ID A0A1M3HG45_9SPHI Unreviewed; 776 AA.
AC A0A1M3HG45;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=BGO55_14460 {ECO:0000313|EMBL:OJW57486.1};
OS Sphingobacteriales bacterium 50-39.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX NCBI_TaxID=1895841 {ECO:0000313|EMBL:OJW57486.1, ECO:0000313|Proteomes:UP000184242};
RN [1] {ECO:0000313|EMBL:OJW57486.1, ECO:0000313|Proteomes:UP000184242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=50-39 {ECO:0000313|EMBL:OJW57486.1};
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:OJW57486.1}.
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DR EMBL; MKTZ01000011; OJW57486.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M3HG45; -.
DR STRING; 1895841.BGO55_14460; -.
DR Proteomes; UP000184242; 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; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR002241; Glyco_hydro_27.
DR InterPro; IPR013780; Glyco_hydro_b.
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; SSF49785; Galactose-binding domain-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|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361168};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361168};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..776
FT /note="Alpha-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012928433"
FT DOMAIN 672..772
FT /note="Alpha galactosidase C-terminal beta sandwich"
FT /evidence="ECO:0000259|Pfam:PF17801"
FT REGION 702..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..734
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 776 AA; 85439 MW; D8B30E7A7FC6C5F5 CRC64;
MLKIVPFFPS LLLSLSIFSL SLSAQDISIR DGWKFKTGDQ PTYASSTLRD SDWAPIHIGA
PWETQGYKGY DGFAWYRLHI VIPSSIKDKA FLKEKLRFDL GKIDDGDEFY LNGFLIGRNA
GVPGPIQNGN WEQQRTYTLP LTDGRIHWDN DNVIAIRVYD RDGDGGMYDG EYGISIMDVT
DYITLNTTAD EFHFSGTTGR GCSKKIVLQS SSEKYDFTGK LNIRVIDPFT GTAVYKQTIG
ADFAHNRPFE FTFKTTLPES GPYRVDYNFE EGRSKKTVTA SEEVPYILTP AAPATPHINS
PEVYGVRPGA AFLYKIPATG EKPMTYAVTG LPAGLTLDKQ TGIITGTLSK KGNYPVQFTV
KNKLGSATRR LTIVCGDKMA LTPALGWNSW NCWALSVSDE KIKASAAAMV SLLADYGWSY
INIDDGWEAE KRDDKGEIVP NNKFPDMKAL CDHVHGLGLK IGIYSSPGPR TCGGYLGSYQ
HEEQDAATYA RWGIDYLKYD WCSYGQIALK PTLDDMKKPY ILMRQALDKT GRDILYSLCQ
YGMGDVWKWG GEIGANSWRT TGDITDTWGS MAGIGFHQDK AAPYTAPGNF NDPDMLVVGK
VGWGPSLHNS RLTPDEQYTH ISLWCLLSAP LLIGCDMSHM DKFTLGLLTN SEVLAVDQDA
LTRPAGKVWE KDGIEVWVKE LKDGSKAVGV FNRTEQATTP TIPFSSIGLS GPGQTGFTRQ
SAGGSNQGRA GARSPVSGQL SVRDLWRQQD LAASGSALTP RLPAHGCVLL RVRKKA
//
