ID C7M892_CAPOD Unreviewed; 1035 AA. AC C7M892; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 27-MAR-2024, entry version 76. 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 OrderedLocusNames=Coch_1807 {ECO:0000313|EMBL:ACU93352.1}; OS Capnocytophaga ochracea (strain ATCC 27872 / DSM 7271 / JCM 12966 / OS NCTC 12371 / VPI 2845) (Bacteroides ochraceus). OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Capnocytophaga. OX NCBI_TaxID=521097 {ECO:0000313|EMBL:ACU93352.1, ECO:0000313|Proteomes:UP000006650}; RN [1] {ECO:0000313|EMBL:ACU93352.1, ECO:0000313|Proteomes:UP000006650} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27872 / DSM 7271 / JCM 12966 / VPI 2845 RC {ECO:0000313|Proteomes:UP000006650}; RX PubMed=21304645; DOI=10.4056/sigs.15195; RA Mavrommatis K., Gronow S., Saunders E., Land M., Lapidus A., Copeland A., RA Glavina Del Rio T., Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., RA Bruce D., Goodwin L., Pitluck S., Pati A., Ivanova N., Chen A., RA Palaniappan K., Chain P., Hauser L., Chang Y.J., Jeffries C.D., Brettin T., RA Detter J.C., Han C., Bristow J., Goker M., Rohde M., Eisen J.A., RA Markowitz V., Kyrpides N.C., Klenk H.P., Hugenholtz P.; RT "Complete genome sequence of Capnocytophaga ochracea type strain (VPI RT 2845)."; RL Stand. Genomic Sci. 1:101-109(2009). 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 -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000256|ARBA:ARBA00001913}; CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. CC {ECO:0000256|ARBA:ARBA00007401, ECO:0000256|RuleBase:RU361154}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001632; ACU93352.1; -; Genomic_DNA. DR RefSeq; WP_015782848.1; NC_013162.1. DR AlphaFoldDB; C7M892; -. DR STRING; 521097.Coch_1807; -. DR CAZy; GH2; Glycoside Hydrolase Family 2. DR GeneID; 29675451; -. DR KEGG; coc:Coch_1807; -. DR eggNOG; COG3250; Bacteria. DR HOGENOM; CLU_002346_0_2_10; -. DR Proteomes; UP000006650; 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: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 Calcium {ECO:0000256|ARBA:ARBA00022837}; 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:UP000006650}. FT DOMAIN 756..1033 FT /note="Beta galactosidase small chain/" FT /evidence="ECO:0000259|SMART:SM01038" SQ SEQUENCE 1035 AA; 119753 MW; E06928076DAEAAD5 CRC64; MKNYLYIIIS FFLTIVSYAQ HLDSIFENPA LQEINRMSMR ASYFPFENIA KAKNGMIEQS ARFLNLNGLW SFLWKEDYRQ LPKDFYKTNF NESQWKKIPV PSNWEVQGYG IPIYVNASYE FNQKNPTPPD IPDSLQQNAG LYRKTFDLPT SWQGEKVYLH LGAVKSAFKL YINGKFVGMG KDSKLASEFD ITPYITKGKN LIAMEVRRWT DASYLECQDM WRFSGISRDC YLYMRPKVHL YDLSISAGLD KNYTNGKLTT SVEVWNETPS DVSKYQVEVS LFDKEQLLYQ EQKATIGLKK AFGKTELQFE AQLPQVRAWS AETPYLYRLQ MALYDAEGKV KEVVSRPIGF RTIEIEGANI LVNGKRILFK GVNRHETDPH TGQVVSQEQM ENDVKQMKAL NFNAVRTSHY PNDPYFYDLC DKYGLYVMDE ANIESHGMHY EMDKTIGNDP VWEYAHLLRM ERMVKRDKNH PSVLFWSMGN ESGNGWNFYK GYQHIKGLDS SRPIHYELAH YDWNTDIESR MYRRIPFLID YALSNHTKPF LQCEYAHAMG NSVGNFQEYW DVYEHYPKLQ GGFIWDFIDQ GLYKTLSNGK KIVTYGGDYG DKNTPSDNNF LINGVIASDR SWHPHAYEVR KVQQEIGFQY QNNQLILRNK HFFKDLLNYE IYWQLLKEGV PVQSGNITNL IVLPQSEATF LLPPLKTDDK AEYILQCTAR LKQDEGLLKK GTELAFAEFP LTSYSPQKAI ADTTPLQVEE TASHILLYNK HYTAKIDKQT GKWVSFQVKN EELFAPEGLE VNLWRAGTDN DFGAGLPKKL QQLQEADKKA DSVRISVEKL NSGQVKITLR KRLVEGTINY TQELLFDGKP SVTVSNHFKP LKNDKTLTFK IGNHLTLLPF QRIQWYGRGP WESYWDRKTS AMVGLYEGAI VSQYYPYVRP QENGNKTDVR WAKLSKKKGV NIAIYSTGSL LNINALPYSP AQLFPGIEKG QTHAGELTPD KYTHLDIDLQ QLGLGGDNSW GNLPMEQYLL YLYQPYSYSY RIEAF //