ID A0A255SXJ1_9BACT Unreviewed; 822 AA.
AC A0A255SXJ1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Glycoside hydrolase {ECO:0000313|EMBL:OYP57689.1};
GN ORFNames=CIK99_06175 {ECO:0000313|EMBL:OYP57689.1};
OS Prevotella sp. P5-92.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=2024222 {ECO:0000313|EMBL:OYP57689.1, ECO:0000313|Proteomes:UP000216769};
RN [1] {ECO:0000313|EMBL:OYP57689.1, ECO:0000313|Proteomes:UP000216769}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P5-92 {ECO:0000313|EMBL:OYP57689.1,
RC ECO:0000313|Proteomes:UP000216769};
RA Accetto T., Nograsek B., Avgustin G.;
RT "Comparative genomics of non-oral Prevotella species.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865}.
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:OYP57689.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NPJG01000054; OYP57689.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A255SXJ1; -.
DR OrthoDB; 3308423at2; -.
DR Proteomes; UP000216769; Unassembled WGS sequence.
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:UniProtKB-KW.
DR CDD; cd04084; CBM6_xylanase-like; 1.
DR CDD; cd02858; E_set_Esterase_N; 1.
DR CDD; cd18618; GH43_Xsa43E-like; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR006584; Cellulose-bd_IV.
DR InterPro; IPR005084; CMB_fam6.
DR InterPro; IPR000801; Esterase-like.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR PANTHER; PTHR43772:SF6; -; 1.
DR PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR Pfam; PF03422; CBM_6; 1.
DR Pfam; PF00756; Esterase; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SMART; SM00606; CBD_IV; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS51175; CBM6; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00022651};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:OYP57689.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651};
KW Reference proteome {ECO:0000313|Proteomes:UP000216769};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..822
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013055761"
FT DOMAIN 331..456
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT SITE 149
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 822 AA; 92859 MW; 60777E88DFE32381 CRC64;
MRIKNMLLAG LVSAAATVQA QNPVVQTWFT SDPAPLADGD RLYMYTGHDE DNADFFWMYE
WRCYSTADMV NWTDHGGLMS LDTFSWADDR AWAAQTIKRN GKYYWYICAH SKITNGMAIG
VAVADSPTGP FKDALGKPLF DNGSWDNIDP TVMIDDDGQA YIYWGNPQIY FARLNNDMVS
IDGEVKKLEM TEEGFGAPTM RERVKGKKYK DCYTEGPWIT KRNGKYWLLY AAGGVPEHIA
YSVSDKPEGP WKYVGPIMPL EDTKSFTNHC GVEDFKGHSY FFYHTGKLPG GGGFGRSCAV
EEFKYNADGS FPIIHHTDKG VDPIGKLCPF QRVEAETMAF SRGVKSEQNV DDGVFITETH
NGDYIKVREV DFNKQPRFFK ASVASGMRGG VMEVRLDSIK GEKIAEVKIG NTGGWTNWTT
VVANVEKTVS GTRDLYFVFV GDKGVKLMNF NWWQFTDGSE MKANKAGLIP SETNLPGSQS
PSLDMENRAH FSIYAPKTSR IVVDVCGKKY PMEKDAHGLW TCVTDPLVVG NHYYFLEVDG
YRVSDPNTYT IFGCSRMASQ IEVAEGAEGD YYRPQQGVAK GQVRSVEYYA ESQKQWRRAM
VYTPADYDKS KKKYPVLYLQ HGMAEDETGW STQGRMNHIM DNLIASGECE PMIVVMESGD
VEVGFAPRRG KDVEQQRMQY GASFYEVMFN DLIPMVEKTF RCKTGRENRA MAGLSWGGFQ
TFNVVLPHLD KFAYLGTFSG ALFGIDVKTC FDGVFTDAKK FNSDVKYFFM GCGSEENFGT
EKMTSDLKQM GINVEFYVSP GTHHEWLTWR RCFRQFVPHL FK
//
