ID G8NWF7_GRAMM Unreviewed; 627 AA.
AC G8NWF7;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
DE Flags: Precursor;
GN OrderedLocusNames=AciX8_3463 {ECO:0000313|EMBL:AEU37760.1};
OS Granulicella mallensis (strain ATCC BAA-1857 / DSM 23137 / MP5ACTX8).
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Granulicella.
OX NCBI_TaxID=682795 {ECO:0000313|EMBL:AEU37760.1, ECO:0000313|Proteomes:UP000007113};
RN [1] {ECO:0000313|EMBL:AEU37760.1, ECO:0000313|Proteomes:UP000007113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1857 / DSM 23137 / MP5ACTX8
RC {ECO:0000313|Proteomes:UP000007113};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Rawat S., Mannisto M.,
RA Haggblom M., Woyke T.;
RT "Complete sequence of Granulicella mallensis MP5ACTX8.";
RL Submitted (NOV-2011) 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|RuleBase:RU000675};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
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DR EMBL; CP003130; AEU37760.1; -; Genomic_DNA.
DR RefSeq; WP_014266634.1; NC_016631.1.
DR AlphaFoldDB; G8NWF7; -.
DR STRING; 682795.AciX8_3463; -.
DR KEGG; gma:AciX8_3463; -.
DR eggNOG; COG1874; Bacteria.
DR HOGENOM; CLU_007853_7_2_0; -.
DR OrthoDB; 9813184at2; -.
DR Proteomes; UP000007113; Chromosome.
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; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR026283; B-gal_1-like.
DR InterPro; IPR048912; BetaGal1-like_ABD1.
DR InterPro; IPR048913; BetaGal_gal-bd.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR InterPro; IPR019801; Glyco_hydro_35_CS.
DR InterPro; IPR001944; Glycoside_Hdrlase_35.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR23421:SF165; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR Pfam; PF21317; BetaGal_ABD_1; 1.
DR Pfam; PF21467; BetaGal_gal-bd; 1.
DR Pfam; PF01301; Glyco_hydro_35; 1.
DR PIRSF; PIRSF006336; B-gal; 1.
DR PRINTS; PR00742; GLHYDRLASE35.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000675};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000675};
KW Reference proteome {ECO:0000313|Proteomes:UP000007113}.
FT DOMAIN 46..360
FT /note="Glycoside hydrolase 35 catalytic"
FT /evidence="ECO:0000259|Pfam:PF01301"
FT DOMAIN 402..512
FT /note="Beta-galactosidase 1-like first all-beta"
FT /evidence="ECO:0000259|Pfam:PF21317"
FT DOMAIN 529..587
FT /note="Beta-galactosidase galactose-binding"
FT /evidence="ECO:0000259|Pfam:PF21467"
FT ACT_SITE 193
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
FT ACT_SITE 269
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
SQ SEQUENCE 627 AA; 70052 MW; 46475D7639EFFFDA CRC64;
MKNFSPAKKY FHKFLAITLL PLLSGAVRGQ VATASAAPLT VGTSGFLLKD KPFRIVSGEL
EYARIPRPYW RDRLRKAHAM GLNAITIYVF WNIHEPTPEV YDFSGQNDVA EFVREAQQEG
LYVILRPGPY VCAEWDLGGY PAWLLKDHEM KLRSLQPEFK AAATRWMLRL GQELTPLQAS
RGGPILAVQV ENEYGSFGDD HEYMKWVHEL VLQAGFGGSL LYTGDGADVL KQGTLPSVFA
GIDFGTGDAA RSIKLYKAFR PQTPVYVAEY WDGWFDHWGE KHQLTDAAKQ ETEIRSMLEQ
GDSISLYMVH GGTSFGWMNG ANNDHDGYQP DVSSYDYDAP LDESGRPRPK YFRLRNIINE
ITNQTPIPVP DSPPLITVPA IHLDEAQSLW NTLPKAIESE APLSMEDVDQ SYGYILYRTK
INGLGTGQLT FNELHSYARI YVDGKLAGVL DRRLGQKSLP LQITGTHRLD ILVENSGRIN
FKPIIRTERA GALGQISFKG AALNHWSIYP LPFAPPPEKG YKKNVCTGPC FYHAEFSTPN
PGDTFLNTEQ LVKGVVWVNG HLLGRFWDIG PAGALYVPGV WLHQGKNELT VFDLNGGRNL
QIEGQDHATY FEPKPESVTP VNTAPKP
//
