ID A0A2T0UB77_9SPHI Unreviewed; 682 AA.
AC A0A2T0UB77;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
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=B0I27_101112 {ECO:0000313|EMBL:PRY55144.1};
OS Arcticibacter pallidicorallinus.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Arcticibacter.
OX NCBI_TaxID=1259464 {ECO:0000313|EMBL:PRY55144.1, ECO:0000313|Proteomes:UP000238034};
RN [1] {ECO:0000313|EMBL:PRY55144.1, ECO:0000313|Proteomes:UP000238034}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.9313 {ECO:0000313|EMBL:PRY55144.1,
RC ECO:0000313|Proteomes:UP000238034};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (MAR-2018) 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:PRY55144.1}.
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DR EMBL; PVTH01000001; PRY55144.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0UB77; -.
DR Proteomes; UP000238034; 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; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000238034};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..682
FT /note="Alpha-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015488206"
FT DOMAIN 31..171
FT /note="Glycosyl hydrolase family 98 putative carbohydrate-
FT binding module"
FT /evidence="ECO:0000259|SMART:SM00776"
SQ SEQUENCE 682 AA; 74414 MW; BDA7F494700B780D CRC64;
MQIQNKSLFG SVRLFILMAL IVMSGHSYAQ NTQTVWLDEL DLSAATQGYG VPKKNTTVDG
NKMTIAGKTF ERGFGTHAES SLIVVLKGDA TSFSAQVGVD DEMKDHEPAV EFVVKGDGQQ
LWSSGVMRLG DAARACSISV AGIQKIELVV TDGGNGNYYD HANWADAKFE TKGTQSIATF
NPIPSEPYIL TPPAPATPRI NGTGVFGVRP GSPFLFRIPA TGDRPMTFSA TGLPKGLQLD
AKTGVITGKL SKAGTFIVGL KARNAKGIGE KKLRIVCGDQ IALTPPMGWN SWNCFAGEVS
ADKIKRAAQA MVNSGLVNHG WTYINIDDFW QNNRASRDPA LQGKLRDENG YILPNARFGD
MKVLADDVHN LGLKIGIYSS PGPWTCGGCA GSYGFEKQDA ESYAKWGFDY LKYDWCSYGG
VIDGMPGNDP YKVGSLSYQG GDKLETAMKP FQVMGDLLRA QPRDIVYSLC QYGMSDVWKW
GNSVGGQTWR TTNDITDTWT SVKNIALAQD QSAAWSKPGS WNDPDMLVVG TVGWGDPHPS
KLKPDEQYLH FSLWSLFSAP LLIGCDMEKL DAFTLNLLTN DEVISINQDP LGKQATCVQT
IGDLRIYVKE LEDGSRAVGF CNFGLEKVNL SYKDFQQLGI TGKQKVRDLW RQKDVATLNT
DNDSLSVDVP VHGVMLYKLT SL
//
