ID F0R9D7_CELLC Unreviewed; 823 AA.
AC F0R9D7;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 61.
DE SubName: Full=Beta-galactosidase {ECO:0000313|EMBL:ADY28259.1};
DE EC=3.2.1.23 {ECO:0000313|EMBL:ADY28259.1};
GN OrderedLocusNames=Celly_0424 {ECO:0000313|EMBL:ADY28259.1};
OS Cellulophaga lytica (strain ATCC 23178 / DSM 7489 / JCM 8516 / NBRC 14961 /
OS NCIMB 1423 / VKM B-1433 / Cy l20).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Cellulophaga.
OX NCBI_TaxID=867900 {ECO:0000313|EMBL:ADY28259.1, ECO:0000313|Proteomes:UP000007487};
RN [1] {ECO:0000313|EMBL:ADY28259.1, ECO:0000313|Proteomes:UP000007487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23178 / DSM 7489 / JCM 8516 / NBRC 14961 / NCIMB 1423 /
RC VKM B-1433 / Cy l20 {ECO:0000313|Proteomes:UP000007487};
RX PubMed=21677859; DOI=10.4056/sigs.1774329;
RA Pati A., Abt B., Teshima H., Nolan M., Lapidus A., Lucas S., Hammon N.,
RA Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA Liolios K., Pagani I., Mavromatis K., Ovchinikova G., Chen A.,
RA Palaniappan K., Land M., Hauser L., Jeffries C.D., Detter J.C.,
RA Brambilla E.M., Kannan K.P., Rohde M., Spring S., Goker M., Woyke T.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P., Ivanova N.;
RT "Complete genome sequence of Cellulophaga lytica type strain (LIM- 21).";
RL Stand. Genomic Sci. 4:221-232(2011).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
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DR EMBL; CP002534; ADY28259.1; -; Genomic_DNA.
DR RefSeq; WP_013620007.1; NC_015167.1.
DR AlphaFoldDB; F0R9D7; -.
DR STRING; 867900.Celly_0424; -.
DR KEGG; cly:Celly_0424; -.
DR eggNOG; COG3250; Bacteria.
DR HOGENOM; CLU_006501_0_1_10; -.
DR OMA; CLHHDQG; -.
DR OrthoDB; 9801077at2; -.
DR Proteomes; UP000007487; 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; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR032311; DUF4982.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR048229; GalB-like.
DR InterPro; IPR040605; Glyco_hydro2_dom5.
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 InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR NCBIfam; NF041463; GalB; 1.
DR PANTHER; PTHR42732; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR42732:SF1; BETA-GALACTOSIDASE (EUROFUNG); 1.
DR Pfam; PF16355; DUF4982; 1.
DR Pfam; PF18565; Glyco_hydro2_C5; 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; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 1.
DR PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:ADY28259.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ADY28259.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007487};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..823
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003259222"
FT DOMAIN 51..177
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 190..293
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 295..453
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 628..704
FT /note="DUF4982"
FT /evidence="ECO:0000259|Pfam:PF16355"
FT DOMAIN 717..819
FT /note="Glycoside hydrolase family 2"
FT /evidence="ECO:0000259|Pfam:PF18565"
SQ SEQUENCE 823 AA; 93236 MW; 1ABA1F19896FAF2C CRC64;
MQTYKLTALL LFLMFFSSCQ EKEIEVLADQ DFNKNWLFIK DSIPNAEAIT IDDSNWRKVN
VPHDWAIEGP FSDKNNARNG GLPIDGIAWY RKHFTVDAKN KNKQISIEFD GVMDNSKVYI
NGNFVGERHY GYSGFEYDLT PFIKFGENNV IAVQLAPEIL SERWYPGAGI YRKVRLKLNE
PIHIPQWGTY ITTPKVASNK AVVSVETKLK NTLNTTENIV LETTILDINN TTVAVSSNKI
ELAKASEQKE VQKITVPNPI LWDIGKPNLY TAVSRVIKDN KTIDEYTTEF GIRTIEFKKE
GFYLNGKAVE LNGVCMHHDL GPLGAAVNYR ATERQMQIMQ QMGANALRTS HNPPSTEMLQ
VCDRLGIVVI DEAFDEWKEA KVPNGYHKYF DKWAEKDLRD MIKRDRNHPS VIMWSIGNEI
LEQGKKDGWK IAKMLNDICH NEDNTRPTTA GFNYYPASFK NKLAYQIDVV GVNYKPAYYA
EIREQNPDMI FYGSETSSQT STRGYYEFPL KERVSKETNQ VSSYDVNIGP SWTYPPEVEF
EAQKQNPHSL GEFIWTGFDY LGEPTPYGGR DNSTNGYWND DWPSHASYFA PVDLVGFPKD
RFYLYQSQWT TEPMVHVLPH WNWEGKEGQN IPVYSYTNCD EVELFVNGKS YGKKIKGKDT
TTIFAEYNGF KGGTIDSKYR LSWNVPYQPG SLKVVGYKNG KPVATKEIKT AGKPYKIKLI
ADRTTINASG EDLSFITVRV EDKDGNLCPK ANHLINFKVS GNGNLEAVGN GNSASLESFQ
ANYITSFYGK SLAILKATEN PGEITLTATA DNLTSATITI KTK
//