ID A0A1Y0EDY7_9RHOB Unreviewed; 694 AA.
AC A0A1Y0EDY7;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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 Name=rafA {ECO:0000313|EMBL:ARU01639.1};
GN ORFNames=LOKVESSMR4R_02334 {ECO:0000313|EMBL:ARU01639.1};
OS Yoonia vestfoldensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Yoonia.
OX NCBI_TaxID=245188 {ECO:0000313|EMBL:ARU01639.1, ECO:0000313|Proteomes:UP000195273};
RN [1] {ECO:0000313|EMBL:ARU01639.1, ECO:0000313|Proteomes:UP000195273}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMR4r {ECO:0000313|EMBL:ARU01639.1,
RC ECO:0000313|Proteomes:UP000195273};
RA Topel M., Pinder M.I.M., Johansson O.N., Kourtchenko O., Godhe A.,
RA Clarke A.K.;
RT "Genome Sequence of Loktanella vestfoldensis Strain SMR4r Isolated from a
RT Culture of the Diatom Skeletonema marinoi.";
RL Submitted (MAY-2017) 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; CP021431; ARU01639.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0EDY7; -.
DR STRING; 1122181.GCA_000382265_01410; -.
DR KEGG; lvs:LOKVESSMR4R_02334; -.
DR OrthoDB; 9758822at2; -.
DR Proteomes; UP000195273; 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; 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}.
FT DOMAIN 23..242
FT /note="Glycosyl hydrolase family 36 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16875"
FT DOMAIN 604..680
FT /note="Glycosyl hydrolase family 36 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16874"
FT ACT_SITE 441
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT ACT_SITE 498
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT BINDING 167
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 331..332
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 476
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 498
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
SQ SEQUENCE 694 AA; 77417 MW; 619E9C12C7AD1BC3 CRC64;
MTQTYRIDDG RQTLVLAATN ARLPQVVYWG ASLPADEDLA MLHIAHAIDV TGGMLDENPD
LSLCPEASRS FPGQPGLILR DGGGAALLAM FRFVKAEQTD AALRLTYRDA DKGLELTCAF
RSDPETHIIT CQTMLDADQP VHLDWLAAPV LPGPHYSDEM IDISGRWCGE FQLARTPWSP
GIRLRESRTG RSGHEHVPGL IVPCRGATNT QGEVYAFHYG WSGGHRMIAE ELPDGRRQIQ
WGHTAGSETS AATHFSTAPL YITYSDSGLN GCAIAFQRHL RDRVVTWPKP DAPRPVHYNC
WEAVYFDHDL PVLKDIASRA AALGAERFVL DDGWFGRRDD DTTSLADWVV DARKYPEGLH
PLIAHIQGLG MGFGLWFEPE MINEDSDIYR AHPGWVLGRA EQIRGRQQLV LNMALPAVRD
YLYDRIAAIL TDHPIEYIKW DHNRVLPMPD AAQTRGTYAL LDRLRADFPG VEIESCASGG
GRIDFGILQR TQRVWLSDSN DALERLRIQH DAALFLPLAV TGSHVGPRLC HTSGRTLDIS
LRAWVAAQRH MGFEMDPREL TDHEAAVLTK VTAWWKQHRH WLQTADILRL DSADPAVIAE
QQLARDKQCF VVFVGKAATS RQIAPRPLRL TGLDPQARYQ VTLVNRDEAP GLSRGAPLLK
SGSLVASGRY LMQHGVTLPW SFPERIWVLQ GESL
//
