ID A0A1Q3PXD7_9BACT Unreviewed; 450 AA.
AC A0A1Q3PXD7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Alpha-galactosidase {ECO:0000256|RuleBase:RU361168};
DE EC=3.2.1.22 {ECO:0000256|RuleBase:RU361168};
DE AltName: Full=Melibiase {ECO:0000256|RuleBase:RU361168};
GN ORFNames=BGO32_00430 {ECO:0000313|EMBL:OJV25714.1};
OS Bacteroidetes bacterium 37-13.
OC Bacteria; Bacteroidota.
OX NCBI_TaxID=1895921 {ECO:0000313|EMBL:OJV25714.1, ECO:0000313|Proteomes:UP000185627};
RN [1] {ECO:0000313|EMBL:OJV25714.1, ECO:0000313|Proteomes:UP000185627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=37-13 {ECO:0000313|EMBL:OJV25714.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|RuleBase:RU361168};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 27 family.
CC {ECO:0000256|ARBA:ARBA00009743, ECO:0000256|RuleBase:RU361168}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OJV25714.1}.
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DR EMBL; MKTC01000031; OJV25714.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3PXD7; -.
DR STRING; 1895921.BGO32_00430; -.
DR Proteomes; UP000185627; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProt.
DR GO; GO:0004557; F:alpha-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd14792; GH27; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR002241; Glyco_hydro_27.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR041233; Melibiase_C.
DR PANTHER; PTHR11452:SF75; ALPHA-GALACTOSIDASE; 1.
DR PANTHER; PTHR11452; ALPHA-GALACTOSIDASE/ALPHA-N-ACETYLGALACTOSAMINIDASE; 1.
DR Pfam; PF05345; He_PIG; 1.
DR Pfam; PF16499; Melibiase_2; 1.
DR Pfam; PF17801; Melibiase_C; 1.
DR PRINTS; PR00740; GLHYDRLASE27.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49313; Cadherin-like; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|RuleBase:RU361168};
KW Glycosidase {ECO:0000256|RuleBase:RU361168};
KW Hydrolase {ECO:0000256|RuleBase:RU361168}.
FT DOMAIN 380..448
FT /note="Alpha galactosidase C-terminal beta sandwich"
FT /evidence="ECO:0000259|Pfam:PF17801"
SQ SEQUENCE 450 AA; 50176 MW; 9E5FC6AC73515FAF CRC64;
MVGNYPNTFF LHTIAATGEK PIVFTAKELP VGLSLDVSTG IIYGTAPKAG IYKVEVSATN
KSGTSTQTLE LNIGEKLALT PPMGWNSWNV FTSDIDEKII MEIADAMVNT GMRDAGYEYI
NIDDYWHADT READGKPKVD EKKFPNGMKH VADYVHSKGL KLGIYSCASE FTCGRRFGGY
GYEEIDAKTY AEWGIDLLKY DYCFAPWNRK TAIERYTKMG EALKNSGRSI VFSICEWGVR
KPWKWGAAAG GSYWRTTFDI FDHWKGNNPF QLSVMQILKQ QIGLEKYAAP GAWNDPDMLI
VGNYGKGNAT SARGKFKGLS DTEYQSHFAL WCMLNSPLLS SCDLRNMNDA TKNILLNNEL
IALNQDIEGK QATLVSKKKG IWVYKKELSD GVAYAVFNTN SKQKSFVVSE LIEKKIKGTV
KDLVSGKVVS NSGEAINLDA HQTFVFKVNR
//
