ID A0A0L0GIV1_9ENTR Unreviewed; 1030 AA.
AC A0A0L0GIV1;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU361154};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU361154};
DE AltName: Full=Lactase {ECO:0000256|ARBA:ARBA00032230, ECO:0000256|RuleBase:RU361154};
GN Name=ebgA {ECO:0000313|EMBL:KNC89055.1};
GN ORFNames=GM31_08280 {ECO:0000313|EMBL:KNC89055.1};
OS Trabulsiella odontotermitis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Trabulsiella.
OX NCBI_TaxID=379893 {ECO:0000313|EMBL:KNC89055.1, ECO:0000313|Proteomes:UP000037393};
RN [1] {ECO:0000313|EMBL:KNC89055.1, ECO:0000313|Proteomes:UP000037393}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12 {ECO:0000313|EMBL:KNC89055.1,
RC ECO:0000313|Proteomes:UP000037393};
RX PubMed=26162887;
RA Sapountzis P., Gruntjes T., Otani S., Estevez J., da Costa R.R.,
RA Plunkett G.3rd., Perna N.T., Poulsen M.;
RT "The Enterobacterium Trabulsiella odontotermitis Presents Novel Adaptations
RT Related to Its Association with Fungus-Growing Termites.";
RL Appl. Environ. Microbiol. 81:6577-6588(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|RuleBase:RU361154};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401, ECO:0000256|RuleBase:RU361154}.
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:KNC89055.1}.
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DR EMBL; JNGI01000177; KNC89055.1; -; Genomic_DNA.
DR RefSeq; WP_049858014.1; NZ_JNGI01000177.1.
DR AlphaFoldDB; A0A0L0GIV1; -.
DR PATRIC; fig|379893.4.peg.1689; -.
DR OrthoDB; 9758603at2; -.
DR Proteomes; UP000037393; 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:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR Gene3D; 2.70.98.10; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR004199; B-gal_small/dom_5.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR014718; GH-type_carb-bd.
DR InterPro; IPR006101; Glyco_hydro_2.
DR InterPro; IPR023232; Glyco_hydro_2_AS.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR023230; Glyco_hydro_2_CS.
DR InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR InterPro; IPR006104; Glyco_hydro_2_N.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR032312; LacZ_4.
DR PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR46323:SF2; BETA-GALACTOSIDASE; 1.
DR Pfam; PF02929; Bgal_small_N; 1.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF02836; Glyco_hydro_2_C; 1.
DR Pfam; PF02837; Glyco_hydro_2_N; 1.
DR Pfam; PF16353; LacZ_4; 1.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SMART; SM01038; Bgal_small_N; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 2.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1.
DR PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361154};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361154};
KW Reference proteome {ECO:0000313|Proteomes:UP000037393}.
FT DOMAIN 727..998
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1030 AA; 118159 MW; E0895FCAEBF8CF44 CRC64;
MNRWENIHLT HENRLPPRAY FFSYPSVAQA RTFAREASTL FQLLSGQWNF RFFDNPLRVP
EIFTSEMMTG WGSITVPGMW QMEGHGNLQY TDEGFPFPID VPYVPTDNPT GAYQRTFTLA
DGWQDKQTII KFDGVETYFE VYVNGHYIGF SKGSRLTAEF DITDAVTTGE NLLCVRVMQW
ADSTYIEDQD MWWSAGIFRD VYLIGKTLAH VQDFTVRTDF SDDYQHATLA CQVELENLAA
AHADLTLEYA LYDGDDILHQ GALDTLSVAQ QQSVRFAIPV THPQPWSAEN PYLYHLVMTL
KARHGEILEV IPQRVGFRDI KVRDGLFYVN NRYLMLHGVN RHDNDHLKGR AVGMDRVERD
LILMKQHNIN SVRTAHYPND PRFYELCDIY GLFVMAETDV ESHGFANVGD LSRITDDPEW
EPVYVERIVR HVQAQKNHPS IIIWSLGNES GYGCNIRAMA RATRELDDTR LIHYEEDRDA
EVVDIISTMY TRVPLMNEFG EYPHPKPRII CEYAHAMGNG PGGLTEYQNV FYRHDSIQGH
YVWEWCDHGI QARDASGEVF YKFGGDYGDY PNNYNFCLDG LIYSDQTPGP GLKEYKQVIA
PVKVFAGDLS RGELRVENKL WFTTLEDYTL HVEVRAEGET LSCQQLKVAN LAPNSGRAIV
FALPRLDERE TFVNIRITRD SRTRYSDAGH EIAVYQFPLK ARTACEAPWV HPNTTPLTLD
DQRLECVITG HNFRLVFSRV TGKLISWQVN GEERISREPK INFFKPVIDN HKQEFEGLWR
PNHLPIMQEH LRGVEVDARG SAVLITTRSI IAPPVFDFGM RCTYRWRVTA DGQLNVELSG
ERYGDFPHII PCIGFTLGIN GDFDQVAYYG RGPGENYPDS QQASIIDVWR STVDDMFENY
PFPQNNGNRQ HIRWASLTNR HGSGLLVVPQ KPIHFSAWHY RAEDIHVAQH CNELIRRDDI
TLNLDHQLLG LGSNSWGSEV LDSWRVWFAP FRYGFTLLPL DGGIATSQVL ARQTFGDGFF
STDSHSEAEQ
//
