AGAL_BACSU
ID AGAL_BACSU Reviewed; 432 AA.
AC O34645;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Alpha-galactosidase {ECO:0000305};
DE EC=3.2.1.22 {ECO:0000269|PubMed:31138628};
DE AltName: Full=Melibiase;
GN Name=melA {ECO:0000303|PubMed:31138628}; OrderedLocusNames=BSU30300;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9387221; DOI=10.1099/00221287-143-11-3431;
RA Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT 200 kb rrnB-dnaB region.";
RL Microbiology 143:3431-3441(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=168 / KM0;
RX PubMed=31138628; DOI=10.1128/jb.00109-19;
RA Morabbi Heravi K., Watzlawick H., Altenbuchner J.;
RT "The melREDCA operon encodes a utilization system for the raffinose family
RT of oligosaccharides in Bacillus subtilis.";
RL J. Bacteriol. 201:E00109-E00109(2019).
CC -!- FUNCTION: Catalyzes the hydrolysis of melibiose and alpha-galactosides
CC of the raffinose family of oligosaccharides (RFOs) such as raffinose
CC and stachyose. Cannot act on polymeric substrates such as locust bean
CC gum. {ECO:0000269|PubMed:31138628}.
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:31138628};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:31138628};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000269|PubMed:31138628};
CC Note=Binds 1 NAD(+) per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10 mM for melibiose {ECO:0000269|PubMed:31138628};
CC KM=25 mM for raffinose {ECO:0000269|PubMed:31138628};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:31138628}.
CC -!- INDUCTION: Repressed by the transcriptional regulator MelR. Induced by
CC melibiose and raffinose. {ECO:0000269|PubMed:31138628}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 4 family. {ECO:0000305}.
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DR EMBL; AF008220; AAC00383.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15008.1; -; Genomic_DNA.
DR PIR; E69656; E69656.
DR RefSeq; NP_390908.1; NC_000964.3.
DR RefSeq; WP_003246000.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; O34645; -.
DR SMR; O34645; -.
DR STRING; 224308.BSU30300; -.
DR CAZy; GH4; Glycoside Hydrolase Family 4.
DR jPOST; O34645; -.
DR PaxDb; O34645; -.
DR PRIDE; O34645; -.
DR EnsemblBacteria; CAB15008; CAB15008; BSU_30300.
DR GeneID; 937255; -.
DR KEGG; bsu:BSU30300; -.
DR PATRIC; fig|224308.179.peg.3286; -.
DR eggNOG; COG1486; Bacteria.
DR InParanoid; O34645; -.
DR OMA; EHIYHAA; -.
DR PhylomeDB; O34645; -.
DR BioCyc; BSUB:BSU30300-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0052692; F:raffinose alpha-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR019802; GlycHydrolase_4_CS.
DR InterPro; IPR001088; Glyco_hydro_4.
DR InterPro; IPR022616; Glyco_hydro_4_C.
DR InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR32092; PTHR32092; 1.
DR Pfam; PF02056; Glyco_hydro_4; 1.
DR Pfam; PF11975; Glyco_hydro_4C; 1.
DR PRINTS; PR00732; GLHYDRLASE4.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF56327; SSF56327; 1.
DR PROSITE; PS01324; GLYCOSYL_HYDROL_F4; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cytoplasm; Glycosidase; Hydrolase; Manganese;
KW Metal-binding; NAD; Reference proteome.
FT CHAIN 1..432
FT /note="Alpha-galactosidase"
FT /id="PRO_0000169851"
FT ACT_SITE 170
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 2..68
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 199
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
SQ SEQUENCE 432 AA; 49264 MW; E773A01018E65562 CRC64;
MKKITFIGAG STIFAKNVLG DCLLTEALNG FEFALYDIDP KRLQESQLML ENLRDRYNPS
VAINSYDDRK LALQNAGYVI NAIQVGGYKP STVIDFEIPK RYGLRQTIAD TVGIGGIFRS
LRTIPVLFDI AKDMEEMCPD AWFLNYTNPM ATLTGAMLRY TNIKTIGLCH SVQVCTKDLF
KALGMEHDGI EERIAGINHM AWLLEVKKDG TDLYPEIKRR AKEKQKTKHH DMVRFELMDK
FGYYVTESSE HNAEYHPYFI KRNYPELISE LQIPLDEYPR RCVKQIENWE KMRDDIVNNK
NLTHERSKEY GSRIIEAMET NEPFTFGGNV LNTGLITNLP SKAVVEVTCV ADRKKITPCF
AGELPEQLAA LNRTNINTQL MTIEAAVTRK KEAVYQAAML DPHTSAELSM KDIISMCDDL
FAAHGDWLPE YK