ID A0A1S9M821_9MICC Unreviewed; 734 AA.
AC A0A1S9M821;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=BMF89_13540 {ECO:0000313|EMBL:OOP61262.1};
OS Arthrobacter sp. SRS-W-1-2016.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1930254 {ECO:0000313|EMBL:OOP61262.1, ECO:0000313|Proteomes:UP000190514};
RN [1] {ECO:0000313|EMBL:OOP61262.1, ECO:0000313|Proteomes:UP000190514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRS-W-1-2016 {ECO:0000313|EMBL:OOP61262.1,
RC ECO:0000313|Proteomes:UP000190514};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) 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:OOP61262.1}.
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DR EMBL; MTPV01000054; OOP61262.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S9M821; -.
DR OrthoDB; 9758822at2; -.
DR Proteomes; UP000190514; 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:UP000190514}.
FT DOMAIN 22..259
FT /note="Glycosyl hydrolase family 36 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16875"
FT DOMAIN 635..720
FT /note="Glycosyl hydrolase family 36 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16874"
FT ACT_SITE 468
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT ACT_SITE 532
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT BINDING 175
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 349..350
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 433
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 466..470
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 510
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 532
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
SQ SEQUENCE 734 AA; 80007 MW; 2F45793CBAD5D27D CRC64;
MDPLHLRSAG TSLVLSFDNG EAEVIHWGAD LGSTLPDLAI LGGPIPHSAI DVTVPAALLP
QASSAWQGRP GLRGQRIADG VPGLDFSLRF RVVDVQADSS SAVATAAAAS AVIVQQDPDA
GITVTSGLTL HPGGLLELRH TAVNDGTSPF QLDELATVLP VGPDAVELLD LTGRWCRERH
PQRRPVQQGT WVRTGRHGRT GHDSSLLFAA GTAGFGNRHG KVWATHLAWS GNHEQFADTV
ADGRTVIGGS ELLGPAEIVL QPGESYTTPA LFAAYSDRGL DGISEAFYGW FRSRPHHVLP
AASTGLPAGK PRPVVLNTWE AVYFDHRLDT LLELAESAAE LGVERFVLDD GWFRGRRDDH
AGLGDWYVDR TLWPDGLTPL IEAVNSHGME FGLWVEPEMI NLDSDVARSH PDWIVGPSAL
SHKDGGRLPL EWRHQHIIDL VNPAAWRYVF DRIDALLREN NIKYLKWDQN RDLSEHGHAG
RASVHGQTLA AYRLFDELRK AHPGVEIESC SSGGARVDLG ILERTDRIWG SDCNDALERQ
TIQRWTGVVV PPELVGGHIG PTTSHTTART HDLSFRAITA MFGHFGMEWD VRQVQRAERE
ELKRFIGLYK EHRGLIHSGR MVRADVPDDS LMVHGVVSDD GGSALFAVVS TRTSFAEQPG
RVAIPGLDPE RSYMVQAIFP APGDADYART FTQVQPPAWL PSGAEASGRF LAEVGLPMPV
LNPEHALLLR ITAV
//
