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
//