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Database: UniProt
Entry: A0A0D4C2H6_9MICC
LinkDB: A0A0D4C2H6_9MICC
Original site: A0A0D4C2H6_9MICC 
ID   A0A0D4C2H6_9MICC        Unreviewed;       732 AA.
AC   A0A0D4C2H6;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
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=UM93_02325 {ECO:0000313|EMBL:AJT42808.1};
OS   Psychromicrobium lacuslunae.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Psychromicrobium.
OX   NCBI_TaxID=1618207 {ECO:0000313|EMBL:AJT42808.1, ECO:0000313|Proteomes:UP000061839};
RN   [1] {ECO:0000313|EMBL:AJT42808.1, ECO:0000313|Proteomes:UP000061839}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IHBB 11108 {ECO:0000313|EMBL:AJT42808.1,
RC   ECO:0000313|Proteomes:UP000061839};
RX   PubMed=25908143;
RA   Kiran S., Swarnkar M.K., Pal M., Thakur R., Tewari R., Singh A.K.,
RA   Gulati A.;
RT   "Complete Genome Sequencing of Protease-Producing Novel Arthrobacter sp.
RT   Strain IHBB 11108 Using PacBio Single-Molecule Real-Time Sequencing
RT   Technology.";
RL   Genome Announc. 3:0-0(2015).
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; CP011005; AJT42808.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D4C2H6; -.
DR   STRING; 1618207.UM93_02325; -.
DR   KEGG; ari:UM93_02325; -.
DR   PATRIC; fig|1618207.4.peg.475; -.
DR   HOGENOM; CLU_009640_3_1_11; -.
DR   Proteomes; UP000061839; 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   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:UP000061839}.
FT   DOMAIN          27..274
FT                   /note="Glycosyl hydrolase family 36 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16875"
FT   DOMAIN          634..719
FT                   /note="Glycosyl hydrolase family 36 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16874"
FT   ACT_SITE        464
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT   ACT_SITE        530
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT   BINDING         189
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT   BINDING         352..353
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT   BINDING         429
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT   BINDING         462..466
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT   BINDING         508
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT   BINDING         530
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
SQ   SEQUENCE   732 AA;  81047 MW;  2463E21BC98FB8EB CRC64;
     MKHPTNALIS LQAAQVALVL DCREGRLPEV VHWGEALGAL SDQELLALAE ANISPVVSNM
     VDLPVRVAIL PAHSAGWLGR PGLSGSRDGT AWSPQFTVSA LQLDGHAVEG LPEPQGPVVL
     QGQRLIVQAS DPAAQLGLRL EIEMTDSGLL RARAELQNQS TQPYQLDELN FAFPVPLAAQ
     ELLDFAGHWG KERVPQRSRM TVGSHLREGR KGRTGSDAAT LLCLGKQGFC FQQGEVWSVH
     LGFSGNHRHY AERTFHGVQL LGAGELLLPG EVRLTQGQSY QSPWVYASYG QGLDEVAAKF
     HRFLRELPGR ASKPRPATLN VWEAVYFDHD LERLLGLAET AAHIGVERFV LDDGWFLGRR
     DDRAGLGDWY VDPAVWPNGL APLVGRVGEL GMEFGLWFEP EMVNLDSELA RRHPEWVMAT
     GDRLPVESRH QQVLNLAIPE AYEFIRDRMV ELLTEYSISY IKWDHNRDLV DAGRQPSGVP
     SVHEQTLATY RLMDELKARF PELEIESCSS GGARVDLGVL ERTDRVWASD CIDPLERQHI
     DRWTGQLIPP ELIGSHVAST RSHTTGRRHD LSFRAGTALF GHFGIEWDLN AASAEELAEL
     ADWIRLYQQE RPLLHSGKVV RVDHADPSLL IRGVVSADQR QGLFQLAYLS RSEFAPRGRF
     QLAGLDPEAR YQVRLLAPGD KPHGLVAPHW LTQLSAAASD DTQYSGAALQ KVGLQLPEAS
     PEQIVLLKLS AL
//
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