ID A0A261F721_9BIFI Unreviewed; 759 AA.
AC A0A261F721;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=ALMA_0203 {ECO:0000313|EMBL:OZG54878.1};
OS Alloscardovia macacae.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Alloscardovia.
OX NCBI_TaxID=1160091 {ECO:0000313|EMBL:OZG54878.1, ECO:0000313|Proteomes:UP000243657};
RN [1] {ECO:0000313|EMBL:OZG54878.1, ECO:0000313|Proteomes:UP000243657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24762 {ECO:0000313|EMBL:OZG54878.1,
RC ECO:0000313|Proteomes:UP000243657};
RX PubMed=28764658; DOI=10.1186/s12864-017-3955-4;
RA Lugli G.A., Milani C., Turroni F., Duranti S., Mancabelli L.,
RA Mangifesta M., Ferrario C., Modesto M., Mattarelli P., Jiri K.,
RA van Sinderen D., Ventura M.;
RT "Comparative genomic and phylogenomic analyses of the Bifidobacteriaceae
RT family.";
RL BMC Genomics 18:568-568(2017).
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:OZG54878.1}.
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; MWWT01000001; OZG54878.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261F721; -.
DR Proteomes; UP000243657; 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:UP000243657}.
FT DOMAIN 29..287
FT /note="Glycosyl hydrolase family 36 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16875"
FT DOMAIN 661..754
FT /note="Glycosyl hydrolase family 36 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16874"
FT ACT_SITE 490
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT ACT_SITE 557
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
SQ SEQUENCE 759 AA; 83334 MW; EEF2BCFA401DA557 CRC64;
MTVYTSDSGI VTLENGGVAV TLSLKNNELP RIVYWGRALG DDQGTAQLYE ALRPQRVSGG
LDDTNFPTVL PTQAEGWTGA PRFVVTRDGH EIFCAFTVTS VETSEAAPVA AGTSALAEEL
AGVKGENRAD APRAASLTVT AEDAAQGVQL TWQMQVLEGG LVRQQARVQN TAEWDAAHEG
SVLSVQTLEL SYPVPATARE VLTTAGHHLR ERHPQRQELT MGRFERVVEI GRPDFDATLL
LNVGPRGFDF EHGEVYSTHV GWSGNSITSV EQTVYTLPLI GGGEHLYAGE AELIAGEGAS
YTSPWVYGSY GEGLNEVSQR FHSFVRSLHP NLATKPRPVI LNTWEAVYFE HDFDTLKQLA
DKAAAAGVER FVVDDGWFGS RRDDTSGLGD WTVSQEVWPD GPKSLKALAD YVHGLGMEFG
LWFEPEMANI VSELNEQHPD WLLAPHAGRL PLQGRFQQVV DLSNPEACRY VFDAMDALVG
ELGIDYIKWD HNKLVTEPGS ACHGYAATQH AQVEAVYAIF EGLKLKHEGL EIESCSSGGG
RVDLGILERA DRVWTSDCVD PVERAEIQRY TSLLVPEVMM GEHVGASPAH STQRATSLTM
RTAMALFGHF GIEWDLNHQP QEDLDELAQW VALYKQVRPW ASQGVSVHGD IADDSVRLDG
VVAADGSKAL YRFAQVRTSV HYPALPVRLP GLDKDALYRV RPVDIQRELD VHHMNGQSDL
LWWTEEGIEI SGAALQNFGI RPPQLHPAQA VVFVVERIA
//
