ID A0A268DZS9_9BACI Unreviewed; 1137 AA.
AC A0A268DZS9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Glycoside hydrolase family 2 {ECO:0000313|EMBL:PAD66372.1};
GN ORFNames=CHH83_24425 {ECO:0000313|EMBL:PAD66372.1};
OS Bacillus sp. 7586-K.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2021690 {ECO:0000313|EMBL:PAD66372.1, ECO:0000313|Proteomes:UP000216230};
RN [1] {ECO:0000313|EMBL:PAD66372.1, ECO:0000313|Proteomes:UP000216230}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7586-K {ECO:0000313|EMBL:PAD66372.1,
RC ECO:0000313|Proteomes:UP000216230};
RA Kalinowski J., Ahrens B., Al-Dilaimi A., Winkler A., Wibberg D.,
RA Schleenbecker U., Ruckert C., Wolfel R., Grass G.;
RT "Isolation and whole genome analysis of endospore-forming bacteria from
RT heroin.";
RL Submitted (JUL-2017) 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:PAD66372.1}.
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DR EMBL; NPCL01000144; PAD66372.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A268DZS9; -.
DR OrthoDB; 9762066at2; -.
DR Proteomes; UP000216230; 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 CDD; cd04084; CBM6_xylanase-like; 1.
DR Gene3D; 2.60.40.1080; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 3.
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; 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 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 PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:PAD66372.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000216230}.
FT DOMAIN 24..137
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 149..248
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 256..401
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 574..636
FT /note="DUF4982"
FT /evidence="ECO:0000259|Pfam:PF16355"
FT DOMAIN 649..750
FT /note="Glycoside hydrolase family 2"
FT /evidence="ECO:0000259|Pfam:PF18565"
SQ SEQUENCE 1137 AA; 129207 MW; AC44B26D76B61EBF CRC64;
MNKKILFNDG WEFAKSSLEV TEHSSLNFQQ VDLPHDWLIY NTLDLYENSI GWYRKTFTRP
KAASQVLLSF DGVYMDSSVY VNQQFVEERK YGYSSFEHDI TDALKEGDNE VLVKVVFQSP
NSRWYSGAGI YRNVWLKTRE ESHIVTDGIY VHTKQEDSRF QVEIDTELNV TEELVLTHTI
VADDKVIATI SDTLPPNQSK KLVNQQTLII ENPLLWSPEQ PNLYKLITKL ETEGGRVLEL
ISQNLGFRKI VLDPNEGMLL NGQKMKLNGV CEHHDLGALG AAFNEAALKR RFKLLKEMGV
NAIRTAHNMP AVELMDLADE MGFFIVSEAF DMWERPKTKY DYARFFKEWA ESDVKSWVLR
DRNHPSLLMW SIGNEIYDTH ADERGQEITK LLKEYVEKYD PKGNASVTIG SNYMPWENAQ
KCADIVKLAG YNYAEKYYQK HHDEHPDWII YGSETASVVQ SRGIYHFPFE KAILTDDDEQ
CSALGNSTTS WGAKSAEACI LAERDTPFSL GQFIWTGFDY IGEPTPYHTK NSYFGQLDTA
TFKKDSFYLY QAAWTNYKEN PMIHIFPYWD FNDGQLIDVR VCSNAPRIEL QLNGETIGAY
DIDHSRGKEL VGWWKVPYQA GELQAIAYDE AGNVIAKDMK KSFGNAKRLK VQADKEQLIA
NGTDLIFVEI SMEDMNGHLV ENATNRVFVN VTGAGRLVGL DNGDSTDYDQ YKGQSRRLFS
GKLMAIIAAT VEPGFIQIEV SSQGIESCKA EYKALPSGES IEGISAMMSN QPLPIVLGTE
EEIPLRKIEL ISEHGQLIDE TRKEINVRAH LYPENTSYKE VEWSVVNDSG IVSNIAKVEA
NGFKAKVSAF GDGEFRLRCT SKNGGDKTRL ISQLEFKATG LGTAYKNPYE FISAGLYDYS
KGEIGSGNER GVATSRDGET QVGFKNIDFG LYGSDTITIP IFALTDEEYS LQIWQGMPGE
NGSELLADVI YQKESKWNVY QEETYRLKKR LTGISSICFV LRSKVHIKGF SFKKYNRAFE
QNRAIDCDHI YGDTFTKTEN NVEGIGNNVS LEYEQMDFTI EGATKLVVSG RSPIDKNTIH
IRFANENGES NQLVEFTQSD GYVERVYDLE KITGEQKVTF IFLPGSQFDF AWFRFER
//
