ID A0A1I1CP91_9BACL Unreviewed; 816 AA.
AC A0A1I1CP91;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-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=SAMN05216312_12124 {ECO:0000313|EMBL:SFB62420.1};
OS Cohnella sp. OV330.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Cohnella.
OX NCBI_TaxID=1855288 {ECO:0000313|EMBL:SFB62420.1, ECO:0000313|Proteomes:UP000198686};
RN [1] {ECO:0000313|EMBL:SFB62420.1, ECO:0000313|Proteomes:UP000198686}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OV330 {ECO:0000313|EMBL:SFB62420.1,
RC ECO:0000313|Proteomes:UP000198686};
RA de Groot N.N.;
RL Submitted (OCT-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}.
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DR EMBL; FOKE01000021; SFB62420.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1CP91; -.
DR Proteomes; UP000198686; Unassembled WGS sequence.
DR GO; GO:0004557; F:alpha-galactosidase activity; IEA:UniProtKB-EC.
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; 2.60.120.260; Galactose-binding domain-like; 3.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR040794; CE2_N.
DR InterPro; IPR002241; Glyco_hydro_27.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR041233; Melibiase_C.
DR PANTHER; PTHR11452:SF75; ALPHA-GALACTOSIDASE; 1.
DR PANTHER; PTHR11452; ALPHA-GALACTOSIDASE/ALPHA-N-ACETYLGALACTOSAMINIDASE; 1.
DR Pfam; PF17996; CE2_N; 1.
DR Pfam; PF16499; Melibiase_2; 2.
DR Pfam; PF17801; Melibiase_C; 1.
DR PRINTS; PR00740; GLHYDRLASE27.
DR SUPFAM; SSF51445; (Trans)glycosidases; 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:UP000198686};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..816
FT /note="Alpha-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038704320"
FT DOMAIN 372..445
FT /note="Alpha galactosidase C-terminal beta sandwich"
FT /evidence="ECO:0000259|Pfam:PF17801"
FT DOMAIN 482..561
FT /note="Carbohydrate esterase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17996"
SQ SEQUENCE 816 AA; 89450 MW; 20D4C169FF58F03E CRC64;
MFKTFIKLRI LLLTVAILAT QAGIAMPQAQ VASAAINGLG QKPYMGWSSY SMQVYSGSNP
FITAAQIKAQ SDAMHATLQS HGYEYINIDA GWNGSMDGFG RPIPSTTLYP NGFQDVIDYV
HDNGQKIGIY LIPGLSKDAY NANLPIYGTT SCHMQDIAVQ PLTTADYWNI GYKIDFSNPC
AQSYVNSIAD LIASWGIDFV KFDSVTPGSG HNDTSIDARG DVKAWATALA PHGIWFELSW
ALDHNYVDYW KQYANGWRVD WDVEAYQPGV KLTEWNNIAR LFPDAETWWR DARPGGWNDF
DSLNVGNGAM DGLTQDERRT AMTLWSMSSA QLYTGNDLTN LDSFGIGLLT NDEVIAVNQA
GRPAHPVSTA TNQQVWYANN GDGSYTVALF NLGSASATVT ANWSDIGLYG SATVRDLWTH
TDLGKFATGY SAVNLAPHAS RMLRVVTNGG ANVVNDDDTG ISYTGSWQRS WNRGLGDFKD
DVHYTQANGD YFEFKFNGTG IDLYTEKDSS QGNVDVYIDG VLKQTVNTYN ATRQTQQKVY
SASGLSNGVH TLKAVKKTGT YMLLDKLSFN VAAPIEANDT DAGFTYSGSW STSTARGFGD
YNDDVHYTMT NNDYFQYAFN GTGVDLVTEK DSAQGDIDIY VDGVFKQTVS TYNATRLAQQ
TVYSIRGLAS GSHTIKAVKK SGTYMLLDKL NVRSSRIQLN NTDSGITYSG SWSLNAGRGY
GDYNDDVHFT AANNDYMQYT FNGTGIEMLG EKASDQGNVD IYIDNVLQTT ANTYNATRLV
NQSIYSVNGL NAGSHTIKAV KKTGSYMLVD SLRVTP
//
