ID A0A1M7NDZ9_9ACTN Unreviewed; 786 AA.
AC A0A1M7NDZ9;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Alpha,alpha-trehalose phosphorylase {ECO:0000313|EMBL:SHN01889.1};
GN ORFNames=SAMN05216499_11880 {ECO:0000313|EMBL:SHN01889.1};
OS Actinacidiphila paucisporea.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Actinacidiphila.
OX NCBI_TaxID=310782 {ECO:0000313|EMBL:SHN01889.1, ECO:0000313|Proteomes:UP000184111};
RN [1] {ECO:0000313|EMBL:SHN01889.1, ECO:0000313|Proteomes:UP000184111}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.2025 {ECO:0000313|EMBL:SHN01889.1,
RC ECO:0000313|Proteomes:UP000184111};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 65 family.
CC {ECO:0000256|ARBA:ARBA00006768}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FRBI01000018; SHN01889.1; -; Genomic_DNA.
DR RefSeq; WP_073501097.1; NZ_FRBI01000018.1.
DR AlphaFoldDB; A0A1M7NDZ9; -.
DR STRING; 310782.SAMN05216499_11880; -.
DR OrthoDB; 9816160at2; -.
DR Proteomes; UP000184111; 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:UP000184111}.
FT DOMAIN 18..270
FT /note="Glycoside hydrolase family 65 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03636"
FT DOMAIN 327..680
FT /note="Glycoside hydrolase family 65 central catalytic"
FT /evidence="ECO:0000259|Pfam:PF03632"
FT DOMAIN 689..751
FT /note="Glycoside hydrolase family 65 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03633"
FT REGION 763..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 488
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036289-50"
FT BINDING 361..362
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 786 AA; 86934 MW; 908DDD1473D3DA71 CRC64;
MITDPAFEVS PWSLRECELN LDLLPQSESV FALSNGHIGW RGNLDEGEPN GLPGTYLNGL
YELHPLPYAE AGFGYPESGQ TVINVTNGKL IRLLVDDEPF DLRYGTIRRH ERELDLRAGV
LHRVCEWVSP AGRAVRVTST RMVSFQQRAV AAIAYEIEPL DGEVRVVVQS ELAANEDVPH
AAGDPRVSAA LDSPLLAEEH YASGTRLRLV HSTTRSRLRV AVAADHRIDG PDSTQVSAES
DDDVSRLTVT SVVEAGQRLR LEKFVAYGWS AARSLPALRD QADAALVGAR DTGWQGLLDQ
QRAYLDDFWE RADVEVDGDT EIQQAVRFAL FHVLQVGARA EERAIPAKGL TGSGYDGHSF
WDAETFVLPL LGFTSPHAAA EVLRWRYNML PVAQERARQL GLAGATFPWR TINGDEASGY
WPAGTAAFHI NADIADAVVR YVAITGDQVF ERDTGLELLV ETARLWRSLG HHDHAGAFHI
DGVTGPDEYS AVSDDNAFTN LMAQANLTAA ADAAERHPRH AAALGVSDEE TAAWRDAAAA
MALPFDEDFG VHEQSKGYCR RQIWDFEGTD PDHYPLMLYY PYFDLYRKQV VKQADLVLAM
YLRGDAFTHE QKARNFAYYE PLTVRDSSLS AYCQSVIAAE VGHLQLAYDY LGETAMIDLE
DLENNARDGL HIAALAGTWT ALVAGFGGMR LIDGDGIRFA PRLPDALSRI AFRLLFRGRR
LRVEVDRKTA TYTLAAGEPL EILHYDEPFT LTADRPVVHQ LPHVAHQPSP PQPPGRAPLR
RPQHLT
//