ID A0A1H3VI66_9BACT Unreviewed; 1039 AA.
AC A0A1H3VI66;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN ORFNames=SAMN05192529_101157 {ECO:0000313|EMBL:SDZ74459.1};
OS Arachidicoccus rhizosphaerae.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Arachidicoccus.
OX NCBI_TaxID=551991 {ECO:0000313|EMBL:SDZ74459.1, ECO:0000313|Proteomes:UP000199041};
RN [1] {ECO:0000313|EMBL:SDZ74459.1, ECO:0000313|Proteomes:UP000199041}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Vu-144 {ECO:0000313|EMBL:SDZ74459.1,
RC ECO:0000313|Proteomes:UP000199041};
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|ARBA:ARBA00001412};
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}.
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DR EMBL; FNQY01000001; SDZ74459.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3VI66; -.
DR STRING; 551991.SAMN05192529_101157; -.
DR Proteomes; UP000199041; Unassembled WGS sequence.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
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; 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; 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; 2.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 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};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000199041}.
FT DOMAIN 31..194
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 283..332
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 334..584
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
SQ SEQUENCE 1039 AA; 116728 MW; 334B899EB148D128 CRC64;
MRKWLLICLI FGQVSLLKAQ YYPVRDKIQC TSLNGTWKIK IFPGQQVPDS LKGWQQNSFN
DKHWQQVQVP GNWETVINQL KAPEYGKDLG DFTGLYRRTF AYNPVWDNKH LILRFDGVNF
SYTVFVNGKK VGCWGSSYNL AQFDITPFLN KTDDNVLSVQ VSTRSLPSQP KNTWQFDTND
DWSLSGISRD VTLFALNNIY LGGIDFKADI LNPNEARVDL KIDLGRFKGS DRSVLNDSSL
NLVASLVDPL GNHILDFNRF LSAGEIFNQK SSGAPVGETK ENTALPSISF SGLIKNPRLW
TAETPQLYSL EVKLRDKNGR VLQQSNQCVG LRSVKVEGYK LMVNNQQVHL RGVCLSEIDP
KNGRAIAFSA RLKELKMMKS AGINFIRTAH YPFAPEFYDL CDQLGFYICD EVPFGYGDKN
LSDTAYLPEL ITRARSTITR DRNHPSVIVW SIGNENPYTP VVEKVIQYVK ALDSSRPRGL
PQRGSDYLRY QGKQSPNVDI YMPHYLDVAA LNESLIKTDK PLILTEYAHS LGLAMDEFEE
QYANIYKQPK IIGGSVWCWK DQALLTDGKD KIKGSIKQLE KGADNSMPQL STVEQGVWID
QTHYMDNFGN NGADGIVYGN LYPQEDYYLV RKVYSPVQIL TDQLEAVFGQ ENEFGIEIAN
RFDFKTLHGY QLCWQLVRPD TVLNEGRLWL TEAAQQTGRE KISVALPQII AMQKALRPFD
YSLHLKIIAP DGSQISEKNL LLVKPDYRQL LAGEMPVSPV RVTVSNKGIL KVQNSHKVLL
ETPLMMRVGR KLTITSENQT LKDHFNWNPY ILSPKVTQYK KQKTDSGVIY TLECVWTSES
ENPSNIDSSG RGIQGTVRVF VNSRNLVDIR YDVTPFSNAT GNLLECGLTV QAGSNYHTFH
WIGAGPFSSS IGKTAYNERG VYALDKNDIR FNGNRSKVDL AAISASDGVT LGLYPGNGQL
GVENKNGNIL ISQNAIITGY GSKFKAPKGR LKISDIKSIK GGLTIALSIP EAPVDLINGI
FHPQEPVNPE NPFKESYGW
//
