ID A0A2Z5FYE3_9BACT Unreviewed; 710 AA.
AC A0A2Z5FYE3;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
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 ORFNames=ACPOL_2408 {ECO:0000313|EMBL:AXC11730.1};
OS Acidisarcina polymorpha.
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Acidisarcina.
OX NCBI_TaxID=2211140 {ECO:0000313|EMBL:AXC11730.1, ECO:0000313|Proteomes:UP000253606};
RN [1] {ECO:0000313|EMBL:AXC11730.1, ECO:0000313|Proteomes:UP000253606}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SBC82 {ECO:0000313|EMBL:AXC11730.1,
RC ECO:0000313|Proteomes:UP000253606};
RX PubMed=30510549; DOI=10.3389/fmicb.2018.02775;
RA Belova S.E., Ravin N.V., Pankratov T.A., Rakitin A.L., Ivanova A.A.,
RA Beletsky A.V., Mardanov A.V., Sinninghe Damste J.S., Dedysh S.N.;
RT "Hydrolytic Capabilities as a Key to Environmental Success: Chitinolytic
RT and Cellulolytic Acidobacteria From Acidic Sub-arctic Soils and Boreal
RT Peatlands.";
RL Front. Microbiol. 9:2775-2775(2018).
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; CP030840; AXC11730.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z5FYE3; -.
DR KEGG; abas:ACPOL_2408; -.
DR OrthoDB; 9800974at2; -.
DR Proteomes; UP000253606; 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:SF2; BETA-GALACTOSIDASE YESZ; 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};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR001084};
KW Reference proteome {ECO:0000313|Proteomes:UP000253606}.
FT DOMAIN 55..416
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 428..640
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT DOMAIN 650..706
FT /note="Beta-galactosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08533"
FT ACT_SITE 190
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT ACT_SITE 339
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 189
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 347
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ SEQUENCE 710 AA; 78990 MW; 763D2743ABF714D8 CRC64;
MPSLPTSANR RRSPRNWLAA AEILTALLLA LLPSTTQAQA TAYPNAPPLL LGAAWYPEQW
PEAQWDRDLA KMEAAHIRLV RMGEFAWSTM EPEEGHYDFT WLDHAIAKAA AHHIVVVLGT
PTAAPPAWLT TKYPETLRVD ENGVRDEHGN RQQFSFINTK YRQLARGIAG EMAKRYGHNP
NVVGWQLDNE YANDSFDPEA KAQFHEFLKK KYGSIQNLNQ KWATTYWSQT YDSFDEIPVR
PKNENPALLL DWRHFVSQGW KSYSVNQIEA IRPLADPRQF ITTNTMGWFD NFDEYVVHTV
LDMASWDDYI SDPVYDPFDN GARHDLTRGY KRKNFWVMET EPAFVNWRKT NNPLDKGQVR
DMAWQAIGHG SDAVEYWQWR AALNGQEQYH GVLVGADGNP VPVYDEVKQV GEEFEKAGAA
LAGTSPHAEV AILNDYNSRW AINFQRHSEK FDPVEELVAF YKPLSEAAQT VDIVSPDAPL
DGYKLVEAPA LNVLPKATAV RLVAYVQQGG NLLLGPRSGM KDEYDALNTQ LQPGDLSNLL
GGHVEQFYAL ENEVPVTADL GSGTAKIWAE QLSIPNIQVS GNSGDTKTIL TYGPSNGWLD
NQPAAITRKI GKGSITYLGV WLDDALLAKL TNQLVQQAGV QPKIPNVPAG VEVCVRSKGS
HAVAILINHT TSEQHVTLPN AATDLLANGT PSVSSEDLPK YGVAVVEISK
//
