ID A0A1F5BA58_9BACT Unreviewed; 516 AA.
AC A0A1F5BA58;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=A2V57_00650 {ECO:0000313|EMBL:OGD27492.1};
OS Candidatus Aminicenantes bacterium RBG_19FT_COMBO_65_30.
OC Bacteria; Candidatus Aminicenantes.
OX NCBI_TaxID=1797277 {ECO:0000313|EMBL:OGD27492.1, ECO:0000313|Proteomes:UP000177619};
RN [1] {ECO:0000313|EMBL:OGD27492.1, ECO:0000313|Proteomes:UP000177619}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGD27492.1}.
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; MEYF01000068; OGD27492.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5BA58; -.
DR STRING; 1797277.A2V57_00650; -.
DR Proteomes; UP000177619; 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 InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR015919; Cadherin-like_sf.
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 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 PRINTS; PR00740; GLHYDRLASE27.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49313; Cadherin-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, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..516
FT /note="Alpha-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009517701"
FT DOMAIN 438..510
FT /note="Alpha galactosidase C-terminal beta sandwich"
FT /evidence="ECO:0000259|Pfam:PF17801"
SQ SEQUENCE 516 AA; 56826 MW; FC678A38325D5FD1 CRC64;
MRRTPRPLVL ILAVSALAAA ALTPLTSAEE KVILTPKPGP EPRINGARVF GVRPRSPFLF
TIPATGERPM TFAVEGLPDG LTLDTATGQI TGALAARGEY AVTFKATNRS GTIERGFKIV
CGDTLALTPH MGWNSWYVWE NHVTDGIMRA AADAMVSSGM IDHGYQYVNI DDCWAVKPGS
NDPTLQGPER DARGMVNSNG RFPDMKALTD YIHAKGLKAG IYTSPGPLTC AGHVAAWQHE
EQDVARFVEW GYDFLKYDWC TYLGGGRDKT IDELQRPYRL ASAILAKQPR DIVLNLCQYG
MGKVWEWGAS VGGNSWRTAD DLGGRFEGIP AALFRDGFDV YSKNELHRHG GPGRWNDPDY
LLIGYLSDWQ GGTAATPLTP NEQYTHFSLW CLVSAPLIFS GDITRLDDFT LNILTNDEVI
DVDQDPLGKP GRRVAKSGDL EVWVKEMEDG SKAVGLFNRG EGLAEVTALW ADIGVQGRQK
VRDLWRQKDL GVYKDALKAF VARHGVVLVR MWPEGK
//
