ID Q7MVX8_PORGI Unreviewed; 1017 AA.
AC Q7MVX8;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2003, sequence version 1.
DT 27-MAR-2024, entry version 118.
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=lacZ-2 {ECO:0000313|EMBL:AAQ66038.1};
GN OrderedLocusNames=PG_0896 {ECO:0000313|EMBL:AAQ66038.1};
OS Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=242619 {ECO:0000313|EMBL:AAQ66038.1, ECO:0000313|Proteomes:UP000000588};
RN [1] {ECO:0000313|EMBL:AAQ66038.1, ECO:0000313|Proteomes:UP000000588}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-308 / W83 {ECO:0000313|Proteomes:UP000000588};
RX PubMed=12949112; DOI=10.1128/JB.185.18.5591-5601.2003;
RA Nelson K., Fleishmann R., DeBoy R., Paulsen I., Fouts D., Eisen J.,
RA Daugherty S., Dodson R., Durkin A., Gwinn M., Haft D., Kolonay J.,
RA Nelson W., White O., Mason T., Tallon L., Gray J., Granger D., Tettelin H.,
RA Dong H., Galvin J., Duncan M., Dewhirst F., Fraser C.;
RT "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT gingivalis strain W83.";
RL J. Bacteriol. 185:5591-5601(2003).
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 -!- SIMILARITY: Belongs to the peptidase C25 family.
CC {ECO:0000256|ARBA:ARBA00006067}.
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DR EMBL; AE015924; AAQ66038.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7MVX8; -.
DR STRING; 242619.PG_0896; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR EnsemblBacteria; AAQ66038; AAQ66038; PG_0896.
DR KEGG; pgi:PG_0896; -.
DR eggNOG; COG3250; Bacteria.
DR HOGENOM; CLU_002346_0_2_10; -.
DR Proteomes; UP000000588; 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:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000000588};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT DOMAIN 750..1015
FT /note="Beta galactosidase small chain/"
FT /evidence="ECO:0000259|SMART:SM01038"
SQ SEQUENCE 1017 AA; 116232 MW; 27889268554676E5 CRC64;
MFGENKEDGH ATFMPYATTA LLQADERYQK PWLTPSQAEF LSLNGLWYFR YFPDARTART
DFVEDLFDVS AWDTITVPSC WQMKGWDTPL YINVNHIFED NPPFIRIQKT YTSAVDPNPT
GSYRRDFILP TGWEKKRVYL HFDGLYSGAY VWINGRYIGY TQGGNNDAEF DISAAVRAGQ
NNVSIQVVRW TDASYLEGQD MFHMSGLHRD VYLYATPRTS IRDHYITSKL HPESDYTTGE
ISVAVEMDNR DGSAARKTVG IRLLDPQGKV LWEERKQTRL SVGEQKQSLH FRKADLRNLS
LWTAETPTLY TLIITQWDDK EREELAFATK YGFRQPEIRD QSVYLNGRKV LFKGVNTQDT
HPLHGRSIDL PTMVKDITMM KQANVNTLRT SHYPRQPKMY ALCDYYGLYV MDEADLECHK
NWDDHGEKGG ITNAESWRAQ YVDRTVRMVC RDRNHPSVLF WSLGNESGGG ENFRHTYAAV
RALDSRIIHY EGATRGGTEY TDLHSVMYPS LAQVQAGSNG RETDGKPYFM CEYAHAMGNG
VGNLQDYWDI MEQSSAGIGG CIWDWVDQAI YDPSEIKRGL YRLHTGYDYP GPHQGNFVNN
GLVTADRSWT PKLYEVKKVY QYVKFDAYDS KSKLLTLHNA YSFTDLNRFG LRFKLLSDGC
VIESGEVDLP KLPAGEKATL RIPVADIPMY STRDFHIDFE LFLREATTWS DKGYTVASEQ
FTLAQREGFA SLLPERMPTL QVTTEGNHLH IANDRVQLVF DLHTAELICW NYGSHPVIIP
RGGPVYDNFR WVENDSPYGS IPPGAPAGPV QPAVPSYEVN ADSTRVILAA SHRALCPYRL
NYYIYGDGTV DIRADFTPEE EHADKLRRLG IKMCLPLQMD RIEYLARGPH ENYVDRRQSA
FFGLYSDRVS RMVEPYVRPQ STGNRTGLRA LTLTDDSGRG IRVEASGQVD FSILPYEDEH
LARTRHQWEL PMPAHHILRF DYMQRGLGNG SCGPGTAPTY LCPSSGTYSF ELRFRPL
//
