ID A0A1M5UVQ0_9ACTN Unreviewed; 691 AA.
AC A0A1M5UVQ0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-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=SAMN05444521_1355 {ECO:0000313|EMBL:SHH67055.1};
OS Streptomyces sp. 3214.6.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1882757 {ECO:0000313|EMBL:SHH67055.1, ECO:0000313|Proteomes:UP000190947};
RN [1] {ECO:0000313|Proteomes:UP000190947}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3124.6 {ECO:0000313|Proteomes:UP000190947};
RA Varghese N., Submissions S.;
RL Submitted (NOV-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|ARBA:ARBA00001255,
CC ECO:0000256|PIRNR:PIRNR005536};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase.
CC {ECO:0000256|PIRNR:PIRNR005536}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LT670819; SHH67055.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M5UVQ0; -.
DR STRING; 1882757.SAMN05444521_1355; -.
DR OrthoDB; 9758822at2; -.
DR Proteomes; UP000190947; Chromosome i.
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; 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.
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:UP000190947}.
FT DOMAIN 29..254
FT /note="Glycosyl hydrolase family 36 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16875"
FT DOMAIN 616..688
FT /note="Glycosyl hydrolase family 36 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16874"
FT ACT_SITE 446
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT ACT_SITE 514
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 334..335
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 411
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 444..448
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 492
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 514
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
SQ SEQUENCE 691 AA; 77243 MW; 55D0C0D1F5C3E078 CRC64;
MPEIADNGRT WLLSGPTSSY ALHLTEADEL IHLHWGPGIA LADAEALAAL PPSERGASFE
GPLDGREEYP VEGGPRFVRP ALSVRTEERR GTEWTFEAYE VDGDGLRLRF RDGGLAVTLH
YRMRGDVVER WTTLRNEDER PLELLRADSA VWTLPEREGW RLSQLHGRWA AESRLTVSPL
TYGEKVIGSR RGHTGHQHLP WVALDTDATE ERGEVYGCAL GWSGSWRIAV AQLPDARVQI
TGGAGYDDSG LLRLATGESF ITPVFAGLWS DAGFGGASRT WHAYQRAHVI PDAEGDRPVL
FNSWEATYFD ISEEQQATLA RRAAAIGVEL FVVDDGWFGA RTGDHAGLGD WRPNPDRFPK
GLKPLADYVH ALGMQFGIWV EPEMVNPDSD LYRAHPDWVQ FQTGRKRTEF RNQLVLNLAR
EDVQEYLWEQ LDALLSSAPV DYVKWDFNRC FTDAGWPDDP YPQRLWVDHV RALYALLDRL
RAAHPGVAFE SCSGGGGRID LGIMSRTDQV WTSDNTDPLD RLDIQHGFSQ IHPARVMAAW
VTDSPNAQLN GRVSSLRFRF VSAMAGVLGV GGDLSEWSEE ELAEAREWVG LYKEIRPLVQ
HGDLYRLRPP AGGLSAVQYV RGDEAVVLAW LQAQRFGEPV PALRLRGLDP TASYECRETG
EVHRGAVLLH RGLRTGLRGD LDATVIRLRR I
//