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Database: UniProt
Entry: A0A3E0GWR2_9PSEU
LinkDB: A0A3E0GWR2_9PSEU
Original site: A0A3E0GWR2_9PSEU 
ID   A0A3E0GWR2_9PSEU        Unreviewed;       679 AA.
AC   A0A3E0GWR2;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   24-JAN-2024, entry version 20.
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=BCF44_121124 {ECO:0000313|EMBL:REH32575.1};
OS   Kutzneria buriramensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Kutzneria.
OX   NCBI_TaxID=1045776 {ECO:0000313|EMBL:REH32575.1, ECO:0000313|Proteomes:UP000256269};
RN   [1] {ECO:0000313|EMBL:REH32575.1, ECO:0000313|Proteomes:UP000256269}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45791 {ECO:0000313|EMBL:REH32575.1,
RC   ECO:0000313|Proteomes:UP000256269};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (AUG-2018) 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   -!- 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:REH32575.1}.
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DR   EMBL; QUNO01000021; REH32575.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3E0GWR2; -.
DR   OrthoDB; 9758822at2; -.
DR   Proteomes; UP000256269; Unassembled WGS sequence.
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-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}.
FT   DOMAIN          96..248
FT                   /note="Glycosyl hydrolase family 36 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16875"
FT   DOMAIN          606..676
FT                   /note="Glycosyl hydrolase family 36 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16874"
FT   ACT_SITE        435
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT   ACT_SITE        505
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT   BINDING         165
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT   BINDING         323..324
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT   BINDING         400
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT   BINDING         433..437
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT   BINDING         483
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT   BINDING         505
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
SQ   SEQUENCE   679 AA;  74246 MW;  C15B0972DA4ABF6E CRC64;
     MTQQWTLRLA TTTYTVGLPE HRRWAELRSW GPLGVEDGPS PLANVGRTPY LTEADGAPVE
     YAPFGLRPFA GADLVAGPVG AARELWWQFD SASATDTSLR LTFGDALTGL RTDLYYKVVD
     GTDVLLRWTE LTNTGSAPIR LERFDSAGFC VPVDTARMSF LIGRWAQEFQ LRQVVLPAGR
     FSIGSQQGVA GHGYSPYLAV QDASDDGPTW GFQLAWPGSW HIDADIELSG SCRVRIGRQP
     HESAVLLEPG ASLETPQVAA AHSAEGLGGL ARVWHSYERQ LSPGGRRVLY NSWEATEFAV
     EADGQLELAK IAAEVGAELF VVDDGWFVGR NDDTGGLGDW TPDPAKFPHG FGAFVEEVRS
     LGLEFGLWVE PEAISPKSRL YAEHPDWVYH LDGRPPTLIR NQLLLDLGRE DVFEFVRATL
     DDLLTDYPIR YLKWDMNRPP TERGRPGAGA PESLDLDGAH ARNYLRILDF LRAAHPNVAI
     EGCAGGGARV ELATIARTDV VWPSDNTGPL DRLSIQYGFL HAHAPHVMSS WVTDAPGLFD
     PRPRSLRFRF VLAMAGALGI GADIRSWTVS QRSEAALLVA QYKELREFLH SATVTMIGTP
     SDPTFAIQYT SPDKVVVLAW NTGALDGSPA LSARQPRVRL SGLEPSARYG TYSGAYLMSA
     GLPVSWADVD ADVIVLERS
//
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