ID A0A1V4IK18_9CLOT Unreviewed; 1258 AA.
AC A0A1V4IK18;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Mannan endo-1,4-beta-mannosidase {ECO:0000313|EMBL:OPJ60219.1};
DE EC=3.2.1.78 {ECO:0000313|EMBL:OPJ60219.1};
GN ORFNames=CLORY_29400 {ECO:0000313|EMBL:OPJ60219.1};
OS Clostridium oryzae.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1450648 {ECO:0000313|EMBL:OPJ60219.1, ECO:0000313|Proteomes:UP000190080};
RN [1] {ECO:0000313|EMBL:OPJ60219.1, ECO:0000313|Proteomes:UP000190080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 28571 {ECO:0000313|EMBL:OPJ60219.1,
RC ECO:0000313|Proteomes:UP000190080};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Clostridium oryzae DSM 28571.";
RL Submitted (MAR-2017) 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}.
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:OPJ60219.1}.
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DR EMBL; MZGV01000034; OPJ60219.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4IK18; -.
DR STRING; 1450648.CLORY_29400; -.
DR OrthoDB; 9802773at2; -.
DR Proteomes; UP000190080; Unassembled WGS sequence.
DR GO; GO:0008810; F:cellulase activity; IEA:InterPro.
DR GO; GO:0016985; F:mannan endo-1,4-beta-mannosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:InterPro.
DR GO; GO:0006080; P:substituted mannan metabolic process; IEA:InterPro.
DR CDD; cd00229; SGNH_hydrolase; 1.
DR Gene3D; 2.60.40.1080; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 3.40.50.1110; SGNH hydrolase; 1.
DR InterPro; IPR003343; Big_2.
DR InterPro; IPR005087; CBM_fam11.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR022790; GH26_dom.
DR InterPro; IPR000805; Glyco_hydro_26.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR InterPro; IPR013830; SGNH_hydro.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR PANTHER; PTHR34407; EXPRESSED PROTEIN; 1.
DR PANTHER; PTHR34407:SF1; EXPRESSED PROTEIN; 1.
DR Pfam; PF02368; Big_2; 1.
DR Pfam; PF03425; CBM_11; 1.
DR Pfam; PF02156; Glyco_hydro_26; 1.
DR Pfam; PF13472; Lipase_GDSL_2; 1.
DR PRINTS; PR00739; GLHYDRLASE26.
DR SMART; SM00635; BID_2; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 1.
DR SUPFAM; SSF52266; SGNH hydrolase; 1.
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:UP000190080};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1258
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039080254"
FT DOMAIN 93..475
FT /note="GH26"
FT /evidence="ECO:0000259|PROSITE:PS51764"
FT ACT_SITE 276
FT /note="Proton donor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01100"
FT ACT_SITE 385
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01100"
SQ SEQUENCE 1258 AA; 137964 MW; F81DA3BA3072F9D8 CRC64;
MKSNKKVLKK TVAFYVAFAL TLTSANMLNW GCKEKVYAAE QDTSVDSNIA VKSADEQQVS
VSDGKLITQK KDESVQGTAL ARNVKLVDGK AKKNTRQIYA YLKAVGKSDS VIYGHQDDTF
QKAGSFNLTC SDTSDVTGSI AGVLGIDGLA LTGNEYSAKT YNSTHNTSLP QTPAGNVEAA
AKITNEGISN GAIVTLSAHM PNFANIKTNS SYNSKTDPDY AKYKFAVYTP KDTTKDCASN
ILPGGKYNKV YKAYLDMIAD YASQVNGTIL FRPFHENTGS WFWWGAAYCD AETYKNVYRY
TVEYLRDAKN IHNMLYEYGP SNTGSSSVTE YETRYPGDNY VDMVGVDMYD SKPTAEDAWI
SQFKSQLEVV NAFAKKHGKL FAVTETGISN DTASGDNQTA LLKTGNGDRN WYNRVLDAVS
QTDASYFLLW ANFSKKDGFY TPYVDSINSN GTLHGHEMLD NFISFYNDGR TIFAANQKKI
LTGGSVGSIS VKPTTAKAIG YIVSPLPGKR IQKAITVTAK ITNAKENTTA KIVFKTDKKN
ITVKAVPNGE GYYTAKITAS QVKSLGQYVG TLMLYIDGKK VQSISQVYNI PKPEIDTCEV
DGFENYNGVD TELTKAWTIN KDNNCNISLT LNKSYKANGA YGLKFTYDET ATGWAGATIN
KAADWSNCNA LQFYMVPDGK NQKTVIQITA NGTVYEAYLN TYEEYVKNGV NPVLVTIPFS
DFCQRDTAGN PTGGLVKDCK SITSFGLWVN AIANSSAVSK GRVSGTLIYD SITAIKAKTN
KVSIIKTSSK AYNDILNLKV SLNTSKVTLL KGKNKTLTAT VTGNGDKSVT WYSTNPAIAA
VNDNGEITAE RTGTVKIVAK VRNGKKAICK FTVKANSDDK DIIPAPTNYV TEDEMKLAQE
WTGVNKSALA AVMKKAESGK KVTIAVIGGS ITQGTISNGT SDSTVSTKAA YTDTFFKWWK
ETFPSVEFNF VNAGIGATDS YLGVHRVQKD VLDKNPDLVL VEFSVNDWET DFYKKTYDNL
IRRILLYKNN PAVMLLFMSQ VNGDSSQNND AYIGTKYELP MISYKNVIID MMKKAIYTKE
QLSGDTVHPS ALGHAIAGEI IWKYLNSVYK DEDIYGKPST FNKTAVTKDC YLDSEILDST
SIKPDSFGTF KTSNEFATFP NDWTCLEGTG DITFTISCKN LGIMYYCQTN GKGGQFDVYV
DGKRVDTLNA DFSGGWGNYA KTQECYTSDE TAKHTITIKK ADDSKENEFS VLGLLVSH
//
