ID C2ET62_9LACO Unreviewed; 649 AA.
AC C2ET62;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN Name=lacL {ECO:0000313|EMBL:EEJ40845.1};
GN ORFNames=HMPREF0549_0648 {ECO:0000313|EMBL:EEJ40845.1};
OS Limosilactobacillus vaginalis DSM 5837 = ATCC 49540.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=1423814 {ECO:0000313|EMBL:EEJ40845.1, ECO:0000313|Proteomes:UP000004483};
RN [1] {ECO:0000313|EMBL:EEJ40845.1, ECO:0000313|Proteomes:UP000004483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49540 {ECO:0000313|EMBL:EEJ40845.1,
RC ECO:0000313|Proteomes:UP000004483};
RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL Submitted (JAN-2009) 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 -!- 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:EEJ40845.1}.
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DR EMBL; ACGV01000115; EEJ40845.1; -; Genomic_DNA.
DR RefSeq; WP_003717500.1; NZ_GG693415.1.
DR AlphaFoldDB; C2ET62; -.
DR STRING; 1423814.HMPREF0549_0648; -.
DR PATRIC; fig|1423814.6.peg.499; -.
DR eggNOG; COG3250; Bacteria.
DR HOGENOM; CLU_002346_3_2_9; -.
DR OrthoDB; 9762066at2; -.
DR Proteomes; UP000004483; Unassembled WGS sequence.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; 1.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
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 PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR46323:SF2; BETA-GALACTOSIDASE; 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 PRINTS; PR00132; GLHYDRLASE2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 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 43..227
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 229..331
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 339..646
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
SQ SEQUENCE 649 AA; 76074 MW; E94E54DC92A1612E CRC64;
MEAEIKWLDD PETFRVNQLP AHSDHHFYRN YAEWQRHKSS FEQSLDGQWQ FKFAQTPQER
IKDFYKVDFD ASNFDQIEVP SEIELSDYVQ NNYINTLIPW EGKIYRRPAY ALSQDDPEEG
SFSEGEDNTV GLYLKHFDLN DKLRGKQIRV RFEGVERSMY LWLNGHFIGY AEDSFTPSEF
DLTPYIQDED NVIAVEVFKH STASWIEDQD MFRFSGIFRS VELLAQPVTH LEDFTLKPRV
ADNYRDGELS MDLNLVGEQA GSVHVMVKDH DGTTLMDKTK PIDESVAIEP HEFKDVHLWD
NYDPYLYQLL IEIHDENGNL VELVPYQFGF RRIEISPEHV VLLNGKRLII NGVNRHEWDD
HRGRSVTMKD MLSDIQTFKE NNINAVRTCH YPDQIPWYYL CDQNGIYMMA ENNLESHATW
QKMGAIEPSY NVPGSVPQWK EVVVDRARSN YEYFKNHTAI LFWSLGNESF AGDNLVAMQQ
FYKEHDDSRL VHYEGVCHTH DYSEQIPSLD PANYLPKGGT KDYRDQISDV ESWMYLPPKQ
VEEYLKNNPD KPFMECEYMH DMGNSAGGMG SYIKLLDKYP QYFGGFIWDF IDQALQVKDP
ISGQMVMRYG GDFDDRHSDY EFSGDGLMFA DRTPKPAMQE VRYYYGLHK
//
