ID A0A0R2AXD5_9LACO Unreviewed; 733 AA.
AC A0A0R2AXD5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=FC34_GL001312 {ECO:0000313|EMBL:KRM71655.1};
OS Lacticaseibacillus brantae DSM 23927.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lacticaseibacillus.
OX NCBI_TaxID=1423727 {ECO:0000313|EMBL:KRM71655.1, ECO:0000313|Proteomes:UP000051672};
RN [1] {ECO:0000313|EMBL:KRM71655.1, ECO:0000313|Proteomes:UP000051672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23927 {ECO:0000313|EMBL:KRM71655.1,
RC ECO:0000313|Proteomes:UP000051672};
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:KRM71655.1}.
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DR EMBL; AYZQ01000003; KRM71655.1; -; Genomic_DNA.
DR RefSeq; WP_057894606.1; NZ_AYZQ01000003.1.
DR AlphaFoldDB; A0A0R2AXD5; -.
DR STRING; 1423727.FC34_GL001312; -.
DR PATRIC; fig|1423727.3.peg.1332; -.
DR OrthoDB; 9758822at2; -.
DR Proteomes; UP000051672; 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:UP000051672}.
FT DOMAIN 30..283
FT /note="Glycosyl hydrolase family 36 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16875"
FT DOMAIN 650..727
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 733 AA; 82741 MW; 77C12519348C10AD CRC64;
MITFDKTKQQ FHLSNGLISY VMRIEALSIL GQVYFGKAIT DPQGLRRYPL IDRSFSPNFP
ETHSRDYSLD TQPLEYPSGL GDFREPAIDV VQANGAHYLD LRYVDYAILA GKPELVGLPA
TFSTDQHSAE TLRVHLRDAN FNVDVYLNYA IFAGLPVVAR SAEIVNNGDE PIHLDRAFSA
SLDFPLGDWE ALSLAGSWSN ERQIVRQPLT HGNYEVSTKR GTSSHQENPF LALLHPTTTE
DQGEVYGFSL VYSGNHRLQA EVDQYGCIRV QAGINDYRFD WELSPKAHFQ TPEVVMAYSD
HGLNAMSQAY HQLYIDNLMT SRFKREVRPI LVNNWEATFF DFTTESLKPI INQAAKLGIE
MFVLDDGWFG HRDNDKSSLG DWFEFKGKIA GGLGEFAQYV HQKGLKFGLW FEPEMVSADS
ELYRRHPDWA FAVPNTTPLL GRDQYVLDFS RSEVRDYIYQ EITGVLDSVD INYIKWDMNR
SLTDVFSLAL PKDRQGEVYH RYILGLYELL DRLTTRYPDI LFESCSGGGG RFDPGMLYYM
PQTWTSDNTD AVSRLNIQYG TSLVYPPVAM GNHVSAVPNS QTGRTTSLDT RAAVAMAGNF
GYELDLNALT TEAQAAVTKQ VAFYKQNREL LQFGTFYRLT SPFDAHSNGA SWGMVSKDQQ
DAIFFVYTLG AAPNPSLKVI KFAGLIPTQH YQVSGFKGAF TGSELMSVGF YLDVNAYRGD
YNSRIYRVTA VNE
//