ID A0A150LJD8_9BACI Unreviewed; 718 AA.
AC A0A150LJD8;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-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=B4135_3057 {ECO:0000313|EMBL:KYD12493.1};
OS Caldibacillus debilis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Caldibacillus.
OX NCBI_TaxID=301148 {ECO:0000313|EMBL:KYD12493.1, ECO:0000313|Proteomes:UP000075683};
RN [1] {ECO:0000313|EMBL:KYD12493.1, ECO:0000313|Proteomes:UP000075683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4135 {ECO:0000313|EMBL:KYD12493.1,
RC ECO:0000313|Proteomes:UP000075683};
RA Berendsen E.M., Wells-Bennik M.H., Krawcyk A.O., De Jong A., Holsappel S.,
RA Eijlander R.T., Kuipers O.P.;
RT "Draft Genome Sequences of Seven Thermophilic Sporeformers Isolated from
RT Foods.";
RL Submitted (JAN-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 36 family.
CC {ECO:0000256|ARBA:ARBA00006202}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYD12493.1}.
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DR EMBL; LQYT01000092; KYD12493.1; -; Genomic_DNA.
DR RefSeq; WP_061569565.1; NZ_LQYT01000092.1.
DR AlphaFoldDB; A0A150LJD8; -.
DR STRING; 301148.B4135_3057; -.
DR PATRIC; fig|301148.3.peg.824; -.
DR OrthoDB; 9758822at2; -.
DR Proteomes; UP000075683; 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; 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-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}.
FT DOMAIN 28..274
FT /note="Glycosyl hydrolase family 36 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16875"
FT DOMAIN 637..714
FT /note="Glycosyl hydrolase family 36 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16874"
FT ACT_SITE 467
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT ACT_SITE 537
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 355..356
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 432
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 465..469
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 515
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT BINDING 537
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
SQ SEQUENCE 718 AA; 82274 MW; D605122172328E53 CRC64;
MPVFVDEKAA LFHLQAKNMS YIFRIMNGYP VHGYWGKKLN HQRGLAHLFK PYAKDFLDRL
PQEYPQYGSG DHRNPAYQIR LEEDGSRISE LVYKSCRIVK GKPKLDGLPA VYTETDKEAE
TLEVVLTDPY SGLEAILSYT VFKDFDCLAR SVRFTNKGKQ TIRLLRALSA SVDFPDNRFD
VLYLSGAWSR EAHIQRRPIG PGITAIESRR GASGHQLNPF MALLSPNADE DQGEVYGFSF
VYSGNFLIAA EVDQFFTTRV SVGINPFDFS WKLAPGESFQ TPETVMVYSS RGIGEMSRTF
HRLYRTRLAR GVYRDKERPI LVNNWEATYF NFNEKKLLEI AKAAAELGIE LFVLDDGWFG
KRDDATTSLG DWQEDRRKLP RGLAGLAKRV NDLGLKFGLW VEPEMVSPES ELYKKHPDWC
LHVKGRRRTL ARNQLILDLS RQDVREYIIE TFSGIFSRVP VSFVKWDMNR NMTEIGSEKW
PADRQMEIAH RYILGLYEIL ERLTSAFPHI LFENCSSGGG RFDPGMLYYM PQTWTSDNTD
AVERLKIQYG TSLVYPISAI GSHVSAVPNH QVGRVTPLAT RGHVAMSGNF GYELDLTKLT
EKEKKLVKEQ VARYKQIRRL VQQGDFYRLL SPFEGNETAW MFVSEDKKEA VVFYFRVLSE
PHPPRKRLLL KGLDPDRVYR LGEKAEYFAG DQLIGAGIPL RLPREDFTSL LFKLSAAT
//