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
//