ID   Q21HR9_SACD2            Unreviewed;       973 AA.
AC   Q21HR9;
DT   18-APR-2006, integrated into UniProtKB/TrEMBL.
DT   18-APR-2006, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   SubName: Full=Putative retaining a-glycosidase {ECO:0000313|EMBL:ABD81760.1};
GN   Name=xyl31A {ECO:0000313|EMBL:ABD81760.1};
GN   OrderedLocusNames=Sde_2500 {ECO:0000313|EMBL:ABD81760.1};
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:ABD81760.1, ECO:0000313|Proteomes:UP000001947};
RN   [1] {ECO:0000313|EMBL:ABD81760.1, 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).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC       {ECO:0000256|ARBA:ARBA00007806, ECO:0000256|RuleBase:RU361185}.
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DR   EMBL; CP000282; ABD81760.1; -; Genomic_DNA.
DR   RefSeq; WP_011468977.1; NC_007912.1.
DR   AlphaFoldDB; Q21HR9; -.
DR   STRING; 203122.Sde_2500; -.
DR   CAZy; GH31; Glycoside Hydrolase Family 31.
DR   KEGG; sde:Sde_2500; -.
DR   eggNOG; COG1501; Bacteria.
DR   HOGENOM; CLU_000631_7_3_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:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd14752; GH31_N; 1.
DR   CDD; cd06591; GH31_xylosidase_XylS; 1.
DR   Gene3D; 2.60.120.380; -; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1760; glycosyl hydrolase (family 31); 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 2.
DR   InterPro; IPR033403; DUF5110.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR048395; Glyco_hydro_31_C.
DR   InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR   InterPro; IPR000322; Glyco_hydro_31_TIM.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR037524; PA14/GLEYA.
DR   InterPro; IPR011658; PA14_dom.
DR   PANTHER; PTHR43863; HYDROLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G03140)-RELATED; 1.
DR   PANTHER; PTHR43863:SF2; MALTASE-GLUCOAMYLASE, INTESTINAL-LIKE; 1.
DR   Pfam; PF17137; DUF5110; 1.
DR   Pfam; PF13802; Gal_mutarotas_2; 1.
DR   Pfam; PF01055; Glyco_hydro_31_2nd; 1.
DR   Pfam; PF21365; Glyco_hydro_31_3rd; 1.
DR   Pfam; PF07691; PA14; 1.
DR   SMART; SM00758; PA14; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF56988; Anthrax protective antigen; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR   PROSITE; PS51820; PA14; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|RuleBase:RU361185, ECO:0000313|EMBL:ABD81760.1};
KW   Hydrolase {ECO:0000256|RuleBase:RU361185};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001947}.
FT   DOMAIN          242..394
FT                   /note="PA14"
FT                   /evidence="ECO:0000259|PROSITE:PS51820"
SQ   SEQUENCE   973 AA;  110199 MW;  678199F4ACF7C1E5 CRC64;
     MNYYLNKKRL GQLLTGAAII PVLYACGSQE KNVEPATVNW HKTSDGVVVS LQDSEAKKVR
     LQVINDRIVR VTATPQQDFN NLPNTLMVVA KPEQTAFEVK QNDASVVLST ADLSAEVSLV
     TGVVSFKDEH GKVLTTEVDR GNFGAVTRDP GVVDADSFAI RQQFTSDENE GYYGLGQQQD
     GEVNYAGDNV ELTTYNLEIS IPYVVSSKDY ALLWNNTSIS RLGDPNPPEP LKEGFKLFDA
     NGNPGGLTAR YFDGDKLLLE RVEADLDYQF LAQGSNRTTP MPDETADAKN LRIEWEGSIE
     SDTNGVHELK MYSSGYAKLY LNGELVLDRW RMNWNPWYHN TKLEMQAGKK VALKLDWQVD
     GGYMRIKQHK PLPVAEQGRL SIASDTAKAI DYYFVVGDNK DELVSGYRTL TGKAVMLPKW
     VFGFWQSRER YKTQDEIIDA LQEYRDRKIP IDNIVLDWSY WPQDAWGSHD FDEQFFPDPS
     ALVDKVHELN GNIMISVWPK FYPTTDNYKA LNAKGCMFNK NIEQKNLDWI GEGYLNGFYD
     AYNPECREMF WAQIRDKINV HGFDAWWLDA VEPDIHSNLS FEHRKDLMTP NALGTGAEVF
     NAYALPHAET VYQGERRDDG DKRAFILTRS GFAGIQRTGS AIWSGDVVSR WSDLKEQIAA
     GVGVGISGMP YWTFDIGGFT PEDRYRYSAK GSVGHFSMMN ESEVPEWQEI NLRWFQFGTF
     VPLFRSHGQN PYREIYNIAD KGTEVYDSMV WYTKTRYRLM PYIYSLVGDA HHKDGTFMRA
     LVMDFPSDLN VRDINDQYMF GPALLVNPVS EFKARSRDVY LPAGADWYDF YTGVKHTGGK
     TIKADAPLAK MPIFVKAGSI IPTGVEIQHV YDKPDAPYTL NVYTGANGSF EIYEDDGKTY
     AYEQGAWARI PVSYNDKTGE LTIGDRVGSF EGMTKEREFR VRWISAKRDD AANFDTGVAK
     AVTYTGKAIT IKR
//