ID A0A069CYA8_9BACE Unreviewed; 408 AA.
AC A0A069CYA8;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Endo-1,4-beta-xylanase D {ECO:0000313|EMBL:GAK35115.1};
GN ORFNames=JCM15093_191 {ECO:0000313|EMBL:GAK35115.1};
OS Bacteroides graminisolvens DSM 19988 = JCM 15093.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1121097 {ECO:0000313|EMBL:GAK35115.1, ECO:0000313|Proteomes:UP000027601};
RN [1] {ECO:0000313|EMBL:GAK35115.1, ECO:0000313|Proteomes:UP000027601}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 15093 {ECO:0000313|EMBL:GAK35115.1,
RC ECO:0000313|Proteomes:UP000027601};
RX PubMed=25736980;
RA Inoue J., Oshima K., Suda W., Sakamoto M., Iino T., Noda S., Hongoh Y.,
RA Hattori M., Ohkuma M.;
RT "Distribution and evolution of nitrogen fixation genes in the phylum
RT bacteroidetes.";
RL Microbes Environ. 30:44-50(2015).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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:GAK35115.1}.
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DR EMBL; BAJS01000001; GAK35115.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A069CYA8; -.
DR eggNOG; COG3507; Bacteria.
DR Proteomes; UP000027601; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR43772:SF2; BETA-1,4-XYLOSIDASE (EUROFUNG); 1.
DR PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361187};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651,
KW ECO:0000313|EMBL:GAK35115.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000027601};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651,
KW ECO:0000313|EMBL:GAK35115.1}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..408
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001662141"
FT ACT_SITE 34
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 203
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 144
FT /note="Important for catalytic activity, responsible for
FT pKa modulation of the active site Glu and correct
FT orientation of both the proton donor and substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-2"
SQ SEQUENCE 408 AA; 46832 MW; C8676B6E1AC3364A CRC64;
MFVSRKAILP FLFACCNSLF AQNIQNPVLT GVADAGVMKY NGKYYLGGVR TNGDFYVSKD
LTHWSKPIHV VSMNNDWSQN TGADNSQIHA NDMLYLNGQF HLYWSVNYWG KDKHAVHIVH
AQSQHVLGPY VEPDKKSWMD NRIDPKLFKD DDGQLYMYMV RFTDGNTIWA RKMKNPSQFA
GDPVCLFASL PNTWETIDNR VAEGPWVIKY RQRYYMMYNA NHTSTHWGNY QLGVAEADSP
LSFQNGNKYS YPVVESNQSI LEENYVDVLR YDGKYNPFFA YTETKPLGGW TLPVYKDSDW
KQGEGGFAAE EIAGSTTRKF GTKWDSSFLW LRKNFTAQQT RNLALRVLHT GDTKVYLNGL
LIYEKGGSNY CIVNLEPKQC AILKEGNNLL AIETQRGIRR FLTFLCLT
//
