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Database: UniProt
Entry: Q21MM7_SACD2
LinkDB: Q21MM7_SACD2
Original site: Q21MM7_SACD2 
ID   Q21MM7_SACD2            Unreviewed;       661 AA.
AC   Q21MM7;
DT   18-APR-2006, integrated into UniProtKB/TrEMBL.
DT   18-APR-2006, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   SubName: Full=A-glucosidase-like protein {ECO:0000313|EMBL:ABD80052.1};
GN   Name=gly97D {ECO:0000313|EMBL:ABD80052.1};
GN   OrderedLocusNames=Sde_0790 {ECO:0000313|EMBL:ABD80052.1};
OS   Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Saccharophagus.
OX   NCBI_TaxID=203122 {ECO:0000313|EMBL:ABD80052.1, ECO:0000313|Proteomes:UP000001947};
RN   [1] {ECO:0000313|EMBL:ABD80052.1, ECO:0000313|Proteomes:UP000001947}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2-40 / ATCC 43961 / DSM 17024
RC   {ECO:0000313|Proteomes:UP000001947};
RX   PubMed=18516288; DOI=10.1371/journal.pgen.1000087;
RA   Weiner R.M., Taylor L.E.II., Henrissat B., Hauser L., Land M.,
RA   Coutinho P.M., Rancurel C., Saunders E.H., Longmire A.G., Zhang H.,
RA   Bayer E.A., Gilbert H.J., Larimer F., Zhulin I.B., Ekborg N.A., Lamed R.,
RA   Richardson P.M., Borovok I., Hutcheson S.;
RT   "Complete genome sequence of the complex carbohydrate-degrading marine
RT   bacterium, Saccharophagus degradans strain 2-40 T.";
RL   PLoS Genet. 4:E1000087-E1000087(2008).
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DR   EMBL; CP000282; ABD80052.1; -; Genomic_DNA.
DR   RefSeq; WP_011467273.1; NC_007912.1.
DR   AlphaFoldDB; Q21MM7; -.
DR   STRING; 203122.Sde_0790; -.
DR   CAZy; GH97; Glycoside Hydrolase Family 97.
DR   KEGG; sde:Sde_0790; -.
DR   eggNOG; COG3589; Bacteria.
DR   HOGENOM; CLU_011166_1_1_6; -.
DR   Proteomes; UP000001947; Chromosome.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:UniProt.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.70.98.10; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR014718; GH-type_carb-bd.
DR   InterPro; IPR029483; GH97_C.
DR   InterPro; IPR019563; GH97_catalytic.
DR   InterPro; IPR029486; GH97_N.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR35803; GLUCAN 1,4-ALPHA-GLUCOSIDASE SUSB-RELATED; 1.
DR   PANTHER; PTHR35803:SF2; RETAINING ALPHA-GALACTOSIDASE; 1.
DR   Pfam; PF14509; GH97_C; 1.
DR   Pfam; PF14508; GH97_N; 1.
DR   Pfam; PF10566; Glyco_hydro_97; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001947};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..661
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004200244"
FT   DOMAIN          38..304
FT                   /note="Glycosyl-hydrolase 97 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14508"
FT   DOMAIN          310..553
FT                   /note="Glycosyl-hydrolase 97 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF10566"
FT   DOMAIN          569..660
FT                   /note="Glycosyl-hydrolase 97 C-terminal oligomerisation"
FT                   /evidence="ECO:0000259|Pfam:PF14509"
SQ   SEQUENCE   661 AA;  73209 MW;  9343B7FDE039BDAB CRC64;
     MKMIIKLALA VTLAVWVAGC TNQAGLNAEN KNIERQTINS PDKSLKVRLS LDESGKVFYS
     ISRNGEQVML PSQLGVELNS QAFTDGLTIT DVDAGKVNDS YTLLHGKQRD ITYNANEKIY
     SLKNKQGDKL IIAFRVSNDG VAFQYRFPNT AKQLLAVKKE ITSFAFEHTT KAWLQPIAVA
     QTGWANTNPS YEEHYQMNIP VDTVSPSPAG WVFPALFKAN KHWLLITEAG MNGDYHASRL
     HAESPNGEYS LGIPMAAEVF EQDGNKGALL AQSNTAFHSP WRVILVGGLD TIIASTLGTD
     LADPAIAKMD FVKPGTASWS WALLKDESVN YETSLEFIDY AAEMGWDYTL VDADWDRRIG
     YERTAQLAAY AQSKNVGLLV WYNSSGDWNT TEYSPKSALL DRDKRRAEFA RLQNMGVKGV
     KIDFFPGDGK SVMAYYNDLA KDAADYNLLV NYHGSSLPRG LHRTYPNIMT MESVHGFEMI
     TFMQPSADKA ATHMAILPFT RNAFDPMDFT PTTFSDIPNI ERRTSNGFEL ALPVLFLSGL
     QHIAETAQGM ATNAPDYVKA YMRDIPVLWD ESKLIDGMPG EHVVIARKHG ERWFVAGINA
     TNEAINLEMN FDFALGKQGT LITDSNINTK GVESFTSHTI TATKNNALTV KANGGFVIVF
     N
//
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