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Database: UniProt
Entry: E8RVA1_ASTEC
LinkDB: E8RVA1_ASTEC
Original site: E8RVA1_ASTEC 
ID   E8RVA1_ASTEC            Unreviewed;       808 AA.
AC   E8RVA1;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=Beta-galactosidase {ECO:0000313|EMBL:ADU15242.1};
DE            EC=3.2.1.23 {ECO:0000313|EMBL:ADU15242.1};
GN   OrderedLocusNames=Astex_3614 {ECO:0000313|EMBL:ADU15242.1};
OS   Asticcacaulis excentricus (strain ATCC 15261 / DSM 4724 / KCTC 12464 /
OS   NCIMB 9791 / VKM B-1370 / CB 48).
OG   Plasmid pASTEX01 {ECO:0000313|EMBL:ADU15242.1,
OG   ECO:0000313|Proteomes:UP000001492}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Asticcacaulis.
OX   NCBI_TaxID=573065 {ECO:0000313|EMBL:ADU15242.1, ECO:0000313|Proteomes:UP000001492};
RN   [1] {ECO:0000313|Proteomes:UP000001492}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15261 / DSM 4724 / KCTC 12464 / NCIMB 9791 / VKM B-1370 /
RC   CB 48 {ECO:0000313|Proteomes:UP000001492};
RC   PLASMID=pASTEX01 {ECO:0000313|Proteomes:UP000001492};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Teshima H., Davenport K., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA   Brun Y.V., Woyke T.;
RT   "Complete sequence of plasmid 1 of Asticcacaulis excentricus CB 48.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007401}.
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DR   EMBL; CP002397; ADU15242.1; -; Genomic_DNA.
DR   AlphaFoldDB; E8RVA1; -.
DR   KEGG; aex:Astex_3614; -.
DR   eggNOG; COG3250; Bacteria.
DR   HOGENOM; CLU_006501_0_1_5; -.
DR   Proteomes; UP000001492; Plasmid pASTEX01.
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; IPR048230; GalA-like.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
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   NCBIfam; NF041462; GalA; 1.
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; 2.
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   PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:ADU15242.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ADU15242.1};
KW   Plasmid {ECO:0000313|EMBL:ADU15242.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001492};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..808
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003230143"
FT   DOMAIN          82..222
FT                   /note="Glycosyl hydrolases family 2 sugar binding"
FT                   /evidence="ECO:0000259|Pfam:PF02837"
FT   DOMAIN          233..332
FT                   /note="Glycoside hydrolase family 2 immunoglobulin-like
FT                   beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF00703"
FT   DOMAIN          340..417
FT                   /note="Glycoside hydrolase family 2 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF02836"
FT   DOMAIN          423..585
FT                   /note="Glycoside hydrolase family 2 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF02836"
FT   DOMAIN          632..688
FT                   /note="DUF4982"
FT                   /evidence="ECO:0000259|Pfam:PF16355"
FT   DOMAIN          704..804
FT                   /note="Glycoside hydrolase family 2"
FT                   /evidence="ECO:0000259|Pfam:PF18565"
SQ   SEQUENCE   808 AA;  90777 MW;  0D663D0D57828757 CRC64;
     MASLPVLGMA TTLTPAATAA PEPNSPRQRL RLEDDWRFHF GHAEDLERDF GFGANQRTLA
     KQGRSGAKPD AADYDDSTWR PVILPHDWAV ELPFVNNEDY RRNPADKDDE DYAAAHGYKP
     IGRKFPETSV GWYRRLITLD KADAARCLWL EFDGVFRDAT IIFNGYVLER HDSGYTSFSV
     DISDFINTDD TPNVLLVRVD ASYGEGWFYE GAGIYRHVWL VKADPVHVPQ WGVFVRPKTN
     GMVEASVDLV NRSDARRVTT LDVTALDRDG TAVATTRQTV ELAAQSRATR EVRLTLPQPR
     LWSIESPYLY TLRVEVTTEA TRDLYTLRFG LRDLRFDAQE GFFLNGKPLK IKGTNNHQDH
     AGVGAAIPDA LQVWRLKQLK SLGSNAYRTS HNPPTPELLD ACDELGLLVI DEARQMTSSR
     QGLSELEALI RRDRNHPSVI LWSIGNEEPQ QMTARGLKVA KSMARRIREL DPTRKVNAAM
     NKGFGDGITT ALDVIGFNYH EAQIEPFRTR FPDMPIIGTE TASAVSTRGE YKTDAKRQVV
     AAFDTEHPYW GATAESWWSL YNSKPYLLGG FIWTGFDYRG EPTPFNWWPS VASNFGVFDS
     CGFPKDVYHY YRAWWQDEPV LHLLPHWNWS EGETVSVWAY SNCDEVELSL NSKSLGRQTM
     RRDSHLEWTV PFTPGTLTAY GYKRGKVVMK TERKTAGAPH RLILSADRMQ LSADGQDVAM
     VSVSAVDKVG TPVPLADDLI QFALTGPSRL IGVGNGNPNS HESDKAPYRR LFNGYAQAIV
     QTTKTSGRFT FQARAEGLTA ASLTFTSR
//
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