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Database: UniProt
Entry: A8UJF6_9FLAO
LinkDB: A8UJF6_9FLAO
Original site: A8UJF6_9FLAO 
ID   A8UJF6_9FLAO            Unreviewed;       768 AA.
AC   A8UJF6;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=Trehalose/maltose hydrolase (Phosphorylase) {ECO:0000313|EMBL:EDP71280.1};
GN   ORFNames=FBALC1_02312 {ECO:0000313|EMBL:EDP71280.1};
OS   Flavobacteriales bacterium ALC-1.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales.
OX   NCBI_TaxID=391603 {ECO:0000313|EMBL:EDP71280.1, ECO:0000313|Proteomes:UP000003630};
RN   [1] {ECO:0000313|EMBL:EDP71280.1, ECO:0000313|Proteomes:UP000003630}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ALC-1 {ECO:0000313|EMBL:EDP71280.1,
RC   ECO:0000313|Proteomes:UP000003630};
RA   Azam F., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (OCT-2007) 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:EDP71280.1}.
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DR   EMBL; ABHI01000002; EDP71280.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8UJF6; -.
DR   STRING; 391603.FBALC1_02312; -.
DR   eggNOG; COG1554; Bacteria.
DR   OrthoDB; 9758855at2; -.
DR   Proteomes; UP000003630; Unassembled WGS sequence.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; 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:SF14; MALTOSE PHOSPHORYLASE; 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   Hydrolase {ECO:0000313|EMBL:EDP71280.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003630}.
FT   DOMAIN          15..267
FT                   /note="Glycoside hydrolase family 65 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03636"
FT   DOMAIN          324..690
FT                   /note="Glycoside hydrolase family 65 central catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF03632"
FT   DOMAIN          699..759
FT                   /note="Glycoside hydrolase family 65 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03633"
FT   ACT_SITE        490
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036289-50"
FT   BINDING         359..360
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036289-51"
FT   BINDING         602..603
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036289-51"
SQ   SEQUENCE   768 AA;  89032 MW;  72AD6980A5090617 CRC64;
     MNLDYIIPDS WSIIEEGFDT NNVKASESLF SIGNGAMGQR ANFEEQYSGP TFQGSYIAGV
     YYPDKTRVGW WKNGYPEYFA KVLNAPNWIG INVFINDEAL DLYTCKKVES FKRELNMKEG
     WLSRSFVATL KNDIKVEVDT KRFLSLDIDE LGAIEYNVKP LNSDASITYR PYIDSGITNE
     DTNWDDKFWD TLNVSHENNQ AFIQAKTMKT DFYTCTFMES QVFIDGKSVI IEPNIKADAN
     YASFSYNYRV KQNETYTIHK FGGYTVDRNH RNNELVSAAK SVLSKATKTG FSTLLDSQKK
     AWAKIWDMAD ITIDGDVKAQ QGIRFNIFHL NQTYLGTDAQ LNIGPKGFTG EKYGGSTYWD
     TEAYCIPFYM ATKDQSVARN LLTYRYKHLE KAIENAEKLG FKNGATLYPM VTMNGEECHN
     EWEITFEEIH RNGAIAFAIF NYYRYTGDFS YIPEMGLEVL IGVARFWHQR ATFSTDKNKY
     VILGVTGPNE YENNINNNWY TNYIAQWCIN YAIESIEKVR EGYEDDYRRI SGKTKISHEE
     LALWKKVADH MYFPYSEKHN VYLQQDGFLD KELITVADLD KSQRPINQKW SWDRILRSPY
     IKQADILQGM YFFEDQFTTE ELARHFDFYE PFTVHESSLS PCVHSIQAAK LDRMEQAYEF
     YLRTSRLDLD DYNHEVHEGL HITSMAGTWM SIVEGFGGMR VENDTLTFEP KIPEQWEAYS
     FKVNFRNQIL KVSVNQNETH FELEGNNELS IEVNGIEVTI SPDNLVTV
//
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