ID E4SCU7_CALK2 Unreviewed; 1026 AA.
AC E4SCU7;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00013303, 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=Calkro_0164 {ECO:0000313|EMBL:ADQ45080.1};
OS Caldicellulosiruptor kronotskyensis (strain DSM 18902 / VKM B-2412 / 2002).
OC Bacteria; Bacillota; Clostridia; Caldicellulosiruptorales;
OC Caldicellulosiruptoraceae; Caldicellulosiruptor.
OX NCBI_TaxID=632348 {ECO:0000313|EMBL:ADQ45080.1, ECO:0000313|Proteomes:UP000006835};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=2002;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA Blumer-Schuette S.E., Kelly R.M., Woyke T.;
RT "Complete sequence of Caldicellulosiruptor kronotskyensis 2002.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADQ45080.1, ECO:0000313|Proteomes:UP000006835}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18902 / VKM B-2412 / 2002
RC {ECO:0000313|Proteomes:UP000006835};
RX PubMed=21216991; DOI=10.1128/JB.01515-10;
RA Blumer-Schuette S.E., Ozdemir I., Mistry D., Lucas S., Lapidus A.,
RA Cheng J.F., Goodwin L.A., Pitluck S., Land M.L., Hauser L.J., Woyke T.,
RA Mikhailova N., Pati A., Kyrpides N.C., Ivanova N., Detter J.C.,
RA Walston-Davenport K., Han S., Adams M.W., Kelly R.M.;
RT "Complete genome sequences for the anaerobic, extremely thermophilic plant
RT biomass-degrading bacteria Caldicellulosiruptor hydrothermalis,
RT Caldicellulosiruptor kristjanssonii, Caldicellulosiruptor kronotskyensis,
RT Caldicellulosiruptor owensenis, and Caldicellulosiruptor lactoaceticus.";
RL J. Bacteriol. 193:1483-1484(2011).
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 ---------------------------------------------------------------------------
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; CP002330; ADQ45080.1; -; Genomic_DNA.
DR RefSeq; WP_013429237.1; NC_014720.1.
DR AlphaFoldDB; E4SCU7; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR KEGG; ckn:Calkro_0164; -.
DR PATRIC; fig|632348.3.peg.171; -.
DR HOGENOM; CLU_002346_0_2_9; -.
DR OrthoDB; 9762066at2; -.
DR Proteomes; UP000006835; 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 Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361154};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361154}.
FT DOMAIN 744..1013
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1026 AA; 118631 MW; 546D6AC5B565853E CRC64;
MLDKSFYQNP KIQHVNMAQP RSSFVPYASV ENALLGDWEL SEYLRLLNGS WYFKLFDMPC
KVDQEIIKSD AKFTGFEKII VPSNFQLFGY DKPIYTNTRY PIPVDPPYVP DINPTGVYKK
EIFISKEDKE KRIFLVFEGV DCAFYLYVNQ EFAGFSKVSH MMHEFDITDL LTEGKNIITV
AVLKYADSTY LEDQDKWRMS GIFRDVYLLV RPKIYLKDIY LKPELNDNLT KGSLVAEIEI
SNSNEEKSEF YVDVQIYADK ELLKSASKLA SILPKTTEQF RVEFQIEKPL LWSAETPNLY
KFIVIIKDTS GKILEVIPQN FGFRKIEIKD GVFYLNNVPI KLKGVNRHDM HPRVGFAVTR
KMMQEDITLM KQHNINCVRT SHYPNHPYFL ELCDKFGIYV IDEADLETHG FGAVGDWGLL
AKDPMWEDAF LERAKMMVMR DKNHPSIIMW SLGNESGYGP NHDKMAQWIR SYDNSRPIHY
ESARDAEVVD IVSVMYPPVE KLEEEGKKQE KRPFFMCEYA HAMGNGPGNL KEYWDVIYKY
PRLLGGCVWE WADHGILTKT PDGKEYYAYG GDFGDEPNDG NFCIDGLLFP DRTPSPGMIE
LKKVYEPVMI ELLDKKSGIF RVTNRYDFIS LNHIEVEWEL LLGGRVVKEG FVDVSDVLPH
SSKEVEIDEV KEVLKSCKEE LFITFTAKLK NSMPWAKRGF VLTKSQIAIN EETSQDAVQK
IEKINAILSK QDRFEVCKLS DKLVVFAGNT EVEFCRWTGD LVSLKHSDLE LIKSSPRFNI
WRAPTDNDVH IKNEWIKAGF DKLQRRIVNV SFEEHSEYFK VQTTSVYGAY SVKPVFEVTT
SYKVFKSGIV ETNVYAQALR QLPPLPKIGL QFMMPKEFEY VKYYGRGPHE NYPDIKQSAT
VEIYDMAIKD MYVPYIMPQE YGNRCDVRWA FVYNIYGIGL CIRGIPTFNF SAREYTDDVL
TKAKHSYELT KADGIVVNVD FKIGGIGSQS CGPGPLEKYL VKDDKFEFCF YMIPVDSNSL
DVEKLW
//
