ID   A1SWB3_PSYIN            Unreviewed;       700 AA.
AC   A1SWB3;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   02-SEP-2026, entry version 89.
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   OrderedLocusNames=Ping_2014 {ECO:0000313|EMBL:ABM03778.1};
OS   Psychromonas ingrahamii (strain DSM 17664 / CCUG 51855 / 37).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Alteromonadales; Psychromonadaceae; Psychromonas.
OX   NCBI_TaxID=357804 {ECO:0000313|EMBL:ABM03778.1, ECO:0000313|Proteomes:UP000000639};
RN   [1] {ECO:0000313|EMBL:ABM03778.1, ECO:0000313|Proteomes:UP000000639}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=37 {ECO:0000313|EMBL:ABM03778.1,
RC   ECO:0000313|Proteomes:UP000000639};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Staley J.,
RA   Richardson P.;
RT   "Complete sequence of Psychromonas ingrahamii 37.";
RL   Submitted (JAN-2007) 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}.
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DR   EMBL; CP000510; ABM03778.1; -; Genomic_DNA.
DR   RefSeq; WP_011770338.1; NC_008709.1.
DR   AlphaFoldDB; A1SWB3; -.
DR   STRING; 357804.Ping_2014; -.
DR   KEGG; pin:Ping_2014; -.
DR   eggNOG; COG3345; Bacteria.
DR   HOGENOM; CLU_009640_3_1_6; -.
DR   OrthoDB; 9758822at2; -.
DR   Proteomes; UP000000639; Chromosome.
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   FunFam; 3.20.20.70:FF:000118; Alpha-galactosidase; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 2.70.98.60; alpha-galactosidase from lactobacil brevis; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR038417; Alpga-gal_N_sf.
DR   InterPro; IPR050985; Alpha-glycosidase_related.
DR   InterPro; IPR017853; GH_hydrolase_sf.
DR   InterPro; IPR002252; Glyco_hydro_36.
DR   InterPro; IPR031704; Glyco_hydro_36_N.
DR   PANTHER; PTHR43053:SF3; ALPHA-GALACTOSIDASE C-RELATED; 1.
DR   PANTHER; PTHR43053; GLYCOSIDASE FAMILY 31; 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.
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:UP000000639}.
FT   DOMAIN          21..248
FT                   /note="Glycosyl hydrolase family 36 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16875"
FT   ACT_SITE        441
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT   ACT_SITE        505
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT   BINDING         163
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT   BINDING         329..330
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT   BINDING         406
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT   BINDING         439..443
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT   BINDING         483
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT   BINDING         505
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
SQ   SEQUENCE   700 AA;  80264 MW;  5AC09B318EEE8D02 CRC64;
     MKNIIHLTSK NCSLIIKVET TPEILHWGPK INQIDPDILL ATERPIPQAR LDVDVPLSLC
     PELGSGHFNA PGLEGHRESF DWAPVFEVFD QDLAAQSVVF KLQDKVAKLQ LEIEIKLDFE
     SDVIQKRIKV INTGETKYSL TKLSSTLPLP NHANELMSFH GRWSREFQTH RQRFAHGGFM
     QENRRGRTSH ENFPGLFVGS DHFNEQNGQV WGFHLGWSGN HQLRADVRSD GRRFVQAGEL
     LLSGEVVLGA LESYSTPWLY ATYSAAGLNG ISEHFHRFVR DNIIKFPEDK PRPVHLNTWE
     GIYFEHDPQY IMKMANEAAV MGVERFIIDD GWFIGRHGER AALGDWYLDK EKYPNGLEPV
     IKHVNDLDME FGLWVEPEMV SEESMLYRAH PDWVLALQGY HQPSGRWQYV LDLQNTACFN
     YLFERLNDLL TRYNISYLKW DMNRELVQPG HQGKPAVSGQ TNALYALLDK LLAVHTEVEI
     ESCSSGGGRI DFEILKRTHR FWPSDCNDAL ERQTIQRGMS YFFPPEVMGT HIGPEESHTT
     RRVHHINMRG MTALSGHMGV ELDPVKVPVE ERQAFAKYIA LHKQYRHLLH SGRSFRVDTA
     DNSQNIYGVH NNDEMLITVC QLTMPDYALP SPLRISCIDT TAQYQVNLVE TPENSFQLMK
     QRPKWLDKTL TLSGESLKEI GLSLPILDPE SALMLHLKKR
//