GLAA_SHEWM
ID GLAA_SHEWM Reviewed; 608 AA.
AC B1KD83;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 71.
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 Flags: Precursor;
GN Name=glaA; OrderedLocusNames=Swoo_3656;
OS Shewanella woodyi (strain ATCC 51908 / MS32).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=392500;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51908 / MS32;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Lykidis A., Zhao J.-S., Richardson P.;
RT "Complete sequence of Shewanella woodyi ATCC 51908.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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 (By
CC similarity). {ECO:0000250}.
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 -!- 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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 110 family. A subfamily.
CC {ECO:0000305}.
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DR EMBL; CP000961; ACA87918.1; -; Genomic_DNA.
DR RefSeq; WP_012326251.1; NC_010506.1.
DR AlphaFoldDB; B1KD83; -.
DR SMR; B1KD83; -.
DR STRING; 392500.Swoo_3656; -.
DR CAZy; GH110; Glycoside Hydrolase Family 110.
DR EnsemblBacteria; ACA87918; ACA87918; Swoo_3656.
DR KEGG; swd:Swoo_3656; -.
DR eggNOG; COG5434; Bacteria.
DR HOGENOM; CLU_017693_0_0_6; -.
DR OrthoDB; 1217730at2; -.
DR Proteomes; UP000002168; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; IPR006626; PbH1.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR Pfam; PF13229; Beta_helix; 1.
DR SMART; SM00710; PbH1; 5.
DR SUPFAM; SSF51126; SSF51126; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell membrane; Glycosidase; Hydrolase; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Repeat; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 22..608
FT /note="Alpha-1,3-galactosidase A"
FT /id="PRO_5000316297"
FT REPEAT 262..292
FT /note="PbH1 1"
FT REPEAT 318..340
FT /note="PbH1 2"
FT REPEAT 426..448
FT /note="PbH1 3"
FT REPEAT 449..470
FT /note="PbH1 4"
FT REPEAT 481..507
FT /note="PbH1 5"
FT LIPID 22
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 22
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ SEQUENCE 608 AA; 68216 MW; 6691BAA70326DB2A CRC64;
MQRRTFIKSI SAMMATSTTL GCVSNSLATE KHVSITDFGL RPNSGDDAIP ALQKALAYCK
KHPGTSLIFP LGRYDFWSTK ADRDFYYISN NDDGIKPVAF PLTEFKNLII DGQGSRFVFH
GGMVPVIVRE SSGITLKNFS VDWDVPFHCE GIVEAVNKKE SYVDLKIKDG FSYKVENGRF
IFVGEGFENP VIKNLLEFDT KRQKQAYMAR DNFQREIQPV TTEIRPGVLR LQGKYPTWPK
VGNTLLLMQE RRDWPAFSVQ DTKNTWLENI DIHHSGAMGV IAQLADGIKL DNVNIHPKDG
SGRTVSTTVD ATHFINCKGH VVLKDCLFQG QIDDGTNVHG MYARVAEIHD SNTITFELVH
YQQLGIDIFK PGSKVNFSDS VLNVFHDNVV DKTVRQDAKY WTVSFKEPLD TALKVDDVLD
NMTWQPDHVM ISGCRFTGNR ARGALLTVSG KIIVENNYFS TPMMAIKIGS GGLKWYESGP
VESVEIRNNI FDNCNYAKDS SAIDIVPGRK SKATTPYHQN VKIYQNEFRV YNERVLTTSR
TQGISFVSNK IVKTSEYPER KSAFAPIHVE RSSNFVYQGN DFIGFGHSEL LFIDGQLVSG
SGKLEGEG