ID A4FGJ9_SACEN Unreviewed; 611 AA.
AC A4FGJ9;
DT 17-APR-2007, integrated into UniProtKB/TrEMBL.
DT 17-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Glycoside hydrolase family 2, sugar binding {ECO:0000313|EMBL:CAM03174.1};
DE SubName: Full=Glycosyl hydrolase family 2 {ECO:0000313|EMBL:PFG96878.1};
GN OrderedLocusNames=SACE_3903 {ECO:0000313|EMBL:CAM03174.1};
GN ORFNames=A8924_4290 {ECO:0000313|EMBL:PFG96878.1};
OS Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 /
OS NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharopolyspora.
OX NCBI_TaxID=405948 {ECO:0000313|EMBL:CAM03174.1, ECO:0000313|Proteomes:UP000006728};
RN [1] {ECO:0000313|EMBL:CAM03174.1, ECO:0000313|Proteomes:UP000006728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 /
RC NRRL 2338 {ECO:0000313|Proteomes:UP000006728}, and NRRL 2338
RC {ECO:0000313|EMBL:CAM03174.1};
RX PubMed=17369815; DOI=10.1038/nbt1297;
RA Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S.,
RA Haydock S.F., Leadlay P.F.;
RT "Complete genome sequence of the erythromycin-producing bacterium
RT Saccharopolyspora erythraea NRRL23338.";
RL Nat. Biotechnol. 25:447-453(2007).
RN [2] {ECO:0000313|EMBL:PFG96878.1, ECO:0000313|Proteomes:UP000225825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40517 {ECO:0000313|EMBL:PFG96878.1,
RC ECO:0000313|Proteomes:UP000225825};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (SEP-2017) 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; AM420293; CAM03174.1; -; Genomic_DNA.
DR EMBL; PDBV01000001; PFG96878.1; -; Genomic_DNA.
DR RefSeq; WP_009944848.1; NZ_PDBV01000001.1.
DR AlphaFoldDB; A4FGJ9; -.
DR STRING; 405948.SACE_3903; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR KEGG; sen:SACE_3903; -.
DR eggNOG; COG3250; Bacteria.
DR HOGENOM; CLU_009935_3_1_11; -.
DR OrthoDB; 9762066at2; -.
DR Proteomes; UP000006728; Chromosome.
DR Proteomes; UP000225825; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
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; 1.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
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 PANTHER; PTHR42732; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR42732:SF2; BETA-MANNOSIDASE; 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 SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CAM03174.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006728};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..611
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038282854"
FT DOMAIN 98..178
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 219..313
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 356..477
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
SQ SEQUENCE 611 AA; 66444 MW; 934D0180EDCC0E3A CRC64;
MRPYPSASRR LTVILTAGLA LTGFAALAGA DIAWEPQEAP LTTPWTAEVG PDNALPEYPR
PQLVRQRWQN LNGTWEYAGG AEPPGTPAER ILVPYPPESA LSGIQRHDDH MLYRRTFTVP
AEWSGQRVLL HFGAVDQRAE VRVNGTSVAI HEGGYTSFSA DVTDALVPGG QQELVVVAQD
RNDAAPYPVG KQRNKPGGIL YTGASGIWQT VWMEPVPEVH IGKLDVTPDV ATGTFAVRAR
TGNSDAQAEV VVGEPGGQEV ARQSGAAGGE LRVAVPNARL WSPSDPFLYD LRVRLLGTGG
QVLDEVTSYA GMRSVGLVND EQGRPRIALN GRILFQHGPL DQGYWPDGIY TAPTDEALRF
DIEAAQRLGF NMIRKHVKVE PARWYYWADR LGMLVWQDMP SLPIDLADPP GSNPPPSEEA
EAHFRTELAE MIDQLRSTTS IVAWVPFNEG WGEFDTAAVA EQVAQADPTR LVDASSGVNC
CYSLPDSGAG HIYDDHTYVG PGKPAVVAPR ASVDGEYGGL GLVEQGHLWP GPPQAYEMTE
SREHLTRRYS EVSTALADVV RASGLSAAVY TQTTDVENEV NGFFTYDRRV LKPDLAIVRD
RNLEVIDAGT P
//
