ID A0A2S5X390_9MICO Unreviewed; 833 AA.
AC A0A2S5X390;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Family 65 glycosyl hydrolase {ECO:0000313|EMBL:PPG38551.1};
GN ORFNames=C5C17_14655 {ECO:0000313|EMBL:PPG38551.1};
OS Pseudoclavibacter sp. RFBA6.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Pseudoclavibacter.
OX NCBI_TaxID=2080573 {ECO:0000313|EMBL:PPG38551.1, ECO:0000313|Proteomes:UP000237697};
RN [1] {ECO:0000313|EMBL:PPG38551.1, ECO:0000313|Proteomes:UP000237697}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RFBA6 {ECO:0000313|EMBL:PPG38551.1,
RC ECO:0000313|Proteomes:UP000237697};
RA Davis E.W.II., Tabima J.F., Weisberg A.J., Lopes L.D., Wiseman M.S.,
RA Wiseman M.S., Pupko T., Belcher M.S., Sechler A.J., Tancos M.A.,
RA Schroeder B.K., Murray T.D., Luster D.G., Schneider W.L., Rogers E.,
RA Andreote F.D., Grunwald N.J., Putnam M.L., Chang J.H.;
RT "Bacteriophage NCPPB3778 and a type I-E CRISPR drive the evolution of the
RT US Biological Select Agent, Rathayibacter toxicus.";
RL Submitted (FEB-2018) 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:PPG38551.1}.
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DR EMBL; PSUA01000014; PPG38551.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S5X390; -.
DR Proteomes; UP000237697; Unassembled WGS sequence.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; 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:SF13; GLYCOSYL TRANSFERASE-RELATED; 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 Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000313|EMBL:PPG38551.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000237697}.
FT DOMAIN 23..289
FT /note="Glycoside hydrolase family 65 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03636"
FT DOMAIN 345..707
FT /note="Glycoside hydrolase family 65 central catalytic"
FT /evidence="ECO:0000259|Pfam:PF03632"
FT DOMAIN 717..777
FT /note="Glycoside hydrolase family 65 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03633"
FT ACT_SITE 508
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036289-50"
FT BINDING 379..380
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036289-51"
FT BINDING 620..621
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036289-51"
SQ SEQUENCE 833 AA; 93768 MW; 548D96A6892E7A14 CRC64;
MNLSTEDPLD RHRFPLDEWA LVEHEFDANS QGLVETLFAT GNGYLGLRGN LEESRDGYMY
GTFINGFHET WPIRHAEDAF GFAQVGQTIV NVPDAKIIRL FVDDEPLVIS EADLLSYSRV
LSFKDGVLTR ELDWRTPSGK HVRIRSHRLV SFTDRHYMLL DYEVEMVDRG ASILLSSQII
NRQDGGDEFQ RGKKETEVAF DPRKAESFTD RVLQSRIARE EGLRSMLAYR TTHSGMTIAV
AADHDIITDN EWDATTRVDA DFAETAFRVR AEPGMPVRII KHVAYHTSKS VPTRELADRA
DRTLDRMREI PVDDVYTWQR EWLDDFWDRS DIVIHGHPVY QQATRWNLFQ LAQATARTDG
GGIAAKGVSG SGYGGHYFWD TEVYVLPFLS YTAPNVARNA LRFRHQMLDA ARQRAHEMNQ
KGALFPWRTI NGLESSAYYA AGTAQYHIDA DISHALMQYV SATGDDELLA QGAIDILVET
ARLWADLGFW RTGGDDHFHI HGVTGPDEYT TVVNDNLYTN VMAKANLRAA YTACERLRET
DPASFERLTM RLHLAEEELV EWAAAAEAMY LPFDEKLGIH PQDAQFLEKE LWDLENTPPS
QRPLLLHFHP LVIYRFQVLK QADVVLALLL QGNEFTPEQK RKDFEYYDAL TTGDSSLSAV
VQSIIAAEVG YADLAEHYFS TALFVDIANL HHNTSDGIHI ASTGGIWSAL VYGFGGMRDH
GGKITFDPRL PADWPRLEFH LTLRGSRIRV DLEQELMTFT AETGSGAEVF VRGRRVAIAP
GEPTTVKLGA VRELEGYPTL SDIEGSIRED GSVITASIPT ISVDHAVLDP GLD
//
