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Database: UniProt/TrEMBL
Entry: K4J214_BIFAP
LinkDB: K4J214_BIFAP
Original site: K4J214_BIFAP 
ID   K4J214_BIFAP            Unreviewed;       700 AA.
AC   K4J214;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|PIRNR:PIRNR001084};
DE            Short=Beta-gal {ECO:0000256|PIRNR:PIRNR001084};
DE            EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|PIRNR:PIRNR001084};
GN   OrderedLocusNames=BAST_1202 {ECO:0000313|EMBL:AFU71775.1};
OS   Bifidobacterium asteroides (strain PRL2011).
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=1147128 {ECO:0000313|EMBL:AFU71775.1, ECO:0000313|Proteomes:UP000007006};
RN   [1] {ECO:0000313|EMBL:AFU71775.1, ECO:0000313|Proteomes:UP000007006}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PRL2011 {ECO:0000313|EMBL:AFU71775.1,
RC   ECO:0000313|Proteomes:UP000007006};
RX   PubMed=23028506; DOI=10.1371/journal.pone.0044229;
RA   Bottacini F., Milani C., Turroni F., Sanchez B., Foroni E., Duranti S.,
RA   Serafini F., Viappiani A., Strati F., Ferrarini A., Delledonne M.,
RA   Henrissat B., Coutinho P., Fitzgerald G.F., Margolles A., van Sinderen D.,
RA   Ventura M.;
RT   "Bifidobacterium asteroides PRL2011 genome analysis reveals clues for
RT   colonization of the insect gut.";
RL   PLoS ONE 7:E44229-E44229(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues
CC         in beta-D-galactosides.; EC=3.2.1.23;
CC         Evidence={ECO:0000256|ARBA:ARBA00001412,
CC         ECO:0000256|PIRNR:PIRNR001084};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 42 family.
CC       {ECO:0000256|ARBA:ARBA00005940, ECO:0000256|PIRNR:PIRNR001084}.
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DR   EMBL; CP003325; AFU71775.1; -; Genomic_DNA.
DR   RefSeq; WP_015022213.1; NC_018720.1.
DR   AlphaFoldDB; K4J214; -.
DR   STRING; 1147128.BAST_1202; -.
DR   GeneID; 41010423; -.
DR   KEGG; bast:BAST_1202; -.
DR   PATRIC; fig|1147128.3.peg.1226; -.
DR   eggNOG; COG1874; Bacteria.
DR   HOGENOM; CLU_012430_1_1_11; -.
DR   OMA; SRRHYCF; -.
DR   Proteomes; UP000007006; Chromosome.
DR   GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006012; P:galactose metabolic process; IEA:InterPro.
DR   CDD; cd03143; A4_beta-galactosidase_middle_domain; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR013739; Beta_galactosidase_C.
DR   InterPro; IPR013738; Beta_galactosidase_Trimer.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR003476; Glyco_hydro_42.
DR   InterPro; IPR013529; Glyco_hydro_42_N.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR36447; BETA-GALACTOSIDASE GANA; 1.
DR   PANTHER; PTHR36447:SF1; BETA-GALACTOSIDASE GANA; 1.
DR   Pfam; PF02449; Glyco_hydro_42; 1.
DR   Pfam; PF08533; Glyco_hydro_42C; 1.
DR   Pfam; PF08532; Glyco_hydro_42M; 1.
DR   PIRSF; PIRSF001084; B-galactosidase; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|PIRNR:PIRNR001084, ECO:0000313|EMBL:AFU71775.1};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR001084, ECO:0000313|EMBL:AFU71775.1}.
FT   DOMAIN          26..397
FT                   /note="Glycoside hydrolase family 42 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02449"
FT   DOMAIN          414..622
FT                   /note="Beta-galactosidase trimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF08532"
FT   DOMAIN          636..671
FT                   /note="Beta-galactosidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08533"
FT   ACT_SITE        162
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT   ACT_SITE        321
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT   BINDING         123
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT   BINDING         161
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT   BINDING         329
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ   SEQUENCE   700 AA;  78705 MW;  826649FA8EDB4315 CRC64;
     MSKPTRRAYR WPKHLKGQQS LWYGCDYNPD QWPEDVWDED IRLMTKAGVN VVALAVFSWS
     RIEPSQGVFD FDWLDRIIDK LGRAGIGVNL ASATASPPLW LTQAHPEVLL RDERGDTVWP
     GARQHWRPTS PVFRSYALKL CRAMAEHYRD NPYLVAWHVG NEYGCHNRFD YSDDAMRAFQ
     RWCRRRYKDI EAVNLAWGTN FWSQRLSDFS QILPPRFIGQ GNFQNPGRML DFERFSSDAL
     KDFYMAERDT LAEITPDIPL TTNFMVSAGG FALDYDDWGD QVDFVANDHY ATPGRNHLEE
     LAYSSSLVDA IARRRPWWLM EQSTSAVNWR PVNPRKEPGQ LERDSLAHLA LGADAICYFQ
     WRQSRAGAEK FHSAMLPHAG EDTAVFRDVC QLGVDLQGLS QAGLAGSTLA KAPLALVFDY
     ASQWASSHAS SPSDRVEHGQ EPPVWYRAFL DNAIRPDVLP VRATWEEYPL VVLPALYLID
     ADLSKRLHKY VHSGGRLIVT WGSGIADEQD RVWTGGYPGP LRDLLGLSVE EFAPMAPGTP
     GLLDHLDLTN GVTAHDWADV IGHLDKGAKV LASYRADPWT GMDGMPAMTV HNWGLGKAAY
     LGCRLDARGL AKVIPVLLEA LDVAEMRSAQ GDSDLLRVER VSQDDRTRFV FLFNRTKHPV
     QVQLEGQVLV GSLASIDGDG KQASLQVNGA LVQRVVGRRH
//
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