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Database: UniProt
Entry: A0A085G0B4_9ENTR
LinkDB: A0A085G0B4_9ENTR
Original site: A0A085G0B4_9ENTR 
ID   A0A085G0B4_9ENTR        Unreviewed;       707 AA.
AC   A0A085G0B4;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
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:KFC77159.1};
GN   ORFNames=GBAG_3892 {ECO:0000313|EMBL:KFC77159.1};
OS   Buttiauxella agrestis ATCC 33320.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Buttiauxella.
OX   NCBI_TaxID=1006004 {ECO:0000313|EMBL:KFC77159.1, ECO:0000313|Proteomes:UP000028653};
RN   [1] {ECO:0000313|EMBL:KFC77159.1, ECO:0000313|Proteomes:UP000028653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33320 {ECO:0000313|EMBL:KFC77159.1,
RC   ECO:0000313|Proteomes:UP000028653};
RA   Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.;
RT   "ATOL: Assembling a taxonomically balanced genome-scale reconstruction of
RT   the evolutionary history of the Enterobacteriaceae.";
RL   Submitted (MAY-2014) 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}.
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:KFC77159.1}.
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DR   EMBL; JMPI01000068; KFC77159.1; -; Genomic_DNA.
DR   RefSeq; WP_034499282.1; NZ_JMPI01000068.1.
DR   AlphaFoldDB; A0A085G0B4; -.
DR   STRING; 1006004.GBAG_3892; -.
DR   eggNOG; COG3345; Bacteria.
DR   OrthoDB; 9758822at2; -.
DR   Proteomes; UP000028653; 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:UP000028653}.
FT   DOMAIN          24..236
FT                   /note="Glycosyl hydrolase family 36 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16875"
FT   DOMAIN          609..693
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        505
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-1"
FT   BINDING         163
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT   BINDING         329..330
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         483
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
FT   BINDING         505
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005536-2"
SQ   SEQUENCE   707 AA;  80269 MW;  10D7CD3C9770A985 CRC64;
     MEPIYHRLTS AQSDIVIRTQ PFAEIVYWGQ HLVHFSPLDC ASLDRPIANG RLDIDTPITL
     GAELGRGLFG SPGIEGHRNG LDASPIFTTT QVEQNGQNLT ITAEDKQAGL RLISELRLDS
     SGVLQIRHGL TNLRATPWQV DRLAITLPIA ERALEVMAFH GRWTREFQPH RIRLEHDSFV
     LENRRGRTSH EHFPAMIAGT AAFSEQQGAV WGVHLGWSGN HRLRCEVKTD GRRYLQAEAL
     YLAGEMALGE GETLHTPWLY ASHSGNGLNG MSQQFHQFLR EQVIRFPENK PRPVHLNTWE
     GIYFDHNPEY IMQMASRAAE LGVERFIIDD GWFKGRNHDR AALGDWYLDE QKYPNGLMPV
     INHVKACGME FGIWVEPEMI NPDSDLYRAH PDWVLALPGY EQATGRYQWV LDLSNPQVFD
     YLLERMNWLL GEHPIDYVKW DMNRELVQAG HNGKAAADAQ TRQFYRLLDE LNRKYPHVEF
     ESCASGGGRI DYEVLKRTHR FWASDNNDAL ERNTIQRGMS YFFPPEVMGA HIGNLRCHAT
     YRQHSIEFRG LTALFGHLGM ELDPMTADAA ESAGYERYVQ LYKQWRPLLH TGKQWRVDMP
     DATTQVQGVV AEDKSQALYL VSQLAMPDYT LAGNLRVPGL DPAARYCITL LDHPQISVVG
     KGGHTMRKLP GWMETTQTVS GEWLAQAGLA LPILDPESAI LIGFERV
//
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