ID A0A1N6KEK8_9BACT Unreviewed; 706 AA.
AC A0A1N6KEK8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=SAMN04488055_5661 {ECO:0000313|EMBL:SIO54757.1};
OS Chitinophaga niabensis.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=536979 {ECO:0000313|EMBL:SIO54757.1, ECO:0000313|Proteomes:UP000185003};
RN [1] {ECO:0000313|EMBL:SIO54757.1, ECO:0000313|Proteomes:UP000185003}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24787 {ECO:0000313|EMBL:SIO54757.1,
RC ECO:0000313|Proteomes:UP000185003};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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|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; FSRA01000002; SIO54757.1; -; Genomic_DNA.
DR RefSeq; WP_074242869.1; NZ_FSRA01000002.1.
DR AlphaFoldDB; A0A1N6KEK8; -.
DR STRING; 536979.SAMN04488055_5661; -.
DR OrthoDB; 9758822at2; -.
DR Proteomes; UP000185003; 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; 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.
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:UP000185003};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..706
FT /note="Alpha-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013133965"
FT DOMAIN 61..263
FT /note="Glycosyl hydrolase family 36 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16875"
FT DOMAIN 623..702
FT /note="Glycosyl hydrolase family 36 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16874"
FT ACT_SITE 459
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT ACT_SITE 528
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 343..344
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 423
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 457..461
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 506
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 528
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
SQ SEQUENCE 706 AA; 80893 MW; BA320F403B6EDA5A CRC64;
MKRKLLIIVL SVFYPAAQLL AQQQIAIETN HLQWLLQVNE KGKLYQSYLG EKLSTPAEVK
ASRHQAYIAA GMNDLFEPAI RVTHKDGNPS LDLVFAGVET KKEDANTSTT IITLKDPVYP
IQVKLHLTAY YRENIFKSFT EITHQEKGTV TLHNYASAML HFDAPHYWLT QFHGDWAEEM
KVQETELTSG IKILDSKLGS RAHMYQPPFF FLSLDQPADE NNGEVLAGTL AWSGNFRFAF
EVDEQNALRM IAGMNNYAAD YPLPAGKSFI TPAFIFTYST TGKGTASRNF HSWAGKYGVM
DGDSSRMVLL NNWEATGFDF DEQKLTSLFA ETRKLGADLF LLDDGWFANK YPRNSDHAGL
GDWEENKAKL PHGIGHLVKE ATANQIKFGI WLEPEMINPR SKLYEDHPDW VLKLPNRPED
YFRNQLVLDL VNPAVQDFVY DVVDKLLTKN PGIAYIKWDC NRMMTNAWSP FLKEQQSSLS
IAYTQSLYKI LEKLRVKYPH LPMMLCSGGG GRVDYGALRY FTEFWPSDNT DGLERVFMQW
GYSYFFPSFT ISSHVTSWGK QSLKFRTDVA MMGRLGYDID VNKFTEEEWR FSQEAIKNYN
RLKDVIAHGA LYRLVSPYKE RRAVLMYVND NKTKSVLFAY NLHTQYGEQF RKVRLNGLDP
QKKYTVKEIN AEGKESAYSG DYLMKIGLPV SSEKELTSKV FEITAM
//
