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Database: UniProt
Entry: A0A150LJD8_9BACI
LinkDB: A0A150LJD8_9BACI
Original site: A0A150LJD8_9BACI 
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
//
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