT /note="Alpha-1,3-galactosidase A"
FT /id="PRO_0000348474"
FT REPEAT 342..364
FT /note="PbH1 1"
FT REPEAT 460..482
FT /note="PbH1 2"
FT REPEAT 483..505
FT /note="PbH1 3"
FT REPEAT 516..537
FT /note="PbH1 4"
FT REPEAT 573..611
FT /note="PbH1 5"
SQ SEQUENCE 625 AA; 67184 MW; 4B80A1A6C94D372E CRC64;
MAHGCSGGAM SRFVFLGVAL ALLGGATSPA AAAPRVTPVV VDVDDYGADP TGRTDSTPAV
AAALRHAKSV DRPVRIVFSK GTYQLYPERA ETRELYMSNT VGADQRYRDK KIGLLVEDMH
DVTVDGGGAK LVHHGLQTAF ASIRSTDVTF QNFSFDYAAP EVIDATVATT GVTDGHAYRV
LKIPAGSPYR VNGTHITWLG ETSPATGQPY WSGVDGLQYT QIHDPEAQRT WRGDNPLFND
VAAVTDLGGR RIRIDYTTAA RPADAGLVYQ MRLIERTEPG AFIWESKNVT MRSMNAYYLQ
SFGVVGQFSE NISIDKVNFA PDPRSGRSTA SFADFVQMSG VKGKVSITRS LFDGPHDDPI
NIHGTYLEVV GKPGPSTLTL AYKHPQTAGF PQFAPGDEVE FATKRTMTPL ADAHAQVTAV
DGPSGMDHTK PLTTMTVTFD RPVPAGVETG GTVVENITAT PSVVISGNVF RNVPTRGILV
TTRKPVLITG NRFDGMSMAS IYVSADAYQW YESGPVADLT IRGNSFTRPS GPVIFVEPTN
QVIDPATPVH HNISVEHNSF DIGDVTVVNA KSVGGFAFTG NTVRRLDGAD HPPYTSPLFV
FHGSSGIRIA RNHYDKGLNT SVVTD
