ID A0A0Q7BWD7_9ACTN Unreviewed; 861 AA.
AC A0A0Q7BWD7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Kojibiose phosphorylase {ECO:0000313|EMBL:KQW53728.1};
GN ORFNames=ASC77_05560 {ECO:0000313|EMBL:KQW53728.1};
OS Nocardioides sp. Root1257.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736439 {ECO:0000313|EMBL:KQW53728.1, ECO:0000313|Proteomes:UP000051939};
RN [1] {ECO:0000313|EMBL:KQW53728.1, ECO:0000313|Proteomes:UP000051939}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1257 {ECO:0000313|EMBL:KQW53728.1,
RC ECO:0000313|Proteomes:UP000051939};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQW53728.1, ECO:0000313|Proteomes:UP000051939}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1257 {ECO:0000313|EMBL:KQW53728.1,
RC ECO:0000313|Proteomes:UP000051939};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQW53728.1}.
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DR EMBL; LMDV01000001; KQW53728.1; -; Genomic_DNA.
DR RefSeq; WP_056149566.1; NZ_LMDV01000001.1.
DR AlphaFoldDB; A0A0Q7BWD7; -.
DR STRING; 1736439.ASC77_05560; -.
DR OrthoDB; 9816160at2; -.
DR Proteomes; UP000051939; 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:0000256|ARBA:ARBA00023295};
KW Reference proteome {ECO:0000313|Proteomes:UP000051939}.
FT DOMAIN 27..293
FT /note="Glycoside hydrolase family 65 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03636"
FT DOMAIN 353..715
FT /note="Glycoside hydrolase family 65 central catalytic"
FT /evidence="ECO:0000259|Pfam:PF03632"
FT DOMAIN 725..787
FT /note="Glycoside hydrolase family 65 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03633"
FT REGION 831..861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 516
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036289-50"
FT BINDING 387..388
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036289-51"
FT BINDING 628..629
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036289-51"
SQ SEQUENCE 861 AA; 96082 MW; E35BF5F09AFF3513 CRC64;
MKAHARSVGP NPMDRGRFPI DEWALVETSY RADDIGVAET LFTVANGYLG MRGNPEEGRP
SYAHGTFVNG FHETWPIRHA EAAFGFARTG QTIVNAPDTK VLKIYVDDEP LTFGTSDLEH
YERRLDFRDG VLHRSLIWRT PSGKRVRIDS TRMVSMTQRH LAVMTLEIEV LTGDAPVVVS
SQILNRQDGI DEYKAPQEHT GETVDPRKAA AFAGRVLVPR MSYATDDRML LGYQCANSGM
TIAVAADHVL ETADKHEVLA RHDDDQVKMV FRVDATQGSP MRITKTVSYH TSRGVPVREL
ADRCDRTLDR ARQHGLEHYR EDQRGWYADF WAAADVEVEG ASADHRAVQQ AVRFNLFSLA
QASGRTDGLG VPAKGVTGSG YEGHYFWDTE VYVIPFLSYT QPEVARNALH FRSVMLPSAR
DRAREMAQSG AMFPWRTING EEASAYYAAG SAQVHIDADI AYALMKYVRA TGDRGFLVRE
GIDILVETAR MWADLGFWRS NGEPSFHIHG VTGPDEYTTV VNNNLFTNVM ARYNLELAAD
AVEWIRDERP EEHMRVTTRL DLDPAEVEEW RRCAEGMAIP YDAGLGIHPQ DDFFLDREVW
DLSQTPPETR PLLLHYHPLV IYRFQVLKQA DVVLALFLQG DRFTAEEKRA DFEYYDPITT
GDSTLSAVVQ SVIAAEVGYH EAALHYFHES LYVDLMNLHG NTVDGLHIAS AGGVWSALVH
GFGGMRDHGG ALAFDPRLPA SWAALRYRLC WQGSRVLVEL TEDEVRFTVV DGDKDVPLLV
RGRSYVVGQD HPLVVPLADQ GERIDGLLGD HPVVGGVRAD GSTITAGVPD PIQHPDEGEQ
HTGEFPVYQD VPPLGPHIPQ S
//
