ID   A0A1G9HZ57_9FIRM        Unreviewed;       791 AA.
AC   A0A1G9HZ57;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Maltose phosphorylase {ECO:0000313|EMBL:SDL18132.1};
GN   ORFNames=SAMN04488692_10269 {ECO:0000313|EMBL:SDL18132.1};
OS   Halarsenatibacter silvermanii.
OC   Bacteria; Bacillota; Clostridia; Halanaerobiales; Halarsenatibacteraceae;
OC   Halarsenatibacter.
OX   NCBI_TaxID=321763 {ECO:0000313|EMBL:SDL18132.1, ECO:0000313|Proteomes:UP000199476};
RN   [1] {ECO:0000313|EMBL:SDL18132.1, ECO:0000313|Proteomes:UP000199476}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SLAS-1 {ECO:0000313|EMBL:SDL18132.1,
RC   ECO:0000313|Proteomes:UP000199476};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FNGO01000002; SDL18132.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9HZ57; -.
DR   STRING; 321763.SAMN04488692_10269; -.
DR   OrthoDB; 9758855at2; -.
DR   Proteomes; UP000199476; Unassembled WGS sequence.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
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   Reference proteome {ECO:0000313|Proteomes:UP000199476}.
FT   DOMAIN          28..283
FT                   /note="Glycoside hydrolase family 65 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03636"
FT   DOMAIN          339..703
FT                   /note="Glycoside hydrolase family 65 central catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF03632"
FT   DOMAIN          715..772
FT                   /note="Glycoside hydrolase family 65 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03633"
FT   ACT_SITE        503
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036289-50"
FT   BINDING         374..375
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036289-51"
FT   BINDING         615..616
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036289-51"
SQ   SEQUENCE   791 AA;  91674 MW;  8AED78D390E58467 CRC64;
     MGSSFEERKD NKNDFEDYFQ IDEWRIVEKG FSPDKNRFAE SVMSLGNGHM GIRGNFEEHY
     SGDSLQGTYI AGVYYPDKTV VGWWKIGYPE YYAKVPNAAD FIGIDVEIGG ERLDLAQWHL
     EDFKRILNMQ KGVLRREFTA ASPEKDNRIE VSVERFLSLA RREVAAISYS ITPLEKPVDI
     SFSPHIDGNI RNEDANYDEI FWEEVDRGVH SGGGQLTLRT KKSEFNVATA MRSELSGLQV
     EEGTGIEREP IERKKFIAEN IQVSAERGQE INLTKYIGVT TDRDYKKERT AARAEDRVRE
     AASCGYDGLL DEHVGEWQEI WRDNDIKIEG DKKAQQGIRF NIFHLNQTYT GHDPRLNIGP
     KGFTGERYGG ATYWDTEAYC LPFYLNSKDD EIARNLLLYR YHHLDKAREN ADKLGLDGAL
     YPMVTMNGEE CHNEWEITFE EIHRNAAIVY AIYNYIRHTG DRQYLADYGF EVIAAVARFW
     SDRAHYNPRR DKYMIIGVTG PNEYENNVHN NWYTNRMAVW CLNYAFDVKN YLEKEHPERS
     EKLLSRLELT EEELERWRDI TEKMYLPRWQ EREIFEQQDG YRDKKLDKVS DLDAEDLPLN
     QNWSWDKILR SPYVKQADVL QGLYFLSDQY DRETKKKNFD FYEPRTVHES SLSPCIHAVI
     AAEIGYPHKA YELYLRTARL DLENVNRDTE DGLHITSMAG TWMAVVEGFA GKKAEGGELS
     ISPMLPESWD SYQFHLNFQN SLLQVSISES GIDVELIGGD PLTLTIYEDQ HRITRDSPAE
     VPLSGGEKRN G
//