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Database: UniProt
Entry: A0A1C0ZWA8_9BACL
LinkDB: A0A1C0ZWA8_9BACL
Original site: A0A1C0ZWA8_9BACL 
ID   A0A1C0ZWA8_9BACL        Unreviewed;       731 AA.
AC   A0A1C0ZWA8;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
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=A8709_31655 {ECO:0000313|EMBL:OCT12386.1};
OS   Paenibacillus pectinilyticus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=512399 {ECO:0000313|EMBL:OCT12386.1, ECO:0000313|Proteomes:UP000093309};
RN   [1] {ECO:0000313|Proteomes:UP000093309}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC13222 {ECO:0000313|Proteomes:UP000093309};
RA   Zhang J., Zhang X.;
RT   "Paenibacillus oryzae. sp. nov., isolated from the rice root.";
RL   Submitted (MAY-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:OCT12386.1}.
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DR   EMBL; LYPC01000027; OCT12386.1; -; Genomic_DNA.
DR   RefSeq; WP_065856635.1; NZ_LYPC01000027.1.
DR   AlphaFoldDB; A0A1C0ZWA8; -.
DR   STRING; 512399.A8709_31655; -.
DR   OrthoDB; 9758822at2; -.
DR   Proteomes; UP000093309; 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 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.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000093309}.
FT   DOMAIN          30..286
FT                   /note="Glycosyl hydrolase family 36 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16875"
FT   DOMAIN          650..726
FT                   /note="Glycosyl hydrolase family 36 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16874"
FT   ACT_SITE        479
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT   ACT_SITE        549
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT   BINDING         200
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT   BINDING         367..368
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT   BINDING         444
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT   BINDING         477..481
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT   BINDING         527
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT   BINDING         549
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
SQ   SEQUENCE   731 AA;  82698 MW;  F99F85DE3D539265 CRC64;
     MSISFEPTQG IFHLQNKHMS YVLQIVHSTY LAHAYWGRPI RSGQLGSIIQ YTERASFSPN
     PDTKNRVFSL DTLPQEFPAY GTSDFREPAY QVALPNGSTI TELVYDKHRI VQGKPGLEGL
     PSTYVEADHE AETLEIELVD KLAGLRAILS YTIFANHAAI TRSVRFINEG SADLKLLRAL
     SMSLDYAHAD WDLLQLSGSW ARERHIERRA LAPGKLTVES RRGSSSHSHN PFVALLSKEA
     NEDHGDVYGF NLVYSGNFAA HAEVDPFATA RVYMGINPFD FSWLLEPGQQ FQTPEVVMVY
     SSNGLGEMSR AYHRLYRTRL CRGEYRDQVR PVLVNNWEAT YFNFNADKIE SIARAGKELG
     IELFVLDDGW FGKRNDDTTS LGDWVVDKVK LPGGIEDLVE RVNNLGLEFG LWFEPEMVSP
     ESDLYRNHPD WCLHVPDRRR TEGRGQLILD FSREDVREGV MGMLRNILSS APITYVKWDM
     NRNMTEIGSA SLPSERQRET AHRYILGLYD VLEKITSEYP HILFESCSGG GGRFDPGMLH
     YMPQTWTSDN TDAVCRLKIQ YGTSIVYPVS SMGSHVSAVP NHQVHRTTSL ETRGHVAMSG
     NFGYELDLTK FTDEEKEIVK AQVADYKKIR PLVQFGDMYR LLSPFEGNDT AWMIVSEDKT
     QAMVVFIRVL AQPYAPLKTL RLKGLNPDFD YQIEGSEGTF AGDHLLYAGL SVAGLHSDFE
     SKIWLLEAKP Q
//
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