ID   AGAL_CELJU              Reviewed;         404 AA.
AC   B3PGJ1;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Alpha-galactosidase A;
DE            EC=3.2.1.22;
DE   AltName: Full=Alpha-D-galactoside galactohydrolase;
DE   AltName: Full=Alpha-galactosidase 27A;
DE   AltName: Full=Melibiase;
DE   Flags: Precursor;
GN   Name=agaA; Synonyms=aga27A; OrderedLocusNames=CJA_0246;
OS   Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp.
OS   cellulosa).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Cellvibrio.
OX   NCBI_TaxID=498211;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP   SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=11064195; DOI=10.1111/j.1574-6968.2000.tb09382.x;
RA   Halstead J.R., Fransen M.P., Eberhart R.Y., Park A.J., Gilbert H.J.,
RA   Hazlewood G.P.;
RT   "Alpha-galactosidase A from Pseudomonas fluorescens subsp. cellulosa:
RT   cloning, high level expression and its role in galactomannan hydrolysis.";
RL   FEMS Microbiol. Lett. 192:197-203(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ueda107;
RX   PubMed=18556790; DOI=10.1128/jb.01701-07;
RA   DeBoy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H.,
RA   Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J.,
RA   Nelson K.E.;
RT   "Insights into plant cell wall degradation from the genome sequence of the
RT   soil bacterium Cellvibrio japonicus.";
RL   J. Bacteriol. 190:5455-5463(2008).
RN   [3]
RP   PHYLOGENETIC STUDY.
RX   PubMed=15285616;
RA   Naumov D.G.;
RT   "Phylogenetic analysis of alpha-galactosidases of the GH27 family.";
RL   Mol. Biol. (Mosk.) 38:463-476(2004).
CC   -!- FUNCTION: Hydrolyzes galactomannan found in plant cell wall, by
CC       cleaving alpha-1,6-D-galactose side-chains from the mannan backbone.
CC       Appears to act in synergy with mannanase (ManA) to elicit hydrolysis of
CC       galactomannan. Has greater activity against galactomannans with
CC       decreased degree of polymerisation values. To a lesser extent, is also
CC       able to degrade other galactosides containing alpha-1,6-linked D-
CC       galactose, such as melibiose and stachyose.
CC       {ECO:0000269|PubMed:11064195}.
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:0000269|PubMed:11064195};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8.2. {ECO:0000269|PubMed:11064195};
CC       Temperature dependence:
CC         Optimum temperature is 50 degrees Celsius. Displays half maximal
CC         activity in 25 minutes and 7 minutes when pre-incubated at 50 degrees
CC         Celsius and 55 degrees Celsius, respectively.
CC         {ECO:0000269|PubMed:11064195};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 27 family. {ECO:0000305}.
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DR   EMBL; CP000934; ACE85287.1; -; Genomic_DNA.
DR   RefSeq; WP_012485929.1; NC_010995.1.
DR   AlphaFoldDB; B3PGJ1; -.
DR   SMR; B3PGJ1; -.
DR   STRING; 498211.CJA_0246; -.
DR   CAZy; GH27; Glycoside Hydrolase Family 27.
DR   DNASU; 6415039; -.
DR   EnsemblBacteria; ACE85287; ACE85287; CJA_0246.
DR   KEGG; cja:CJA_0246; -.
DR   eggNOG; COG3345; Bacteria.
DR   HOGENOM; CLU_013093_2_2_6; -.
DR   OMA; AMTPTMG; -.
DR   OrthoDB; 469334at2; -.
DR   Proteomes; UP000001036; Chromosome.
DR   GO; GO:0004557; F:alpha-galactosidase activity; IDA:UniProtKB.
DR   GO; GO:0052692; F:raffinose alpha-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051682; P:galactomannan catabolic process; IDA:UniProtKB.
DR   CDD; cd14792; GH27; 1.
DR   Gene3D; 2.60.40.1180; -; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR002241; Glyco_hydro_27.
DR   InterPro; IPR000111; Glyco_hydro_27/36_CS.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR041233; Melibiase_C.
DR   PANTHER; PTHR11452; PTHR11452; 1.
DR   Pfam; PF16499; Melibiase_2; 1.
DR   Pfam; PF17801; Melibiase_C; 1.
DR   PRINTS; PR00740; GLHYDRLASE27.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00512; ALPHA_GALACTOSIDASE; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Glycosidase; Hydrolase; Reference proteome; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..404
FT                   /note="Alpha-galactosidase A"
FT                   /id="PRO_0000393719"
FT   ACT_SITE        152
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        207
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         185..189
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   DISULFID        45..77
FT                   /evidence="ECO:0000250"
FT   DISULFID        124..154
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   404 AA;  45900 MW;  45440E3439242539 CRC64;
     MRKQLLLGLG LVSALLVSVQ ASAQKFEQLA KTPQMGWNSW NTFGCNVDEK MIRAMADAMV
     TSGMKAAGYE YINIDDCWHG ERDKNGFIQA DKKHFPSGMK ALADYVHAKG LKLGIYSDAG
     NTTCAGRPGS RGHEYQDALT YASWGIDYVK YDWCDTQDIN PKSAYATMRD AIHKAGRPML
     FSICEWGDNQ PWEWAQDVGH SWRTTGDIYP CWNCEHNHGS WSSFGVLPIL DKQAGLRKYA
     GPGHWNDMDM MEVGNGMTEE EDRAHFSLWA FMASPLIAGN DLRNMSDTTR AILTHKETIA
     INQDKLGIQA MKWIDEGDLE IYIKPLEKGH YAVLFLNRAD DAMDYRFDWS FHYMKDDISK
     HEIFFDKQAF NWRNIWNGET GSTKEVLNIK VPAHGVVVLR LSPR