ID A0A1Q5XK34_9BACL Unreviewed; 883 AA.
AC A0A1Q5XK34;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Endo-beta-N-acetylglucosaminidase {ECO:0000313|EMBL:OKP94268.1};
GN ORFNames=A3849_29835 {ECO:0000313|EMBL:OKP94268.1};
OS Paenibacillus sp. P46E.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1349436 {ECO:0000313|EMBL:OKP94268.1, ECO:0000313|Proteomes:UP000185715};
RN [1] {ECO:0000313|EMBL:OKP94268.1, ECO:0000313|Proteomes:UP000185715}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P46E {ECO:0000313|EMBL:OKP94268.1,
RC ECO:0000313|Proteomes:UP000185715};
RA Ploux O.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}.
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:OKP94268.1}.
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DR EMBL; LVYZ01000099; OKP94268.1; -; Genomic_DNA.
DR RefSeq; WP_074114801.1; NZ_LVYZ01000099.1.
DR AlphaFoldDB; A0A1Q5XK34; -.
DR OrthoDB; 1089471at2; -.
DR Proteomes; UP000185715; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0033925; F:mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR CDD; cd06547; GH85_ENGase; 1.
DR CDD; cd00146; PKD; 1.
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; 2.
DR InterPro; IPR032979; ENGase.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR005201; Glyco_hydro_85.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR000601; PKD_dom.
DR InterPro; IPR035986; PKD_dom_sf.
DR PANTHER; PTHR13246:SF1; CYTOSOLIC ENDO-BETA-N-ACETYLGLUCOSAMINIDASE; 1.
DR PANTHER; PTHR13246; ENDO BETA N-ACETYLGLUCOSAMINIDASE; 1.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF03644; Glyco_hydro_85; 1.
DR Pfam; PF18911; PKD_4; 1.
DR SMART; SM00089; PKD; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF49299; PKD domain; 1.
DR PROSITE; PS50022; FA58C_3; 1.
DR PROSITE; PS50093; PKD; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..883
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012231482"
FT DOMAIN 657..737
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 736..883
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
SQ SEQUENCE 883 AA; 96492 MW; 679D41C67907F426 CRC64;
MKKIGAGFIF LVVICAALST SALAKQPYSS YWFPEQLLQW SPASDPDAAF NRSTIPLQDR
FVGAGVNSHA TKAPKVMALS AMNPGTSGVP SQGSDKFGAN TFTYWQYVDQ LVYWGGSAGE
GIIVPPSADT IDAAHKNGVP ILGTVFFPPA VYGGKYEWVK EMLEQKSDGS FPAADKLIQV
AEYYGFDGWF INQETEGGTP ADAQQMKAFL SYLESHQTAS LHTVWYDSMT KEGSISWQNA
LNDKNAMFLQ DNGKQISDSM FLNFWWKDLG SSAEKAKSLG RSPFALYAGI DVEAKGYDTK
VNWNLLFPEG KPAVTSLGIY RPDWAFNSAE SMEDFFIREN KFWVGPNGNP GNTASNQTWK
GIANDVVEAS PVNKLPFITS FNTGSGQKYY VHGKQVRDKG WNNRSLQDIL PTWRWIADSK
GTPLTPVLDW SDAYYGGSSL KVSGVLSHDN ATHLKLYKTD LKIEASTKLS VTYKTQNKPS
LKVGLAFADQ PDQFVFLNVK DKTSPGWTTE TLNLTPYKGK RIVALSLYFD TRDTISDYAI
HIGQLAIQNA NDSIQPLPAV SELKATSSDF RNGIYGDARL QWNPLDQQVK QYEIYRVLPD
GNEVLMGATP NHVFYVPEMR RIDKEAVTVL KVVAVNGRYG QGQASSVKIS WPAYPKPTAD
FKAGRTLVAP GESVNFTDLS TEVTEGWSWT FDGGSPAVST TKNPVVMFNQ EGVYSVTLTA
TNSSGQDTMS KKALITVSKE AGSVKNLALG KSVTADQACG DKEGAPNAVD GKVTDNSKWC
ALGNLPHWLQ VDLGAEHPIS AFVIKHAESG GEWSGFNTSD YTIQVSSDGT NWTDAVKVQG
NTAAETTEAI ALVKARYVKL IITKPSQGAD TAARIYEFEV KGL
//