ID A0A1H8FI37_9BACT Unreviewed; 602 AA.
AC A0A1H8FI37;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Beta-galactosidase {ECO:0000256|RuleBase:RU000675};
DE EC=3.2.1.23 {ECO:0000256|RuleBase:RU000675};
GN ORFNames=SAMN04488505_109207 {ECO:0000313|EMBL:SEN31306.1};
OS Chitinophaga rupis.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=573321 {ECO:0000313|EMBL:SEN31306.1, ECO:0000313|Proteomes:UP000198984};
RN [1] {ECO:0000313|EMBL:SEN31306.1, ECO:0000313|Proteomes:UP000198984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21039 {ECO:0000313|EMBL:SEN31306.1,
RC ECO:0000313|Proteomes:UP000198984};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOBB01000009; SEN31306.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8FI37; -.
DR STRING; 573321.SAMN04488505_109207; -.
DR OrthoDB; 703126at2; -.
DR Proteomes; UP000198984; 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; 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:UP000198984};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..602
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011553964"
FT DOMAIN 34..349
FT /note="Glycoside hydrolase 35 catalytic"
FT /evidence="ECO:0000259|Pfam:PF01301"
FT DOMAIN 391..501
FT /note="Beta-galactosidase 1-like first all-beta"
FT /evidence="ECO:0000259|Pfam:PF21317"
FT DOMAIN 524..580
FT /note="Beta-galactosidase galactose-binding"
FT /evidence="ECO:0000259|Pfam:PF21467"
FT ACT_SITE 183
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
FT ACT_SITE 258
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
SQ SEQUENCE 602 AA; 67510 MW; 64AC2020213DAC7E CRC64;
MRTLLLSHLL LLACVVMQGA YAQDKHSFEF SKTEFLLDGK PFQIISGEMH PARIPKEYWK
HRIQMAKAMG CNTIAAYVFW NYHEQEPGTF DFSSTNHNIA EFIQMVQQEG MWVLLRPGPY
VCAEWEFGGL PPYLLRTPDI KVRCLDPRYM QAVERYVAAL SAQVKPLLAA NGGPILMVQI
ENEYGSFGND KAYLNRLKEL WVQNGITGPF YTADGAAKPN LEAGTVPGAA IGLDPGASEA
DFTATSNLYP DVPIFSSESY PGWLTHWGEQ WARPDKEGIL REVKYLLDNK RSFNLYVIHG
GTNFAYTAGA NSGGKGYEPD LTSYDYDAPI NEQGVATAKY MAFRQMISNH LHKALPRIPA
PIPTISFPAV PMIPFTSVWE QLPEAVHSAQ PQPFEAYAQD YGFMLYRTTL VGHKSGKLTI
TDLHDYATIY LNGEYMGKLD RRLGENSIEI PKSNVKDPVL EILVEGMGRI NFAQQIIDRK
GITDRVTLNG MTLMSWDVFG LPMTEKYIQN LHPTSGTTAK PGQFFKGTFK LSRVGDTYID
FTQLKKGLIW VNGHNLGRYW DIGPQTRLYC PASWLKKGNN EIVVFDLHQT APASVSGART
LE
//