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
//