ID A0A1H0BZD2_9FIRM Unreviewed; 782 AA.
AC A0A1H0BZD2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, 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=SAMN05192585_12118 {ECO:0000313|EMBL:SDN50916.1};
OS Acetanaerobacterium elongatum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Acetanaerobacterium.
OX NCBI_TaxID=258515 {ECO:0000313|EMBL:SDN50916.1, ECO:0000313|Proteomes:UP000199182};
RN [1] {ECO:0000313|EMBL:SDN50916.1, ECO:0000313|Proteomes:UP000199182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.5012 {ECO:0000313|EMBL:SDN50916.1,
RC ECO:0000313|Proteomes:UP000199182};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FNID01000021; SDN50916.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0BZD2; -.
DR STRING; 258515.SAMN05192585_12118; -.
DR OrthoDB; 9758822at2; -.
DR Proteomes; UP000199182; 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:UP000199182}.
FT DOMAIN 26..284
FT /note="Glycosyl hydrolase family 36 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16875"
FT DOMAIN 650..778
FT /note="Glycosyl hydrolase family 36 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16874"
FT ACT_SITE 477
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT ACT_SITE 547
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT BINDING 198
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 365..366
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 442
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 475..479
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 525
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 547
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
SQ SEQUENCE 782 AA; 88435 MW; AAB9E1974425AB54 CRC64;
MDISMSTIIH LNTRHTSYIM SVLPTGHLQN LYYGRRIRPL KDAAVLTQPN AVPYGSMVAY
QKEYPTIGLD DQCLEYSALG KGDYREPAIE LTAANGCMVA DFKYVCHKTY KGRRGIPKLP
SALGTEQNCE TTEVILRDEA IGMDLTLFYC VYPEYDVITR FVCAKNNSGQ KITLRRLMSA
QLDLFDSNYS FVTFDGTWAS ERTMHSRRLC EGIFVNDSKL GVSSARHNPF VMLTADGCTE
ETGRCYGMNL VYSGNHSEIC EVTFNHKTRL LTGINPSSFA WLLAPGEEFY TPEAVFTYSE
EGLNGLSHNL HGFVNNHIVR GEWQNRERPI VINNWEATSF SFTQGKLLSI AKEAADMGIE
LFVLDDGWFG RRNDDTSSLG DWHVNEKKLP SGLKGLAEKM NALGLDFGLW VEPEMVNEDS
DLYRAHPDWA IKAPNRTPSE GRNQFILDLT RKEICDYLTE TLSKVFSSAN ITYIKWDMNR
NFSDIYSPTL PPERQGEFFH RYVLGLYGVL ETLTQRFPKI LFESCASGGN RFDLGMLCYM
PQTWASDNTD AQCRIAIQEG TSYGYPISTM GAHVSASPCF ATLRNTPIET RFNVAAFGCF
GYELDLSKLF EFDKKAIKEQ VAYYKAHRRV IQFGRFYRLR GGFNPDKRIW LCVSPDKREA
VAALFQETAA VGRGNELLRL TGLDDHLDYT VTGRRQYVNL KTLGDLVNNV LPVEIRGDGV
IHTVLSSHYM LAMCDEVFEA GGDLLNGYGI KLKHQFSGTG YNDNVKIFGD YSSRMYELKA
RE
//