ID A0A2A9EJG1_9MICO Unreviewed; 801 AA.
AC A0A2A9EJG1;
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=Trehalose/maltose hydrolase-like predicted phosphorylase {ECO:0000313|EMBL:PFG39217.1};
GN ORFNames=ATJ97_1715 {ECO:0000313|EMBL:PFG39217.1};
OS Georgenia soli.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Bogoriellaceae;
OC Georgenia.
OX NCBI_TaxID=638953 {ECO:0000313|EMBL:PFG39217.1, ECO:0000313|Proteomes:UP000222106};
RN [1] {ECO:0000313|EMBL:PFG39217.1, ECO:0000313|Proteomes:UP000222106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21838 {ECO:0000313|EMBL:PFG39217.1,
RC ECO:0000313|Proteomes:UP000222106};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (OCT-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:PFG39217.1}.
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DR EMBL; PDJI01000004; PFG39217.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A9EJG1; -.
DR OrthoDB; 9816160at2; -.
DR Proteomes; UP000222106; 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:PFG39217.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000222106}.
FT DOMAIN 16..271
FT /note="Glycoside hydrolase family 65 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03636"
FT DOMAIN 328..679
FT /note="Glycoside hydrolase family 65 central catalytic"
FT /evidence="ECO:0000259|Pfam:PF03632"
FT DOMAIN 689..752
FT /note="Glycoside hydrolase family 65 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03633"
FT REGION 761..801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..778
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 489
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036289-50"
FT BINDING 362..363
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036289-51"
FT BINDING 592..593
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036289-51"
SQ SEQUENCE 801 AA; 88141 MW; 3B40679F995C9F63 CRC64;
MKGHADLGRD PWVLCEKELD LEHLGQTESL FALSNGHIGL RGNFDEGEPN VVPGTYVSGV
FEHHPLPYPE GGYGYPEAGQ AIVNVTNGKL IRLLVDDEPF DVRYGKLTKH ERRLDMRTGI
LRREVHWTSP AGRPVRIKSS RLVSFSHRAV AAIAYTVEAE EETRIIVQSG LVANEAGPVP
AEGDDPRVAK ALHSPLVAVS QDVEQRGAVL VHRTAQSELH LAAGMDHDIE CDAQYDLENE
ARADWARTSV VTVLQPGQKL RLVKYVAYGW SGTRTSTALR DQVAAALTSA RYGGWTTLRG
LQEEYLAEFW DAADVEIEGD PVLQQAVRLG LFHVLQAGAR SEGRAIGAKG LTGTGYNGHT
FWDIEGFVLP VLTLTAPEAA AYALRWRAGT LQAARDRART LGLGGATFPW RTIDGAETSA
YWPAGTAAFH INADIVRAFE VYRQVTGDIT LEREGGFAVL VETARLWHSR GHHDSHGGWH
MDGVTGPDEY TAVVDDNVFT NLQAARNLTS AVEACRRNPD LAAEMGVTTA ELAAWEKAAR
NVHIPFDETL GVHEQCSHFT RFAEWEFEPN GHRYPLLLHA PYVQLYRKQV VKQADLVLAM
HWHPQAFTAE EKARNLDYYE RRTVRDSSLS ACTQAVMCAE VGHLDLARDY LHEAALVDLH
DLQQTTEHGV HLASLAGAWI GVVAGFGGLR EDGEVLRLAP ALPSTIKALT FRVRWHGMRL
EVRIGEGEVR CAVAGPAGCR MPLRLYDEDV EVGDDVPLVR PLRTPQPLLP PPTQPPGRAP
RRINGEGGFE VPRALEADHV A
//
