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Database: UniProt
Entry: B1Y1P2_LEPCP
LinkDB: B1Y1P2_LEPCP
Original site: B1Y1P2_LEPCP 
ID   B1Y1P2_LEPCP            Unreviewed;       728 AA.
AC   B1Y1P2;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   24-JAN-2024, entry version 68.
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   OrderedLocusNames=Lcho_3246 {ECO:0000313|EMBL:ACB35504.1};
OS   Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix
OS   discophora (strain SP-6)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Leptothrix.
OX   NCBI_TaxID=395495 {ECO:0000313|EMBL:ACB35504.1, ECO:0000313|Proteomes:UP000001693};
RN   [1] {ECO:0000313|EMBL:ACB35504.1, ECO:0000313|Proteomes:UP000001693}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51168 / LMG 8142 / SP-6
RC   {ECO:0000313|Proteomes:UP000001693};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Lykidis A., Emerson D., Richardson P.;
RT   "Complete sequence of Leptothrix cholodnii SP-6.";
RL   Submitted (MAR-2008) 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; CP001013; ACB35504.1; -; Genomic_DNA.
DR   RefSeq; WP_012348251.1; NC_010524.1.
DR   AlphaFoldDB; B1Y1P2; -.
DR   STRING; 395495.Lcho_3246; -.
DR   CAZy; GH36; Glycoside Hydrolase Family 36.
DR   KEGG; lch:Lcho_3246; -.
DR   eggNOG; COG3345; Bacteria.
DR   HOGENOM; CLU_009640_3_1_4; -.
DR   OMA; WEGIYFD; -.
DR   OrthoDB; 9758822at2; -.
DR   Proteomes; UP000001693; 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   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR038417; Alpga-gal_N_sf.
DR   InterPro; IPR002252; Glyco_hydro_36.
DR   InterPro; IPR031704; Glyco_hydro_36_N.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR43053:SF3; ALPHA-GALACTOSIDASE-RELATED; 1.
DR   PANTHER; PTHR43053; GLYCOSIDASE FAMILY 31; 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|PIRNR:PIRNR005536};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR005536, ECO:0000313|EMBL:ACB35504.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001693}.
FT   DOMAIN          37..257
FT                   /note="Glycosyl hydrolase family 36 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16875"
FT   ACT_SITE        461
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT   ACT_SITE        526
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
SQ   SEQUENCE   728 AA;  79743 MW;  0E6B09603C44F08A CRC64;
     MNTRTHSASL PDSPAQFIAL HGRASSIVIE AHADEAPIWR YWGPRLPDAA TPGAALRDSR
     PLPSFMLDFD QPLTVAPTFG VGWFGQSALL AHRDGLDFAQ AYTRCEIEWL APGSAVCLHL
     HDDVARLRLD LTLKLDAASD VLTLQSTLHN LGDSAIDVQW LASGTLPLPG HSQQVRSYAG
     QHVHEFLLQT DPLTRSLWRK ESRRGRTSHD CFPGAVVTTP GATDDAGLVF GAHLAWSGNH
     QQTIEWLHDG QYQWQMGEWL APGEGRLAPG QALHTPEIVA SCSTAGLNGL AANFHAELRS
     RLNWPGGAMR ARPVHLNTWE GFYFDVHPGP VKELATAAAA VGIERFVLDD GWFHGRHHDR
     AALGDWWPDE SKFPAGLGEL IGHVNGLGMS FGLWVEPEMV NPDSELFRAH PDWALQVAGR
     PLLTARNQLV LDISRPEAAD YLFDKISALL AAHPIDYLKW DHNRDLAPAG LANGAPGYRA
     QVHAVYALMA RLRAAHPQVE IESCSGGGGR IDFAVLRHTH RVWTSDCIDA LSRVAIQRGF
     LQFFPPEIMG SHVGTAPSHT TGRTQNMAFR AAVALPGHLG VELDVRHLNE AETTELRAWI
     ALYKQLRDRL HTGRVWLGEV ADGIAWQAHG NAAAGDVLLL VYRTAPSSHR YTPVLRLTML
     DAGARYRVHE VLPDGTVRAT GHHNTAPFFD AINTPEGLTL DGAWLAHAGL PLPRAQAETA
     FIVRLQKV
//
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