ID Q1Z8X4_9GAMM Unreviewed; 997 AA.
AC Q1Z8X4;
DT 02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 02-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 82.
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 ORFNames=P3TCK_20910 {ECO:0000313|EMBL:EAS44984.1};
OS Photobacterium profundum 3TCK.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=314280 {ECO:0000313|EMBL:EAS44984.1, ECO:0000313|Proteomes:UP000003789};
RN [1] {ECO:0000313|EMBL:EAS44984.1, ECO:0000313|Proteomes:UP000003789}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3TCK {ECO:0000313|EMBL:EAS44984.1,
RC ECO:0000313|Proteomes:UP000003789};
RA Bartlett D.H., Valle G., Lauro F.M., Vezzi A., Simonato F., Eloe E.,
RA Vitulo N., Stratton T.K., D'angelo M., Ferriera S., Johnson J., Kravitz S.,
RA Beeson K., Sutton G., Rogers Y., Friedman R., Frazier M., Venter J.C.;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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:EAS44984.1}.
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DR EMBL; AAPH01000002; EAS44984.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1Z8X4; -.
DR HOGENOM; CLU_002346_0_2_6; -.
DR Proteomes; UP000003789; 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}.
FT DOMAIN 687..958
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 997 AA; 114414 MW; 935EFD4ECB1E234B CRC64;
MLLSGQWTFN FFNNPMLVPD EFYNQEMAEW DSIQVPNMWQ MEGHGKLQYT DEGFPFPIDV
PFVPTNNPTG AYQRTFTLGD AWDEQQTIIR FDGVETYFEV YVNGQYVGFS KGSRLTAEFD
ISEQVKVGKN LLSVRVMQWA DSTYIEDQDM WWTAGIFRDV YLIGKKPVHV YDYTIRTDFD
TQYQSATLSG SVVIENLQTA QASGFQLEYA LYDGNQLISD GSVDNLAIEE CHTATFAIDV
TNPVHWTAEN PHLYHLFLTL KDHTGSTIEI IPQRVGFRDI KVKDGLFYIN NQYAMLHGVN
RHDNDHLNGR AVGMDRVEKD LILMKQHNIN SVRTAHYPND PRFYEMCDIY GLFVMAETDV
ETHGFANVGD LSRITDDAEW ENVFVDRIER QIHAQKNHPS IIMWSLGNES GYGCNIRAMC
KAAKAIDDTR LVHYEEDRNA EVVDIVSTMY SRVQLMNYFG EQPMDKPRII CEYAHAMGNG
PGGLTEYQNV FYKHDHIQGH FLWEWCDHGI LEQDEKGRDV YKYGGDYGDY PNNYNFCMDG
LVYSDQTPGP GLREYKQVIC PVKVSVKDAE NGLITVENKY WFSTLDDITL LVDIRAEGET
LAQYQLSVAN VKVGESRDLQ VALPELDERE VFINVSVRKN SSTRYSVANS ELGIFQFQIK
ENTAQLPTFT HTNSTALNVK EQRLEWIVEG YNFELTFSKI SGQLTSWLSN GIEIIASSPK
MNFFKPMIDN HKQEYEGLWE PAHLQIMEEH FRTLHIEQQD GNVIVTVNSI VAPPVLDFGM
RCTYIYEIHS EGQVNLSLTG KKYGEYPHVI PVLGLDMGIN KQFEHVEYYG RGPEENYLDS
KQCNIIDVYQ STVTRMFENY PFPQNNGNRQ DVRWASLVNR QGNGLFVKPQ QPINLSAWHY
TSKHLHEAQH INELEKSGYI TLNLDHKLMG LGSNSWGSEV LDSYRVYMND FQYALTLLPF
SQANCRANYL AGQDFSLNTQ TAQNIQENTP SMIGGDK
//
