ID A0A0R1UUE4_9LACO Unreviewed; 739 AA.
AC A0A0R1UUE4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=FC21_GL001139 {ECO:0000313|EMBL:KRL95091.1};
OS Limosilactobacillus equigenerosi DSM 18793 = JCM 14505.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=1423742 {ECO:0000313|EMBL:KRL95091.1, ECO:0000313|Proteomes:UP000051084};
RN [1] {ECO:0000313|EMBL:KRL95091.1, ECO:0000313|Proteomes:UP000051084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18793 {ECO:0000313|EMBL:KRL95091.1,
RC ECO:0000313|Proteomes:UP000051084};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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 -!- 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:KRL95091.1}.
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DR EMBL; AZGC01000026; KRL95091.1; -; Genomic_DNA.
DR RefSeq; WP_054652273.1; NZ_BBAS01000001.1.
DR AlphaFoldDB; A0A0R1UUE4; -.
DR STRING; 417373.GCA_001570685_00108; -.
DR PATRIC; fig|1423742.4.peg.1182; -.
DR OrthoDB; 9758822at2; -.
DR Proteomes; UP000051084; 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-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:UP000051084}.
FT DOMAIN 32..284
FT /note="Glycosyl hydrolase family 36 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16875"
FT DOMAIN 651..734
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 739 AA; 84618 MW; 65944B2CB77B5DA6 CRC64;
MSIHYNEQTK VFHLQTDHTS YIFQILPTGV AGQVYYGPQI PVKAEYQNLM TREEHDCTNT
YTDEQTDLQY ELLKQEYASY GSGDYRYPAV SVTNPTGDRI SEFKFTNAEI VDGKDRLAEL
PSTFDDDHHD AQTLHVHFVD AVNQLEMVLN YTVFATEDVI ARSTTFINHG EPLKLNRALS
LQLDLPDFNY DLIQFDGSWA RERHLHRTPL RYGMQSNSSL RFTSGHHSNP FFMLARPETN
ELTGSAYGFN LIYSGNFIDS VEVDQFDVAR VLTGINPAEF SWELTSDATF QTPEAIMTYT
DAGLNTLSQN LADFYNHHLL PSRFVKQERP TLVNNWEATF MDFTEDKLMP IVNKAHDLGI
EMFVLDDGWF GHRDNDQSSL GDWFVDHKKF VNGVGGFAHR VHQLGMKFGL WFEPEMVSED
SELFKAHPEW RIGAPHRHHT PARHQFVLDY SNPAVVDFIY DEMAKVITDT KLDYVKWDMN
RSITEAFSTN LPADRQTEFG HRYILGVYRL YDRLTTAFPN VLFESCASGG GRFDLGMMYY
APQAWASDNT DAVERLSVQT GSSYGYSQNM WGAHVSAVPN DQNGRLTSLD FRAKVAYFGA
FGYELDLNEL SNAEQAQVKD QVAFYKQYRS LFQFGKFYRL PQRLQNPANV TAWAVVNDDQ
TQAIATYFQV LNPANPAYVR FYLAGLDPQK HYRVNDGDEI FSGQELMTAG YFLPRIMPRV
AHKDPADFKA TMLIIKAVD
//