ID A0A0N1FU88_9ACTN Unreviewed; 1032 AA.
AC A0A0N1FU88;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Beta-galactosidase {ECO:0000313|EMBL:KPI06284.1};
DE EC=3.2.1.23 {ECO:0000313|EMBL:KPI06284.1};
GN ORFNames=OK006_6429 {ECO:0000313|EMBL:KPI06284.1};
OS Actinobacteria bacterium OK006.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1592326 {ECO:0000313|EMBL:KPI06284.1, ECO:0000313|Proteomes:UP000037912};
RN [1] {ECO:0000313|EMBL:KPI06284.1, ECO:0000313|Proteomes:UP000037912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK006 {ECO:0000313|EMBL:KPI06284.1,
RC ECO:0000313|Proteomes:UP000037912};
RA Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT "Draft genome sequences for four Actinobacteria strains OK006 OK074 OV450
RT and OV320.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPI06284.1}.
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DR EMBL; LJCU01000231; KPI06284.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1FU88; -.
DR PATRIC; fig|1592326.3.peg.7858; -.
DR Proteomes; UP000037912; 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 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; IPR040605; Glyco_hydro2_dom5.
DR InterPro; IPR006101; Glyco_hydro_2.
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 InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR42732; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR42732:SF1; BETA-MANNOSIDASE; 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; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:KPI06284.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KPI06284.1}.
FT DOMAIN 47..203
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 213..316
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 323..477
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 648..744
FT /note="DUF4982"
FT /evidence="ECO:0000259|Pfam:PF16355"
FT DOMAIN 757..858
FT /note="Glycoside hydrolase family 2"
FT /evidence="ECO:0000259|Pfam:PF18565"
FT REGION 530..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 862..894
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1032 AA; 111977 MW; 937924A9B0A87030 CRC64;
MSVTRRSVLI AGTAAPAAGS LLGAADAWAD SPGRAAGRRL VELRDGWRFA LVNPGGITDP
TGAYEGAAQP GYDDSAWREV SVPHDWSIEQ TPTTEHGTTS GTGFFPGGLG WYRTTFTLPP
ALAGRRISVE FDGVYMDSHV YCNGEEVGRH PYGYTGFGLD LTGLLHTDGT TENVIAVKVQ
NQLPSSRWYS GSGIYREARL VVTEPVHVQR WGTYVTTPDI TAERAVVRVR TTVVNESGAA
AEVQVISRIV DPDGRTAART STRVAVADRA DETHELTVAK PRLWDFATPD HRYTLETELR
VGDARVDTCR TPFGIRTFRF DPDEGFHLNG VHAKIKGVDL HHDQGALGAA ISVDAVRRQM
TIMKSMGVNA FRTSHNPPSP QMIQVCEELG IVMMVEAFDC WRTGKTRYDY GRFFDEWCEQ
DATEMVLAAR NSPAVVLWSI GNEIPDSTST PGLAMADRII AAIKAADDTR PLVIGSDKYR
RVPTKGSAAD LMLAKLDGLG LNYNTAQSVD ALHAAYPHLF LFESESSSET STRSTYQEPQ
HLNTGENHTP GRRAVSSYDN NLASWTMSGE YGHKKDRDRK WFAGEFLWSG IDYIGEPTPY
DVFPVKASFF GAVDTAGFPK DMYHLFRSQW VSEPMVHLVP MTWNHEAGDT VEVWAYANVD
TVELFLNGKS LGTRRFDTKT TTDGRTYLET TEATGDDKTF ASGPYPGSYT SPNGSAGKLH
LTWEVPYAPG ELKAVARRDG RTVATDVLRT AGAPHTIRLT PDRTSLAADG RSLLFVTAEV
VDARGVVVPD AEHLIAFDID GGSLAGLDNG REESAERYQA STRTAFHGKA LAIVRSGTRP
GSLKVTARSE GVRGATLTVR TTSARAKATT PPAVFRPDPG PGVPNDPLAD ASYSGRPDTL
PAAMLDGDAA TDWSNAFYKS ATALLPAFSG ARPEDWVSVT WARPRAVDRV EVSFTVDATH
TLPASVEVAV WDGKRYVPVK GTAVDWATAS DTPTVITFDG VRGSRLRLLM ASGHPGAVEG
GLRISRLEVP VV
//
