ID A0A1M3G602_9SPHI Unreviewed; 659 AA.
AC A0A1M3G602;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Alpha-galactosidase {ECO:0000256|RuleBase:RU361168};
DE EC=3.2.1.22 {ECO:0000256|RuleBase:RU361168};
DE AltName: Full=Melibiase {ECO:0000256|RuleBase:RU361168};
GN ORFNames=BGO54_02710 {ECO:0000313|EMBL:OJW35080.1};
OS Sphingobacteriales bacterium 46-32.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX NCBI_TaxID=1895839 {ECO:0000313|EMBL:OJW35080.1, ECO:0000313|Proteomes:UP000184358};
RN [1] {ECO:0000313|EMBL:OJW35080.1, ECO:0000313|Proteomes:UP000184358}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=46-32 {ECO:0000313|EMBL:OJW35080.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-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|RuleBase:RU361168};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 27 family.
CC {ECO:0000256|ARBA:ARBA00009743, ECO:0000256|RuleBase:RU361168}.
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:OJW35080.1}.
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DR EMBL; MKTY01000014; OJW35080.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M3G602; -.
DR STRING; 1895839.BGO54_02710; -.
DR Proteomes; UP000184358; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProt.
DR GO; GO:0004557; F:alpha-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd14792; GH27; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.60.120.1060; NPCBM/NEW2 domain; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR013222; Glyco_hyd_98_carb-bd.
DR InterPro; IPR002241; Glyco_hydro_27.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR041233; Melibiase_C.
DR InterPro; IPR038637; NPCBM_sf.
DR PANTHER; PTHR11452:SF75; ALPHA-GALACTOSIDASE; 1.
DR PANTHER; PTHR11452; ALPHA-GALACTOSIDASE/ALPHA-N-ACETYLGALACTOSAMINIDASE; 1.
DR Pfam; PF05345; He_PIG; 1.
DR Pfam; PF16499; Melibiase_2; 1.
DR Pfam; PF17801; Melibiase_C; 1.
DR Pfam; PF08305; NPCBM; 1.
DR PRINTS; PR00740; GLHYDRLASE27.
DR SMART; SM00776; NPCBM; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49313; Cadherin-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|RuleBase:RU361168};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361168};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361168};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 22..161
FT /note="Glycosyl hydrolase family 98 putative carbohydrate-
FT binding module"
FT /evidence="ECO:0000259|SMART:SM00776"
SQ SEQUENCE 659 AA; 73842 MW; 9274DDD729AA2345 CRC64;
MVRRFSYLFS LITALGIAVS GFSKEVYLDK LDVSYMLQDW GGPVVNKSVL GTPFAVAGVK
YSRGIGTHSV SRYMLKLDGK ATSISGYVGA DDRNDYAGSM EFKILADGKV IWTSNIMRKG
MPALRFNVDL TGKQQIVLMV TEGGDGIMYD HADWLEVKIE TSGEVIPQTA YPESIAKDKY
ILTPKPRETP RINSPRVFGV RPGNPFLYQV AATGKRPMKF TAYQLPKGLS IDEKTGLITG
TVEKAGRYYI VVRADNELGG DFRRVTVEVG DKIALTPPMG WNSWNCWGLN VDEQKVKDAA
DFMSRELINH GWSYINIDDG WEAKERTKEG ELLGNAKFPD FKRLSDYIHS KGLKFGIYSS
PGPKTCGGYL GTYAHEAIDA RTWANWGVDY LKYDYCLYSE IAPVPTENLI KDPYILMGDE
LQKVNRDIVY CVGYGAPNVW YWGQEAKGHQ WRTTRDITDD WNVVVAIGAF QDVCAPVTKP
GQYNDPDMLV VGKLGGGWGA KMHDSKLTAD EQYSHMSLWS LLSSPLLIGC DMNAIDDFTL
NLLTNDEVIA VNQDPLVKPA KKIVTENGQI WYKELEDGSV AVGFFNIDPY YILWDKTKEK
AIQNQEYELS VDWAKLGLTG EYTVRDLWKQ QDIGRAKGKY SAKVPYHGVK LVKLTPVKK
//
