ID A0A0R1RH15_9LACO Unreviewed; 683 AA.
AC A0A0R1RH15;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=FD35_GL000644 {ECO:0000313|EMBL:KRL54058.1};
OS Furfurilactobacillus rossiae DSM 15814.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Furfurilactobacillus.
OX NCBI_TaxID=1114972 {ECO:0000313|EMBL:KRL54058.1, ECO:0000313|Proteomes:UP000051999};
RN [1] {ECO:0000313|EMBL:KRL54058.1, ECO:0000313|Proteomes:UP000051999}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15814 {ECO:0000313|EMBL:KRL54058.1,
RC ECO:0000313|Proteomes:UP000051999};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRL54058.1}.
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DR EMBL; AZFF01000011; KRL54058.1; -; Genomic_DNA.
DR RefSeq; WP_017263026.1; NZ_AZFF01000011.1.
DR AlphaFoldDB; A0A0R1RH15; -.
DR STRING; 1114972.FD35_GL000644; -.
DR PATRIC; fig|1114972.6.peg.644; -.
DR eggNOG; COG1874; Bacteria.
DR Proteomes; UP000051999; Unassembled WGS sequence.
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 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; 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:UP000051999}.
FT DOMAIN 11..379
FT /note="Glycoside hydrolase family 42 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02449"
FT DOMAIN 393..608
FT /note="Beta-galactosidase trimerisation"
FT /evidence="ECO:0000259|Pfam:PF08532"
FT DOMAIN 631..679
FT /note="Beta-galactosidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08533"
FT ACT_SITE 145
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT ACT_SITE 305
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1"
FT BINDING 106
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
FT BINDING 314
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2"
SQ SEQUENCE 683 AA; 79010 MW; BB84AB362D171AE9 CRC64;
MLNHFLYGSA YYYEYLPYER LDEDIKMMKE ANINVVRIGE STWSTYEPQE GKFDFSKLDK
VIDAMATAHI NVILGTPTYA IPTWMAKKYP EVMLTDKSGK HQYGARQLID FTHPTFKFLA
ERIIRKMLKR TSQKPNVIGF QVDNETKHFS TSSNNVYIAF QKWLKNRFDS NLDQLNAEFG
MDYWSNRINA WEDFPPINST INGSLGSAFE KFQRTLVTAY LQWQVNIVND YKRSDQFVTN
NFDLEWRDQS FGLNAAVDIY KTSKVLTDTA IDIYHPTQSH LTGAEIAFGG DIARSTKDKP
YIVMETEAQS FKNWVPYPGQ LRLQAYSHIA SGAKMVEYWH WHSIHNSFET YWKGLLSHDF
KPNPVYNEAK KIGAELQSIG SNFVNSTKQN RIAIVVSNDS LTSVDWFPFR DKSEDHQYND
VLRNYYDTLY KLNTEVDILP IDSPKIFKYD LLIVPMLYSA TDGQLSSLNQ YVHEGGNIVY
GFRSGFTNEN VKVRTTVQPG IISKAIGAEY ELFVDPNQNA GTNEVENLVT VSGQSELADL
KNAAVHDWME LLTVTTGKIL AQYNHDYWGK YAAITENKYG KGKAFYIGSF FDQKDMKIIF
KYILKKTGVW SNRQEQSFPI INKRLIDSVH RNHLDFYFNY SSKPQKVIFY SSEGTSLFTH
ENLHNQDTFI LKPWDLQIFS TSF
//
