ID Q934H7_GEOSE Unreviewed; 729 AA. AC Q934H7; DT 01-DEC-2001, integrated into UniProtKB/TrEMBL. DT 01-DEC-2001, sequence version 1. DT 27-MAR-2024, entry version 71. 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 Name=agaB {ECO:0000313|EMBL:AAG49421.1}; OS Geobacillus stearothermophilus (Bacillus stearothermophilus). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus. OX NCBI_TaxID=1422 {ECO:0000313|EMBL:AAG49421.1}; RN [1] {ECO:0000313|EMBL:AAG49421.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=KVE39 {ECO:0000313|EMBL:AAG49421.1}; RA Janz L., Ganter C., Stezowski J., Mattes R.; RT "Elucidation of functional domains in thermostable isoenzymes of alpha- RT galactosidase in Bacillus stearothermophilus. Enzymatic properties are RT encoded in a genetically exchangeable domain."; RL (In) Reuss M., Chmiel H., Gilles E-.D., Knackmuss H-.J. (eds.); RL BIOCHEMICAL ENGINEERING, STUTTGART, pp.170-173, Unknown Publisher (1991). RN [2] {ECO:0000313|EMBL:AAG49421.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=KVE39 {ECO:0000313|EMBL:AAG49421.1}; RA Watzlawick H., Ganter C., Mattes R.; RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0007829|PDB:4FNQ} RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS). RX PubMed=23012371; DOI=10.1074/jbc.M112.394114; RA Merceron R., Foucault M., Haser R., Mattes R., Watzlawick H., Gouet P.; RT "The molecular mechanism of thermostable alpha-galactosidases AgaA and AgaB RT explained by x-ray crystallography and mutational studies."; RL J. Biol. Chem. 287:39642-39652(2012). 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 36 family. CC {ECO:0000256|ARBA:ARBA00006202}. 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; AY013287; AAG49421.1; -; Genomic_DNA. DR PDB; 4FNQ; X-ray; 1.80 A; A=1-729. DR PDBsum; 4FNQ; -. DR AlphaFoldDB; Q934H7; -. DR SMR; Q934H7; -. DR CAZy; GH36; Glycoside Hydrolase Family 36. 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 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:4FNQ}; KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PIRNR:PIRNR005536}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR005536}. FT DOMAIN 29..285 FT /note="Glycosyl hydrolase family 36 N-terminal" FT /evidence="ECO:0000259|Pfam:PF16875" FT DOMAIN 648..724 FT /note="Glycosyl hydrolase family 36 C-terminal" FT /evidence="ECO:0000259|Pfam:PF16874" FT ACT_SITE 478 FT /note="Nucleophile" FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1" FT ACT_SITE 548 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1" FT BINDING 199 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2" FT BINDING 366..367 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2" FT BINDING 443 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2" FT BINDING 476..480 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2" FT BINDING 526 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2" FT BINDING 548 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2" SQ SEQUENCE 729 AA; 83467 MW; DF7FF8E5D3A016C1 CRC64; MAVTYNPQTK QFHLRAGKAS YVMQLFRSGY LAHIYWGKAV RDVRGERRFS RLDRAFSPNP DPSDRTFSLD TLPQEYPAYG NTDFRSPAYQ VQLENGSTVT DLRYKTHRIY KGKPRLNGLP ATYVEHEQEA ETLEIVLGDA LIGLEVTLQY TAYEKWNVIT RAARFENKGG ERLKLLRALS MSVDFPTADY DWIHLPGAWG RERWIERRPL VTGVQAAESR RGASSHQQNP FIALVAKNAD EHQGEVYGFS FVYSGNFLAQ VEVDQFHTAR VSMGINPFDF TWLLQPGESF QTPEVVMVYS DQGLNGMSQT YHELYRTRLA RGAFRDRERP ILINNWEATY FDFNEEKLVN IAKTEAELGI ELFVLDDGWF GKRDDDRRSL GDWIVNRRKL PNGLDGLAKQ VNELGMQFGL WVEPEMVSPN SELYRKHPDW CLHVPNRPRS EGRNQLVLDY SREDVCDYII ETISNVLASA PITYVKWDMN RHMTEIGSSA LPPERQRETA HRYMLGLYRV MDEMTSRFPH ILFESCSGGG GRFDPGMLYY MPQTWTSDNT DAVSRLKIQY GTSLVYPISA MGAHVSAVPN HQVGRVASLK ARGHVAMSGN FGYELDITKL TETEKQMIKQ QVAFYKDVRR LVQFGTFYRL LSPFEGNEAA WMFVSADRSE ALVAYFRVLA EANAPLSYLR LKGLDPNQDY EIEGLGVYGG DELMYAGVAL PYRSGDFISM MWRLKAVQQ //