ID A0A0N0TTH9_9PSEU Unreviewed; 526 AA.
AC A0A0N0TTH9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=ADK67_11970 {ECO:0000313|EMBL:KOX28253.1};
OS Saccharothrix sp. NRRL B-16348.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1415542 {ECO:0000313|EMBL:KOX28253.1};
RN [1] {ECO:0000313|EMBL:KOX28253.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-16348 {ECO:0000313|EMBL:KOX28253.1};
RA Noorani M.;
RL Submitted (JUL-2015) 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:KOX28253.1}.
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DR EMBL; LGED01000113; KOX28253.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0TTH9; -.
DR STRING; 1415542.ADK67_11970; -.
DR PATRIC; fig|1415542.3.peg.2600; -.
DR Proteomes; UP000037722; Unassembled WGS sequence.
DR GO; GO:0004557; F:alpha-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd14792; GH27; 1.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR002241; Glyco_hydro_27.
DR InterPro; IPR000111; Glyco_hydro_27/36_CS.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR041233; Melibiase_C.
DR PANTHER; PTHR11452:SF75; ALPHA-GALACTOSIDASE; 1.
DR PANTHER; PTHR11452; ALPHA-GALACTOSIDASE/ALPHA-N-ACETYLGALACTOSAMINIDASE; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF16499; Melibiase_2; 1.
DR Pfam; PF17801; Melibiase_C; 1.
DR PRINTS; PR00740; GLHYDRLASE27.
DR SMART; SM00637; CBD_II; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR PROSITE; PS00512; ALPHA_GALACTOSIDASE; 1.
DR PROSITE; PS51173; CBM2; 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}.
FT DOMAIN 417..526
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
SQ SEQUENCE 526 AA; 55653 MW; A5492E9F4153E4A9 CRC64;
MLVAAGMVTV LNADPDPARA LDNGVARTPP MGWNSWNTFG CNINETLIRQ MTDAMVNSGM
RDAGYEYVVV DDCWMNPNRD SAGNLQGDPG RFPSGMKALG DYIHGKGLKF GIYQAPLTET
CAQYFNSYPG STGALGHEEQ DARQFAAWGV DFLKYDWCSP SGTMDDQVRA FAKMRDALRA
TGRPIVYSIN SNSIHDKTGP RRNWGDVANM WRTTEDITNK WDTGQTNGYP MGVQNIVNVT
VPLASYAKPG AFNDPDMMEV GRGGMNDTEM RSHFALWAIM ASPLIAGNDL RNMDAATQTI
LKNANLIGIN QDPLGLQAVQ ISNDGTRRVL AKRLSTGEVA VALFNQGSTP TTVSTAGYMI
GLEGVSITLR DAWTNAISSG SDGISATVPA HGTVVYLAKG SGMPTTTTTT TTTTTTTSAP
GGSCRVTNTV NAWGNGLTSD ITITNTGSTP VSGWSLAFTL PGGQTITSGW NASYSPSSGQ
VAARNVSYNA DIAPGGSVSI GFQATHTGNT AKPTAYTLNS STCTAA
//
