ID A0A242A1W0_9ENTE Unreviewed; 875 AA.
AC A0A242A1W0;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Glycosyl hydrolase {ECO:0008006|Google:ProtNLM};
GN ORFNames=A5886_000072 {ECO:0000313|EMBL:OTN75028.1};
OS Enterococcus sp. 8G7_MSG3316.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1834191 {ECO:0000313|EMBL:OTN75028.1, ECO:0000313|Proteomes:UP000195043};
RN [1] {ECO:0000313|EMBL:OTN75028.1, ECO:0000313|Proteomes:UP000195043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8G7_MSG3316 {ECO:0000313|EMBL:OTN75028.1,
RC ECO:0000313|Proteomes:UP000195043};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genomic Center for Infectious Diseases;
RA Earl A., Manson A., Schwartman J., Gilmore M., Abouelleil A., Cao P.,
RA Chapman S., Cusick C., Shea T., Young S., Neafsey D., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Enterococcus sp. 8G7_MSG3316.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 65 family.
CC {ECO:0000256|ARBA:ARBA00006768}.
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:OTN75028.1}.
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DR EMBL; NGKU01000001; OTN75028.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A242A1W0; -.
DR STRING; 1834191.A5886_000072; -.
DR OrthoDB; 9758855at2; -.
DR Proteomes; UP000195043; Unassembled WGS sequence.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.70.98.40; Glycoside hydrolase, family 65, N-terminal domain; 1.
DR Gene3D; 2.60.420.10; Maltose phosphorylase, domain 3; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR005194; Glyco_hydro_65_C.
DR InterPro; IPR005195; Glyco_hydro_65_M.
DR InterPro; IPR005196; Glyco_hydro_65_N.
DR InterPro; IPR037018; Glyco_hydro_65_N_sf.
DR InterPro; IPR017045; Malt_Pase/Glycosyl_Hdrlase.
DR PANTHER; PTHR11051; GLYCOSYL HYDROLASE-RELATED; 1.
DR PANTHER; PTHR11051:SF8; PROTEIN-GLUCOSYLGALACTOSYLHYDROXYLYSINE GLUCOSIDASE; 1.
DR Pfam; PF03633; Glyco_hydro_65C; 1.
DR Pfam; PF03632; Glyco_hydro_65m; 1.
DR Pfam; PF03636; Glyco_hydro_65N; 1.
DR PIRSF; PIRSF036289; Glycosyl_hydrolase_malt_phosph; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE 3: Inferred from homology;
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 97..343
FT /note="Glycoside hydrolase family 65 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03636"
FT DOMAIN 398..796
FT /note="Glycoside hydrolase family 65 central catalytic"
FT /evidence="ECO:0000259|Pfam:PF03632"
FT DOMAIN 808..865
FT /note="Glycoside hydrolase family 65 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03633"
FT ACT_SITE 575
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036289-50"
FT BINDING 436..437
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036289-51"
FT BINDING 696..697
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036289-51"
SQ SEQUENCE 875 AA; 99471 MW; 73DC5255A895FFE2 CRC64;
MNIITLSDAQ WLLQEADDKA TSFAGPLLER VQALTSYLKD TQSGGILSET VVFTNEEGTF
SLDQWLTEKL NQPFVCGTKE TFEEKSAAIP WTLEYYGYTP GKDEYSVESL LTVGNGYIGL
RGTTPEMAIS EENYPGLYIA SLYNTAASEV AGHTIHNEDF VNAPNLQKMY IAIDGEVIDI
AHNQIDSFKR TLDLRTGLFQ STVDIETSKQ KRIRIETKKI ANMQDVHQYS IMYTFTPLNF
SGAITLISEA DGAVYNYNVA RYRSLTNQHL QVITTDAEAT KAHLVAETTN SRITVVQSSE
LFADDISLSE MTSDVSESSV KQSLLLSVEE GHTYQFEKTV TVAAYRPDEE QPATTWNELQ
LPRFDAMYQE SQQAWRTLWQ DAAIEVSGDL MSQKMLNLHT YHVLVSASPN AYQESLDASI
TARGLHGEAY RGHIFWDELF ILPFYIVHFP DTAKEILRYR YRRLAAAKAD AKKAGYQGAM
FPWQSGLDGS EQSQELHLNP ISGEWKEDHS RLQRHVSLAI AYNVWQYWHN TKDKQFMADY
GLELMLEIAH FWQSAATWDS QAQRYFIDKV MGPDEFHENY PDSETGGLKN NAYTNMMVVW
LFEEIDHLQA AIDAETFQTI LQKTEMTATD LDTMAAIRTK LGLEIDSEGI IAQFEGYFQL
EDLDWDHYKE TYGNIYRMDR ILNAEGKSAD SYKVAKQADS LMIFYNFSKQ QVNQILTDLD
YELPTDYVEK NLNYYLQRTS HGSTLSRIVH AQLAAMVDNQ ELAWSLYQEA LSSDYRDIQG
GTTAEGIHAG VMAATLFIPL TTFAGIDIRE QLVQITPNLP KAWEALAFSL RVRNVHYQIN
VTHETLTITV DRPETILIKG IEYHLVPNEP QTITY
//
