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Database: UniProt
Entry: A0A1H8FI37_9BACT
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Original site: A0A1H8FI37_9BACT 
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
//
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