ID A0A0L8V931_9BACT Unreviewed; 735 AA.
AC A0A0L8V931;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=NC99_22950 {ECO:0000313|EMBL:KOH44863.1};
OS Sunxiuqinia dokdonensis.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Prolixibacteraceae;
OC Sunxiuqinia.
OX NCBI_TaxID=1409788 {ECO:0000313|EMBL:KOH44863.1, ECO:0000313|Proteomes:UP000036958};
RN [1] {ECO:0000313|Proteomes:UP000036958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK {ECO:0000313|Proteomes:UP000036958};
RA Ahn S., Kim B.-C.;
RT "Genome sequencing of Sunxiuqinia dokdonensis strain SK.";
RL Submitted (JUL-2015) 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|ARBA:ARBA00001255,
CC ECO:0000256|PIRNR:PIRNR005536};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase.
CC {ECO:0000256|PIRNR:PIRNR005536}.
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:KOH44863.1}.
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DR EMBL; LGIA01000151; KOH44863.1; -; Genomic_DNA.
DR RefSeq; WP_053183420.1; NZ_LGIA01000151.1.
DR AlphaFoldDB; A0A0L8V931; -.
DR STRING; 1409788.NC99_22950; -.
DR PATRIC; fig|1409788.3.peg.2369; -.
DR OrthoDB; 9758822at2; -.
DR Proteomes; UP000036958; 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 C-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:UP000036958}.
FT DOMAIN 51..284
FT /note="Glycosyl hydrolase family 36 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16875"
FT DOMAIN 643..728
FT /note="Glycosyl hydrolase family 36 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16874"
FT ACT_SITE 480
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT ACT_SITE 548
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT BINDING 197
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 364..365
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 444
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 478..482
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 526
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 548
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
SQ SEQUENCE 735 AA; 85167 MW; B1E3563D396E925B CRC64;
MYSIYRFIPW LFRSLSVFIL LLFMVSGIQA QIIPVETSQN AMVFQVDKSN DLKMIYFGER
LSIDSEYTYI SEQYKQATDY TNVYNSAYTS AGSRNLLEPA IRLTHSDGNQ SLDLEYVNHQ
TETIDANVSL LKVTMKDRVY PVQVELYYQS YFNEDVIEQW AVISHQEKKP VVLHKFASAN
LSLKGKEFYL TQYYGDWAKE MQPEESKLTH GIKTIDSKLG TRANLFQPSV FMVSFDQPAN
EDEGTVLYGA LEWSGNFKIE MELDPQDNLR IIAGMNDYAS EYKLPAKQKF KTPAFLHVLS
QKGKGEASRK LHTWARNYKV LDGKGDRLTL LNNWEATYFD FNEQKLFSLL KDTKKLGVDL
FLLDDGWFGN EYPRNNDDAG LGDWQANRKK LPNGVSSLVE EATKNGVKFG IWVEPEMVNP
ESSLYHEHPD WVIKQPRRDE HYFRNQLVLD LSNPEVQDFV FKVVDDLFVE NPDLAYIKWD
CNAVIYNAYS NHLKEQTHLY IDYVRGLYNV LERIRDKYPT VPMMLCSGGG GRVDYAALQY
FTEFWPSDNT DPLERVFMQW EYSYFYPAIS TSNHVTDWGK QSLKYKVDVA MMGKLGFDIV
IGELPDEELR FCQQAVEAYD KLKETVWHGD LYRLADPKEN DFASLMFVNL EKSEGVVFNY
LVNNRYDKKS EDPIRFKGLD TAKNYQIQEV NIYPGTSSPL NSDQVFSGEF LMKIGYNPQV
HAGRKSVVLL IREVK
//
