ID C7QBZ5_CATAD Unreviewed; 1392 AA.
AC C7QBZ5;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
DE Flags: Precursor;
GN OrderedLocusNames=Caci_3712 {ECO:0000313|EMBL:ACU72614.1};
OS Catenulispora acidiphila (strain DSM 44928 / JCM 14897 / NBRC 102108 / NRRL
OS B-24433 / ID139908).
OC Bacteria; Actinomycetota; Actinomycetes; Catenulisporales;
OC Catenulisporaceae; Catenulispora.
OX NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU72614.1, ECO:0000313|Proteomes:UP000000851};
RN [1] {ECO:0000313|EMBL:ACU72614.1, ECO:0000313|Proteomes:UP000000851}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44928 / JCM 14897 / NBRC 102108 / NRRL B-24433 / ID139908
RC {ECO:0000313|Proteomes:UP000000851};
RX PubMed=21304647; DOI=10.4056/sigs.17259;
RA Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S., Chen F.,
RA Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., Mikhailova N.,
RA Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Chain P.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Chertkov O., Brettin T.,
RA Detter J.C., Han C., Ali Z., Tindall B.J., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT 139908).";
RL Stand. Genomic Sci. 1:119-125(2009).
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
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DR EMBL; CP001700; ACU72614.1; -; Genomic_DNA.
DR STRING; 479433.Caci_3712; -.
DR CAZy; CBM51; Carbohydrate-Binding Module Family 51.
DR CAZy; GH35; Glycoside Hydrolase Family 35.
DR KEGG; cai:Caci_3712; -.
DR eggNOG; COG1874; Bacteria.
DR HOGENOM; CLU_005732_2_0_11; -.
DR InParanoid; C7QBZ5; -.
DR Proteomes; UP000000851; Chromosome.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.102.20.10; Beta-galactosidase, domain 2; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 3.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.120.1060; NPCBM/NEW2 domain; 1.
DR InterPro; IPR018905; A-galactase_NEW3.
DR InterPro; IPR018954; Betagal_dom2.
DR InterPro; IPR037110; Betagal_dom2_sf.
DR InterPro; IPR025972; BetaGal_dom3.
DR InterPro; IPR036833; BetaGal_dom3_sf.
DR InterPro; IPR025300; BetaGal_jelly_roll_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR InterPro; IPR013222; Glyco_hyd_98_carb-bd.
DR InterPro; IPR001944; Glycoside_Hdrlase_35.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR038637; NPCBM_sf.
DR PANTHER; PTHR23421:SF165; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR Pfam; PF13364; BetaGal_ABD2; 2.
DR Pfam; PF10435; BetaGal_dom2; 1.
DR Pfam; PF13363; BetaGal_dom3; 1.
DR Pfam; PF01301; Glyco_hydro_35; 1.
DR Pfam; PF08305; NPCBM; 1.
DR Pfam; PF10633; NPCBM_assoc; 1.
DR PRINTS; PR00742; GLHYDRLASE35.
DR SMART; SM01029; BetaGal_dom2; 1.
DR SMART; SM00776; NPCBM; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF117100; Beta-galactosidase LacA, domain 3; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 3.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 2.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:ACU72614.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ACU72614.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000851};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 563..721
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000259|SMART:SM01029"
FT DOMAIN 1246..1391
FT /note="Glycosyl hydrolase family 98 putative carbohydrate-
FT binding module"
FT /evidence="ECO:0000259|SMART:SM00776"
SQ SEQUENCE 1392 AA; 145968 MW; 1E9285349C16C8E3 CRC64;
MRLRVHSVTR LRHGGRVVAA ATAVMALIFG SVAGAHASPV QGRDVAQSRD VAAATAPASV
GTAHTVTYDG YSFLVDGSRT YLWSGEFHYF RLPSPSLWLD IFQKMKAAGF NATSLYFDWG
YHSPAPGVYD FTGVRDVDEL LDMAQQAGLY VIARPAPYIN AEVDGGGLPA WLGTKDVKNR
TDDPAFLSYA DQWLTQIDAI LARHQLTNGT GSVIAYQVEN EYYNGSATGR AYMQHLEDKA
RADGITVPLT GNNNGTFGSG TGALDVDGPD SYPQGFNCSN PSAWNGVPDI SYDHPAGKPL
YTPEFQGGAF DPWGGPGYDK CAQLINDQFA DVFYKNNIAV GATAQSFYMT YGGTNWGWLG
EPENYTSYDY GAAIRETRQL DPKYSEDKLI GDALASMPDL TKTDPIQTTA PDDAAIVDTA
RRNPDTGAQF HVLRHSDSTS TAVDNTHIAV DFNALPAGNY TYDDVDPVLQ YTGAWSHVAN
QSYTGSDFKN TESFSNTAND SLTVPFTGTA IRWIGSKTNN HGYADVYLDG VKQTTVDCSG
SQSQAVLYQA SGLTAGPHTL KIVVDGTHAS GSTDNFVSVD AVDLPPAGSG AGPTYPSVPQ
EPGTAITLNG RESDLLVADT KIGDSRLQYS TSQLMTSQTI GSRDVAVFYG DKGTDGETVL
RYASRPTVQS TDGAVKVTWD AASGDLRLNY QHSGLTRVTI TGSGSRPLLL LLADKPTAET
FWTQNTATGP VLVRGTHLLR TAASADGGRV LNLTGDNGTD PGIEVFTSAT SVTWNGHAVH
AKGSATGSLV GTVSTAAAIT LPALTDWKYQ AESPEAQSGF DDSTWTVADK TSTNSVTGVG
SLPVLYADDY GFHTGSTWYR GRFRSSPTAT GIHLVSDSGG GAQAFSVWLN GTFLGSSTNG
SGDFTFPAGS LKQSGDNIVS VLTVNMGHEE DYNSTNNSTS ARGLTSASLV GAPLTSVTWR
LQGVRGGEQE IDPVRGPLST GGLYGERAGW PLPGFDDSAW KPVSLPAHDT TPGVAWYRTT
ANLNLPKGQD TSLGLTITDD PSKKYRAELY VNGWMVGNYV NYLGPQHSFP IPNGILKTDG
SNTIAIAVWN LDGSTGGLGT VSLTDYGSYA SSLKVDTVDS PRYNKATYAM PAAPGVNVNL
QVPDTAQAGT AFTATATVSV PAGRGRASGL TPSLSLPPGW TASAPSPATI SSVKDGQSAT
FTWSVQPSAG AQPSAAALTA TIGYTQHDKP GTAKDERVVG YYVPPAAGQD NISDLAFTAA
TNGWGPVERD MSNGEQAAGD GHTITINGAT SAKGLGTNAT SDVRIYLGGH CTTFTASVGV
DDETNGAGTV TFSVLADGRT LTTTPVIGGH QAATQLSADL TGAQMLDLVV GDGGDGNAHD
HGDWGGAQIT CS
//
