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Database: UniProt
Entry: A0A1G9WCV1_9ACTN
LinkDB: A0A1G9WCV1_9ACTN
Original site: A0A1G9WCV1_9ACTN 
ID   A0A1G9WCV1_9ACTN        Unreviewed;       547 AA.
AC   A0A1G9WCV1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-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=SAMN05216259_101595 {ECO:0000313|EMBL:SDM82093.1};
OS   Actinacidiphila guanduensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Actinacidiphila.
OX   NCBI_TaxID=310781 {ECO:0000313|EMBL:SDM82093.1, ECO:0000313|Proteomes:UP000199341};
RN   [1] {ECO:0000313|EMBL:SDM82093.1, ECO:0000313|Proteomes:UP000199341}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.2022 {ECO:0000313|EMBL:SDM82093.1,
RC   ECO:0000313|Proteomes:UP000199341};
RA   de Groot N.N.;
RL   Submitted (OCT-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}.
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DR   EMBL; FNIE01000001; SDM82093.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9WCV1; -.
DR   STRING; 310781.SAMN05216259_101595; -.
DR   Proteomes; UP000199341; Unassembled WGS sequence.
DR   GO; GO:0004557; F:alpha-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd14792; GH27; 1.
DR   CDD; cd00161; RICIN; 1.
DR   Gene3D; 2.80.10.50; -; 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; 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   InterPro; IPR035992; Ricin_B-like_lectins.
DR   InterPro; IPR000772; Ricin_B_lectin.
DR   PANTHER; PTHR11452:SF75; ALPHA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR11452; ALPHA-GALACTOSIDASE/ALPHA-N-ACETYLGALACTOSAMINIDASE; 1.
DR   Pfam; PF16499; Melibiase_2; 1.
DR   Pfam; PF17801; Melibiase_C; 1.
DR   Pfam; PF00652; Ricin_B_lectin; 1.
DR   PRINTS; PR00740; GLHYDRLASE27.
DR   SMART; SM00458; RICIN; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR   SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR   PROSITE; PS00512; ALPHA_GALACTOSIDASE; 1.
DR   PROSITE; PS50231; RICIN_B_LECTIN; 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   Reference proteome {ECO:0000313|Proteomes:UP000199341};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           34..547
FT                   /note="Alpha-galactosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038966115"
FT   DOMAIN          418..547
FT                   /note="Ricin B lectin"
FT                   /evidence="ECO:0000259|SMART:SM00458"
SQ   SEQUENCE   547 AA;  56404 MW;  0E4C197CA90627FB CRC64;
     MLDRIREAVH LHRRRAAAVS TALALCASGV LVAAASSATV LVAAPPAAAL DNGLARTPQM
     GFNDWNAYGC NVSESLIEST AQAMHTDGMQ AAGYTYVNID DCWMTHSRDS AGRLVPDPAK
     FPDGIAGTAA YVHSLGLKLG IYEDAGTATC AGYPGSLGHE TTDAQTFASW GVDYLKYDNC
     NNNGVPAQSR YTAMRDALAA TGRPILFSLC NWGQENVWTW GAGVGNSWRT TGDINASFSS
     MLSIFHSNAG LAAYAGPGHW NDPDMLEVGN GSLTQTEARS EFSLWSEMAA PLIAGTNIAS
     ASSATLSTLT NTRVIAVDQD PLGKQGVLVS SAGGLDVLAK PLSNGDVAVA LFNETGSTAT
     ISTTAGAVGK TGASSYTLTD LWSGAVSSTS GTISASVPSH GTVMYRLSGG SSTGSDPSGP
     IRAVGAGRCL DVPGSTSTAG TQVDIWDCNG GANQLWTRTA SGQLTVTSGG ARMCLDAYDN
     RTAPGTKVEI WSCNGQANQQ WQVNADGTIV GTQSGLCLDV TQAATANGTP VELWTCNGAS
     NQHWTLS
//
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