ID A0A1C0AQE3_9ACTN Unreviewed; 839 AA.
AC A0A1C0AQE3;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Alpha,alpha-trehalose phosphorylase {ECO:0000313|EMBL:VEP39278.1};
DE SubName: Full=Kojibiose phosphorylase {ECO:0000313|EMBL:OCL36604.1};
GN Name=treP {ECO:0000313|EMBL:VEP39278.1};
GN ORFNames=BCR15_01720 {ECO:0000313|EMBL:OCL36604.1}, TLA_TLA_00698
GN {ECO:0000313|EMBL:VEP39278.1};
OS Tessaracoccus lapidicaptus.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Tessaracoccus.
OX NCBI_TaxID=1427523 {ECO:0000313|EMBL:OCL36604.1, ECO:0000313|Proteomes:UP000093501};
RN [1] {ECO:0000313|EMBL:OCL36604.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IPBSL-7 {ECO:0000313|EMBL:OCL36604.1};
RA Puente-Sanchez F., Arce-Rodriguez A.;
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000093501}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IPBSL-7 {ECO:0000313|Proteomes:UP000093501};
RA Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:VEP39278.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TLA_E {ECO:0000313|EMBL:VEP39278.1};
RA Peiro R., Begona, Cbmso G., Lopez M., Gonzalez S., Sacristan E.,
RA Castillo E.;
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|Proteomes:UP000516347}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Peiro R., Begona, Cbmso G., Lopez M., Gonzalez S., Sacristan E.,
RA Castillo E.;
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 65 family.
CC {ECO:0000256|ARBA:ARBA00006768}.
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DR EMBL; MBQD01000011; OCL36604.1; -; Genomic_DNA.
DR EMBL; LR214441; VEP39278.1; -; Genomic_DNA.
DR RefSeq; WP_068751007.1; NZ_MBQD01000011.1.
DR AlphaFoldDB; A0A1C0AQE3; -.
DR Proteomes; UP000093501; Unassembled WGS sequence.
DR Proteomes; UP000516347; Chromosome.
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:UP000093501}.
FT DOMAIN 29..289
FT /note="Glycoside hydrolase family 65 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03636"
FT DOMAIN 345..710
FT /note="Glycoside hydrolase family 65 central catalytic"
FT /evidence="ECO:0000259|Pfam:PF03632"
FT DOMAIN 719..780
FT /note="Glycoside hydrolase family 65 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03633"
FT ACT_SITE 510
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 622..623
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036289-51"
SQ SEQUENCE 839 AA; 93281 MW; 7A835CE885D437A5 CRC64;
MIRDITGDPM DRDRFPVDTW RLVETEPGED HGLTETLFAV ANGHIGIRGT TEEGRPSHSP
GTFVNGFHET WPIKHAEEAY GFARTGQTIV NVPDTTLLKV YVDDEPFVIS VADLQSYERA
VDFRRGRLTR SLVWRTPAGK RVRIRSSRMV SFTDRHVVLH ELEVTVLSGG GAPVVVNSLI
VNRQDGYTDY RRPAAAGEGW DPRRSSAFNG RVLLPQLHWE HDPRMVLTYQ TARSGMTLAV
GADHAVETDN PVEILSSTQE DIGKYVFRVE AAEGVPITVR KAVAIHTSRG VPAEELSDRC
RRTLDRVRDK GFEYYHAEQE AWLDTFWRDS DVVIDGDPAV QQAVRWCLFQ LAQAAARSDQ
LGIAAKGVTG SGYEGQYFWD TEIYVVPFLI YTSPRVARNV LRFRVNLLPR ARERAAVLSQ
RGALFPWRTI SGEEASAYYA AGTAQYHIDA DVAYAFAKYG DLTGDTGFMH RDGVEVLIET
ARMWADLGFW RQDADGTDQF HIHGVTGPDE YTTVVNNNMF TNVMARANLR AAATLVREMA
TADAEVYRRL AARLNLDPAE VDEWEACADG MVVLFDETFG IHPQDAQFLA SELWDLENTP
DENRPLLLHY HPLVIYRFQV LKQADVVLAL FLQGDQFTPA QKRADFEYYD PITTGDSTLS
GVVQSVVAAE VGYQDMAMRY FLSGLFVDLA DLHGNARDGV HIASTGGVWT ALVYGFGGLR
DHGGRITFDP RLPDQWDSLR FPLQIRGSRV RVHLERTAIT FEIEVGEPVA VSVRGQDVTV
EPGTPLRVPL DGQGPRLASL HGRHPVLGAN REDGSIVRAV VPGAQAQDPD GPTVLGGPL
//
