ID   I7A0W8_MELRP            Unreviewed;       941 AA.
AC   I7A0W8;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=Glycosyl hydrolase, family 31 {ECO:0000313|EMBL:AFN74878.1};
GN   OrderedLocusNames=MROS_1644 {ECO:0000313|EMBL:AFN74878.1};
OS   Melioribacter roseus (strain JCM 17771 / P3M-2).
OC   Bacteria; Ignavibacteriota; Ignavibacteria; Ignavibacteriales;
OC   Melioribacteraceae; Melioribacter.
OX   NCBI_TaxID=1191523 {ECO:0000313|EMBL:AFN74878.1, ECO:0000313|Proteomes:UP000009011};
RN   [1] {ECO:0000313|EMBL:AFN74878.1, ECO:0000313|Proteomes:UP000009011}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 17771 / P3M-2 {ECO:0000313|Proteomes:UP000009011};
RX   PubMed=23301019; DOI=10.1371/journal.pone.0053047;
RA   Kadnikov V.V., Mardanov A.V., Podosokorskaya O.A., Gavrilov S.N.,
RA   Kublanov I.V., Beletsky A.V., Bonch-Osmolovskaya E.A., Ravin N.V.;
RT   "Genomic analysis of Melioribacter roseus, facultatively anaerobic
RT   organotrophic bacterium representing a novel deep lineage within
RT   Bacteriodetes/Chlorobi group.";
RL   PLoS ONE 8:E53047-E53047(2013).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC       {ECO:0000256|ARBA:ARBA00007806, ECO:0000256|RuleBase:RU361185}.
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DR   EMBL; CP003557; AFN74878.1; -; Genomic_DNA.
DR   RefSeq; WP_014856312.1; NC_018178.1.
DR   AlphaFoldDB; I7A0W8; -.
DR   STRING; 1191523.MROS_1644; -.
DR   GeneID; 78566594; -.
DR   KEGG; mro:MROS_1644; -.
DR   PATRIC; fig|1191523.3.peg.1742; -.
DR   eggNOG; COG1501; Bacteria.
DR   HOGENOM; CLU_000631_7_3_10; -.
DR   OrthoDB; 176168at2; -.
DR   Proteomes; UP000009011; 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.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|RuleBase:RU361185};
KW   Hydrolase {ECO:0000256|RuleBase:RU361185, ECO:0000313|EMBL:AFN74878.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009011};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..941
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003707048"
FT   DOMAIN          223..365
FT                   /note="PA14"
FT                   /evidence="ECO:0000259|PROSITE:PS51820"
SQ   SEQUENCE   941 AA;  109719 MW;  93D877E40815DBD0 CRC64;
     MKFILSALSS FIFLLAAFTP AQTESNNSFQ MKTGSGADTK LLKVEFINDY IVHVVASPAE
     QFSFRKSLII DENVKPSGNL KTEDKGDYIL LSSSALKVRI DKSTERISFY DRDGNIILQE
     HENVCRTFDD SYIMGENVYK IRQVFKASPD EAFYGFGAHQ NGIMNYRDED VDLWQYNIVD
     IIPFMVSSKN YGILWDNYSR TKFGDYRDYL SVNKVFKLIA KDDKSNGFSA EYFEDEKFEK
     SAIKRIEERI EHEYIDKNDP FPEGFDKVKS VRWEGFIESN REGLHKLRLY CSGYTKMWID
     DSLLVDSWRQ NWLPWTHIIK LDLKKGERKK IKIEWIHSGG YIGLKALPPS GENYDGIISL
     QSEVADQIDY YFVYGKNLDD VIKGYRYLTG KAPVMPKWAM GFWQCRERYK TQDELLDVVR
     EYRKRKIPID NIVQDWFYWK EDDWGSHDFD PLRFPDPEGM IKELHDSLNA HIMISVWPKF
     YVGTAHFEEF KKNGWLYMRN VEVGEKDWVG PGYVSTFYDP YSEGARKLYW KQIENKLFSK
     GIDAWWLDAT EPDIHSNLSP EETLRRMGPT ELGTSARYRN TYSLMNSKAV YEGQRLSNPD
     KRVFILTRSA FAGQQKYSAA TWSGDVAARW YDLKVQIPAG LNFSLSGIPY WTTDIGGFAV
     EPRYENPSEK DLDEWRELNT RWFQFGAFCP LFRSHGQFPY REIFNISPEG HPAYESMVYY
     DKLRYRLMPY IYSLAGMVTF EDYTIMRALI LDFPNDNKVY DISDQYMFGP AFLVNPVTDY
     KARSRKVYLP EGAEWYDFYT GKKYPGGKTI SADAPYERIP LFVKAGSIVP FGPGIQYTGQ
     KQADTLMLFV YSGKDGSFVL YEDEGTNYNY EEGLYSTIEF KYKDSDRELV IGERKGEFPG
     MLSERIINVV FISPDSPRPF DFNIKPDRAV NYNGKEVKIK L
//