ID A0A3B0B9Z7_9MICO Unreviewed; 709 AA.
AC A0A3B0B9Z7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=D7252_04715 {ECO:0000313|EMBL:RKN69454.1};
OS Microbacterium sp. CGR2.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1805820 {ECO:0000313|EMBL:RKN69454.1, ECO:0000313|Proteomes:UP000278458};
RN [1] {ECO:0000313|EMBL:RKN69454.1, ECO:0000313|Proteomes:UP000278458}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGR2 {ECO:0000313|EMBL:RKN69454.1,
RC ECO:0000313|Proteomes:UP000278458};
RA Mandakovic D., Cintolesi A., Maldonado J., Cortes M.P., Mendoza S.,
RA Aite M., Gaete A., Saitua F., Cambiazo V., Agosin E., Siegel A., Maass A.,
RA Gonzalez M., Latorre M.;
RT "Comparative genome-scale metabolic modeling of two Microbacterium species
RT isolated from Atacama Desert.";
RL Submitted (SEP-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:RKN69454.1}.
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DR EMBL; RBHX01000001; RKN69454.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B0B9Z7; -.
DR OrthoDB; 9758822at2; -.
DR Proteomes; UP000278458; 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; 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:UP000278458}.
FT DOMAIN 12..254
FT /note="Glycosyl hydrolase family 36 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16875"
FT DOMAIN 614..694
FT /note="Glycosyl hydrolase family 36 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16874"
FT ACT_SITE 444
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT ACT_SITE 510
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 332..333
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 409
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 442..446
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 488
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 510
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
SQ SEQUENCE 709 AA; 77404 MW; BE2D77E1274321CA CRC64;
MSLLVHVGGD DLPAIVHWGA ALGPLTDAEA RTLASASIEP VVPNAIDVPI RLAVIPEGWR
GWTGKPGIEG HRAGSDWSPR FRPTQVSLDD APVAPGLVEV AAGVIIVEAV DPEAELALAL
HLELTESGVV RAKAVLRNTG AGDYDVAALN VAFPIPPVAR EILDFAGRWG KERVPQRSPL
VVGIHEREGR KGRTGADAAT VLSVGVPGFG FGAGEVWGVH VGFSGNHRSY AERLFSGVQV
VGGGELLLPG EVRLRTGEEY FSPWIYGVYG NGLDEQASRL HRMLRAREVH PRHPRPVTLN
VWEAVYFDHD RDRLFDLAER AAPLGIERFV LDDGWFRGRR DDSAGLGDWY VDEEVWPEGL
APLAEHVREL GMEFGLWFEP EMINPDSDLA REHPEWILAV AGRTPVLARN QLVLDLGRDE
AYEHVLERMT AVLEATAVSY IKWDHNRDLV DAGHGVHGVP GVHAQTLATY RLMAELKRRF
PSLEIESCSS GGARVDLGII EHTDRVWVSD CIDPLDRQQM NRWTMQLLPP EMLGSHVASG
VSHSTGRSHT LGFRAASAMY GHFGVEWDLA AATEDEVREL GAWIEAHKSY RELLHTGDMV
RVDTSDPTLN LYGAVASDRS AALFVLASVG RSEVAPLGRF TLRGLDPDRR YRVRPVTPGG
APRGLIAPPW FGDDDNGVEL SGRALMTAGL HTPAMYPESA ILLDVSATT
//
