ID A0A179DN53_9SPHI Unreviewed; 772 AA.
AC A0A179DN53;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Maltose phosphorylase {ECO:0000313|EMBL:OAQ42364.1};
GN ORFNames=A5893_04435 {ECO:0000313|EMBL:OAQ42364.1};
OS Pedobacter psychrophilus.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1826909 {ECO:0000313|EMBL:OAQ42364.1, ECO:0000313|Proteomes:UP000078459};
RN [1] {ECO:0000313|EMBL:OAQ42364.1, ECO:0000313|Proteomes:UP000078459}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCM 8644 {ECO:0000313|EMBL:OAQ42364.1,
RC ECO:0000313|Proteomes:UP000078459};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OAQ42364.1, ECO:0000313|Proteomes:UP000078459}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCM 8644 {ECO:0000313|EMBL:OAQ42364.1,
RC ECO:0000313|Proteomes:UP000078459};
RA Svec P.;
RT "Pedobacter psychrophilus sp. nov., isolated from Antarctic fragmentary
RT rock.";
RL Submitted (JUN-2016) 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:OAQ42364.1}.
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DR EMBL; LWHJ01000011; OAQ42364.1; -; Genomic_DNA.
DR RefSeq; WP_068821392.1; NZ_LWHJ01000011.1.
DR AlphaFoldDB; A0A179DN53; -.
DR STRING; 1826909.A5893_04435; -.
DR OrthoDB; 9758855at2; -.
DR Proteomes; UP000078459; Unassembled WGS sequence.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProt.
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:UP000078459}.
FT DOMAIN 14..265
FT /note="Glycoside hydrolase family 65 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03636"
FT DOMAIN 322..688
FT /note="Glycoside hydrolase family 65 central catalytic"
FT /evidence="ECO:0000259|Pfam:PF03632"
FT DOMAIN 697..757
FT /note="Glycoside hydrolase family 65 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03633"
FT ACT_SITE 488
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036289-50"
FT BINDING 357..358
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036289-51"
FT BINDING 600..601
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036289-51"
SQ SEQUENCE 772 AA; 89299 MW; 7D6457E78A84C5E7 CRC64;
MKDYIIKDEW NIIEEGFDPH LNKISESIFS LGNGRMGQRA NFEETYSGET LSGNYIAGVY
YPDKTRVGWW KNGYPEYFAK VLNAANWIGI EVKIEDEILD LATSKVTDFK RILNMQEGYL
ERIFTAELPS GNKIKVNAIR FCSIVDDEVG VINYSITPLN FDGKIEFTSY IDGDVKNQDS
NYDEKFWDFV NNEITNNEAY LTLRTKKTEF EVCTASFIQL LADEKAIDFN SEAIRKEKFV
GQKIGINAVQ NQEISLIKIA ANLTSQNHQK SDLLNHTKII IAKASTKGFH QLKLEQKQAW
ASKWQESDII IEGDIAAQQA IRFNIFQLFQ TYTGKDDRLN IGPKGFTGEK YGGSTYWDTE
AYCVPFYLAT APQQVSKNLL IYRYKQLDKA IENAQKLGFD NGAALFPMVT MNGEECHNEW
EITFEEIHRN GAIAYAIHNY IRYTGDENYL NDYGLEVLIG ISRFWKQRVN WSKAQNKFVM
LGVTGPNEYE NNINNNWYTN ILATWCMKYT IKAAQIVEKN RPSQYKNLIE KLNFNKQEFS
DWASIIDNMY YPEDADKGIF LQQDGYLDKE QILVKDLPKS ERPINQKWSW DRILRSCFIK
QADVLQGIYF FEEDYDLATI KRNFDFYEAR TVHESSLSPC VHSILAAKLN DEAKAYQFYL
RTARLDLDDY NNDTEDGLHI TSMAGTWMSI VEGFAGMRVR DNQLHFNPFL PKHWQSFSFK
INFRGANLNI KIDGKSFQIA ANDDKDLEIF IHGQKHQFKG SGIIELQNKE LV
//