ID   A0A1I2R6N0_9BACT        Unreviewed;       780 AA.
AC   A0A1I2R6N0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Glycosyl hydrolase family 26 {ECO:0000313|EMBL:SFG33416.1};
GN   ORFNames=SAMN05216383_11063 {ECO:0000313|EMBL:SFG33416.1};
OS   Prevotella sp. KH2C16.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=1855325 {ECO:0000313|EMBL:SFG33416.1, ECO:0000313|Proteomes:UP000198560};
RN   [1] {ECO:0000313|Proteomes:UP000198560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KH2C16 {ECO:0000313|Proteomes:UP000198560};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 26 family.
CC       {ECO:0000256|ARBA:ARBA00007754, ECO:0000256|PROSITE-ProRule:PRU01100}.
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DR   EMBL; FOOW01000010; SFG33416.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2R6N0; -.
DR   STRING; 1855325.SAMN05216383_11063; -.
DR   OrthoDB; 9803686at2; -.
DR   Proteomes; UP000198560; Unassembled WGS sequence.
DR   GO; GO:0016985; F:mannan endo-1,4-beta-mannosidase activity; IEA:InterPro.
DR   GO; GO:0006080; P:substituted mannan metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.80; Glycosidases; 2.
DR   InterPro; IPR022790; GH26_dom.
DR   InterPro; IPR000805; Glyco_hydro_26.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31297:SF17; ENDOGLUCANASE; 1.
DR   PANTHER; PTHR31297; GLUCAN ENDO-1,6-BETA-GLUCOSIDASE B; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   Pfam; PF02156; Glyco_hydro_26; 1.
DR   PRINTS; PR00739; GLHYDRLASE26.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 2.
DR   PROSITE; PS51764; GH26; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PROSITE-
KW   ProRule:PRU01100};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01100}; Reference proteome {ECO:0000313|Proteomes:UP000198560};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..780
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011549539"
FT   DOMAIN          102..422
FT                   /note="GH26"
FT                   /evidence="ECO:0000259|PROSITE:PS51764"
FT   ACT_SITE        260
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01100"
FT   ACT_SITE        370
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01100"
SQ   SEQUENCE   780 AA;  86590 MW;  3F3A835DF2E69B61 CRC64;
     MKKLLFSIVA LLMALNVSAQ ADTDVYTVHK TDGTSEQFSI KDNNHLKFTD ANTLVNYMTG
     FEDWGATGTW NVSDIKSITF DVFHQDPIDV TGVSLADAQA SDEAKKLYKY LQLVYGTKIL
     SGVMANVAWN HTEADKIYSL TGKYPAINCF DFIHITVPNQ GSNGWINYND ITPVTEWASA
     GGIVSLMWHF NVPKNENTKI GADGSGTGIK AGETTFKAAN ALVTGTWENR FFMEQLENVA
     NVMLKLQDAG VVALWRPFHE AAGNSTEKSG TWGKAWFWWG EAGAETFRQL WQTMFNYFAT
     KGIHNLIWEW TSQNYNGDAA NYNNDYGWYP GDAYVDIIGR DLYGTNATQQ VTEYRQLKAQ
     FPTKMITLSE CGINGNTPTA DVGDAWDAGA KWLNFMPWYG ASMPSDAWWK KVMDEGVVIT
     RDEVNTDATY MAEPAQSAVV NFGLGFNLGN TLEANGIGKG QDLAKYETQW GQQPTTQSQL
     TFLKKEGFNS VRIPITWYEH MDDAGNVDAA WMGRVKEVVD YAMNAGLYVI INVHHDTAAG
     KGAWIKADPA VYAATKDRYK KLWTQIANAF ADYDQHLLFE GYNEMLDASN TWNQPLDASS
     YTALNNYAQD FVDAVRATGG NNATRNLVVS TYAAAKGVEV LNNFTIPTDK TTGHLVAEVH
     SYDPWNFIND KDTWDDECHI TLTNIFSDVS KKFDSIPFII GEYGTAGAAD ANGNETSVNK
     SSAPEKIKMA ADQAADMVRQ AKGKKAATFY WMSIFNGADR TVPQWSLPTV VEAMKKAYNE
//