ID A0A1H5NJM0_9ACTN Unreviewed; 1395 AA.
AC A0A1H5NJM0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
GN ORFNames=SAMN05216489_09578 {ECO:0000313|EMBL:SEF01071.1};
OS Streptomyces sp. 3213.3.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1855348 {ECO:0000313|EMBL:SEF01071.1, ECO:0000313|Proteomes:UP000198754};
RN [1] {ECO:0000313|EMBL:SEF01071.1, ECO:0000313|Proteomes:UP000198754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3213 {ECO:0000313|EMBL:SEF01071.1,
RC ECO:0000313|Proteomes:UP000198754};
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
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DR EMBL; FNTK01000001; SEF01071.1; -; Genomic_DNA.
DR STRING; 1855348.SAMN05216489_09578; -.
DR Proteomes; UP000198754; 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; 2.60.390.10; Beta-galactosidase, domain 3; 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; 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 InterPro; IPR006311; TAT_signal.
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; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000198754};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..1395
FT /note="beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038480251"
FT DOMAIN 565..723
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000259|SMART:SM01029"
FT DOMAIN 1249..1394
FT /note="Glycosyl hydrolase family 98 putative carbohydrate-
FT binding module"
FT /evidence="ECO:0000259|SMART:SM00776"
FT REGION 1374..1395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1395 AA; 148479 MW; FFA2CBDF0E104864 CRC64;
MRGSRNGSEG ARPGRRRWWR AVLATAATIA LAAGMTAPAT AVAQDIGEQT PAVGPDAADT
PQAHTVTLDG YSFLVDGKRT YLWSGEFHYF RLPSQDLWRD IFQKMKAAGF NSTSLYFDWG
YHSPKPGVYD FTGVRDVDKL LDMAQEAGLY VIARPAPYIN AEVDGGGLPG WLSTKAGNNR
SDDPQFLKYA DEWLTQIDRI IARHQLTNGT GSVIAYQVEN EYYNGSAAGR SYMQHLEDKA
RADGITVPLT GNNNGTFNFG TGALDVDGPD SYPQGFNCSN PAKWNGVPDI SYDHPAGKPL
YSPEFQGGAF DPWGGPGYDK CAQLINDQFA NVFYKQNIAV GATAQSFYMT YGGTNWGWLG
MPQNYTSYDY GAAIRETRQL DPKYYEDKLI GYFTQSVAPL TKTEAIRTTP PDDSAVVDTA
RMNPDTKTQF HVLRHGNSTS TAVDKTHISL DFNAVPSADT TYTWDDPDSA LQYAGSWSHV
ADTSYTGGDY KHTESFSKTA GDSLTVPFDG TAIRWIGSKT NNHGNADVYL DGTKVATVDD
SGSESQAVLF QKTGLTPGAH TLKIVVAGSH SSGSTDNYVA IDAIDVPTSD SAAEPTYPVV
PQQPGTAITL DGRDSHVIVA NYRLGDAQLQ YSTSEIMTDA TIGNRDVAVL YGDEDSDGET
VLRYATEPTV TANGGAVATS WDPSTGDLRL NYTHKGLIRI SISGDGKRPL LLLVGDKATA
ETFWRQDTAS GPVLVRGTHL LRTATSLRGG RTVALTGDNA DDKNIEVFTS AAQVTWNGRV
LGTHATDTGS LTGKIPVAAP VNLPALTNWK HAEESPEAAS GFDDTSWQVA DKATTNSVSG
VNSLPVLYAD DYGFHTGNTW YRGRFRATGK ETGIHLVSDS GGDAQAFSVW LNGTFLGSST
TGSGDFAFPA DALKSQGDNV ISVLTVNMGH EEDYNSTNGN KAARGLTSAS LVGAPLTSVT
WRLQGVRGGE DLQDTVRGPL STGGLYGERA GWSLPGYPDA DWNRVTLPTT DTTPGVSWYR
TDAKLDLPHG QDTSVGLTFT DAPARKYRAT IFVNGWQVGN YVNYLGPQHT FPVPNGILNP
NGHNSIAIAV WNLDGRTGGL GQVSLTDYGS YASSLRVAQN DSPRYDARTY AMPKRPGADV
TLDVPDTAQP GQAFTARTTV RVPKDGRPAS GLTASLAAPD GWSVSATSPE SVERLRPGTS
ATFTWQVRPP AGTLPSASAL TSTVHYRRNG RQAVGGDERI VRGIPPAPPA GQSDVSALPF
LSSTNGWGPV ERDTSVGEQA AGDGRPITIA GVGYAKGLGT NSVSDVELYL AGQCSRLTAY
VGVDDETNGA GTVTFSVIAD GKTLVTTPTI HGKQAAVPID VDVSGAQVLD LKVGDAGDGN
GNDHGDWGSP TLTCE
//
