ID A0A1V0ADU9_9ACTN Unreviewed; 707 AA.
AC A0A1V0ADU9;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Alpha-galactosidase {ECO:0000256|ARBA:ARBA00012755, ECO:0000256|PIRNR:PIRNR005536};
DE EC=3.2.1.22 {ECO:0000256|ARBA:ARBA00012755, ECO:0000256|PIRNR:PIRNR005536};
GN ORFNames=BKM31_49250 {ECO:0000313|EMBL:AQZ68400.1};
OS Nonomuraea sp. ATCC 55076.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Nonomuraea.
OX NCBI_TaxID=1909395 {ECO:0000313|EMBL:AQZ68400.1, ECO:0000313|Proteomes:UP000190797};
RN [1] {ECO:0000313|Proteomes:UP000190797}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55076 {ECO:0000313|Proteomes:UP000190797};
RX PubMed=28626548; DOI=10.1039/c6md00637j;
RA Nazari B., Forneris C.C., Gibson M.I., Moon K., Schramma K.R.,
RA Seyedsayamdost M.R.;
RT "Nonomuraea sp. ATCC 55076 harbours the largest actinomycete chromosome to
RT date and the kistamicin biosynthetic gene cluster.";
RL Med. Chem. Commun. 8:780-788(2017).
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|ARBA:ARBA00001255,
CC ECO:0000256|PIRNR:PIRNR005536};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase.
CC {ECO:0000256|PIRNR:PIRNR005536}.
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DR EMBL; CP017717; AQZ68400.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V0ADU9; -.
DR STRING; 1909395.BKM31_49250; -.
DR KEGG; noa:BKM31_49250; -.
DR OrthoDB; 9758822at2; -.
DR Proteomes; UP000190797; Chromosome.
DR GO; GO:0004557; F:alpha-galactosidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016052; P:carbohydrate catabolic process; IEA:InterPro.
DR CDD; cd14791; GH36; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 2.70.98.60; alpha-galactosidase from lactobacil brevis; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR038417; Alpga-gal_N_sf.
DR InterPro; IPR000111; Glyco_hydro_27/36_CS.
DR InterPro; IPR002252; Glyco_hydro_36.
DR InterPro; IPR031705; Glyco_hydro_36_C.
DR InterPro; IPR031704; Glyco_hydro_36_N.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR43053:SF3; ALPHA-GALACTOSIDASE C-RELATED; 1.
DR PANTHER; PTHR43053; GLYCOSIDASE FAMILY 31; 1.
DR Pfam; PF16874; Glyco_hydro_36C; 1.
DR Pfam; PF16875; Glyco_hydro_36N; 1.
DR Pfam; PF02065; Melibiase; 1.
DR PIRSF; PIRSF005536; Agal; 1.
DR PRINTS; PR00743; GLHYDRLASE36.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS00512; ALPHA_GALACTOSIDASE; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PIRNR:PIRNR005536};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR005536};
KW Reference proteome {ECO:0000313|Proteomes:UP000190797}.
FT DOMAIN 35..266
FT /note="Glycosyl hydrolase family 36 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16875"
FT DOMAIN 628..704
FT /note="Glycosyl hydrolase family 36 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16874"
FT ACT_SITE 457
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT ACT_SITE 526
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT BINDING 180
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 345..346
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 422
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 455..459
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 504
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 526
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
SQ SEQUENCE 707 AA; 78204 MW; D9C3F8B951C61F52 CRC64;
MPVIPLDDHH WALTTPASTY VIGVEIDPDT GEAAPRQTYW GPRLPDEAAR QVTGLPRRHV
SSFSTPGEVE ELLPVDGGKR WGVPSLQVAF GDTRSLELRF AGARRHDEGG GAERLDVLLA
DAHFPFEVVL SLRVRDDTDV IERWTTVRAG TQAVVTRLDS GNWFVPDAPG YRYSGVFGAW
AEESQLQRGP LPVGELVFTS RQGITSHVAN PWVMIDDGAA TEEHGEVWGV ALAWSGSWRL
TTTHRPEGGV CVSGGFGHDG LRWTLAPGEE LVTPSVLGLY SPGGFGGASR AWHAYARGHV
LPTPAEERPV LYNSWEATTF AVTEAHQLEL AKTAASIGVE LFVIDDGWFG RRDDDTTSLG
DWFPHRERFP DGLRGMLDGI RDLGLRVGLW VEPEGLSKES ELYRAHPDWA LHLEHRRRDE
KRGQLVLNFA RDDVRAWALG WLDTLVTELG LDYLKWDMNR PFTQAGWPER GAGQDHVWIE
HTRGVYQVMR ELRGRHPGLR IESCAGGGGR VDLGIMRYTD EVWPSDNTDA RDRQTVQHGF
SQLYPASAMS AWVTDSPNPT TRRAMPLRYR FHVAMAGVLG VGGNLSEWTA GELETAAELI
AQYKRVRRTI QQGAQYRLAG TPGQERSAVQ YVLGDQVAVL VYNPLGNAKR GPRTLRLAGL
DPDAVYELES DGSRWYGATL MGAGIRPAAW APIGADHRSE LVVLKKV
//