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Database: UniProt
Entry: A0A0D7W2G9_9FLAO
LinkDB: A0A0D7W2G9_9FLAO
Original site: A0A0D7W2G9_9FLAO 
ID   A0A0D7W2G9_9FLAO        Unreviewed;       698 AA.
AC   A0A0D7W2G9;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Glycogen debranching protein {ECO:0000313|EMBL:KJD32047.1};
GN   ORFNames=PK35_10550 {ECO:0000313|EMBL:KJD32047.1}, PK35_11435
GN   {ECO:0000313|EMBL:KJD32209.1};
OS   Tamlana nanhaiensis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Tamlana.
OX   NCBI_TaxID=1382798 {ECO:0000313|EMBL:KJD32047.1, ECO:0000313|Proteomes:UP000032361};
RN   [1] {ECO:0000313|EMBL:KJD32047.1, ECO:0000313|Proteomes:UP000032361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FHC16 {ECO:0000313|EMBL:KJD32047.1,
RC   ECO:0000313|Proteomes:UP000032361};
RX   PubMed=25735434; DOI=10.1007/s10482-015-0410-x;
RA   Liu X., Lai Q., Du Y., Li G., Sun F., Shao Z.;
RT   "Tamlana nanhaiensis sp. nov., isolated from surface seawater collected
RT   from the South China Sea.";
RL   Antonie Van Leeuwenhoek 107:1189-1196(2015).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing alpha-L-rhamnose residues
CC         in alpha-L-rhamnosides.; EC=3.2.1.40;
CC         Evidence={ECO:0000256|ARBA:ARBA00001445};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing beta-D-fructofuranoside
CC         residues in beta-D-fructofuranosides.; EC=3.2.1.26;
CC         Evidence={ECO:0000256|ARBA:ARBA00000094};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 100 family.
CC       {ECO:0000256|ARBA:ARBA00007671}.
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:KJD32047.1}.
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DR   EMBL; JTDV01000010; KJD32047.1; -; Genomic_DNA.
DR   EMBL; JTDV01000010; KJD32209.1; -; Genomic_DNA.
DR   RefSeq; WP_044626692.1; NZ_JTDV01000010.1.
DR   AlphaFoldDB; A0A0D7W2G9; -.
DR   STRING; 1382798.PK35_10550; -.
DR   PATRIC; fig|1382798.3.peg.664; -.
DR   OrthoDB; 49490at2; -.
DR   Proteomes; UP000032361; Unassembled WGS sequence.
DR   GO; GO:0033926; F:glycopeptide alpha-N-acetylgalactosaminidase activity; IEA:InterPro.
DR   GO; GO:0016791; F:phosphatase activity; IEA:UniProt.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 1.50.10.10; -; 1.
DR   Gene3D; 3.90.1070.10; -; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR035396; Bac_rhamnosid6H.
DR   InterPro; IPR024746; Glyco_hydro_100.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006379; HAD-SF_hydro_IIB.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR006380; SPP-like_dom.
DR   NCBIfam; TIGR01484; HAD-SF-IIB; 1.
DR   PANTHER; PTHR46521:SF16; S6PP DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR46521; SUCROSE-PHOSPHATASE 2-RELATED; 1.
DR   Pfam; PF17389; Bac_rhamnosid6H; 1.
DR   Pfam; PF12899; Glyco_hydro_100; 1.
DR   Pfam; PF05116; S6PP; 1.
DR   SFLD; SFLDG01141; C2.B.1:_Sucrose_Phosphatase_Li; 1.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000032361}.
FT   DOMAIN          13..251
FT                   /note="Sucrose phosphatase-like"
FT                   /evidence="ECO:0000259|Pfam:PF05116"
FT   DOMAIN          353..510
FT                   /note="Alpha-L-rhamnosidase six-hairpin glycosidase"
FT                   /evidence="ECO:0000259|Pfam:PF17389"
SQ   SEQUENCE   698 AA;  79604 MW;  49D879809F9360FF CRC64;
     MNKTEDGNHA VIKLLSFDID NTLIDFHTHK SNFKKIWESY KPQNVLLTYN TGRLIDDVLG
     LIEKGTLPEP DYIIAGVGTL IYDYKKQRTV KAFNDVLDDG WDLEAVEKIV QNIKHPISEQ
     PTKFQHAYKR SYFFHDATDD LIESIEKDFA DANMFVNIVY SGNQFLDVLP KWANKGNALQ
     WLLNNVDINA ENVLVAGDSG NDSAMFDMDG VKGIVVANAH EELYKYTKYK QMYHAENIHS
     DGIIEGLIYY GVLPKDAKVS ENIDHTDDYI IQQELSHIAE EDEDEKLALI REGYEKAVIA
     LKKNITPLGF SACSIKDNVS KGTDENYYSV WARDGAITVI GSLPLIHDEE IHACQRKTLE
     TLFEHISRNG QIPSNVRIKD NQPDYSGVGG ICSIDSGIWV VIAFYEYVNV TKDIKFLRKY
     IKDIKETMRW LGAHDSNNDA LLEIPEAGDW TDLFGGSYNI LYDEILWYRA NVCFGRMLEM
     LGDYEEAGEY IRWSQVIKKE ILQNFWPSTQ QKLFQSVSFA ERQFTLGDTS YLIAQTTPFD
     FSWRCDVFGN VLAFLHGATD SEKAHETFKF MLGVGVNDPF PVSNVYPVVT PGDPDWRPYY
     TVNLLNLPNH YHNGGIWPFV GGFWVKFINK LGLKDVAISE LYKLALINKE GLTEEWEFTE
     WAHGITGKAM GKAYQAWSAA QYISACHDLK IINRLTKI
//
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