GenomeNet

Database: UniProt
Entry: C3QER1_9BACE
LinkDB: C3QER1_9BACE
Original site: C3QER1_9BACE 
ID   C3QER1_9BACE            Unreviewed;       475 AA.
AC   C3QER1;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 2.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=Glycosyl hydrolase, family 43 {ECO:0000313|EMBL:EEO50509.2};
GN   ORFNames=BSAG_02220 {ECO:0000313|EMBL:EEO50509.2};
OS   Bacteroides sp. D1.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=556258 {ECO:0000313|EMBL:EEO50509.2, ECO:0000313|Proteomes:UP000003361};
RN   [1] {ECO:0000313|EMBL:EEO50509.2, ECO:0000313|Proteomes:UP000003361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D1 {ECO:0000313|EMBL:EEO50509.2,
RC   ECO:0000313|Proteomes:UP000003361};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Strauss J., Sibley C.,
RA   White A., Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA   Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA   Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA   MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA   Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Bacteroides sp. D1.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
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:EEO50509.2}.
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; ACAB02000008; EEO50509.2; -; Genomic_DNA.
DR   AlphaFoldDB; C3QER1; -.
DR   HOGENOM; CLU_009397_11_2_10; -.
DR   Proteomes; UP000003361; 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; cd18618; GH43_Xsa43E-like; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   InterPro; IPR006584; Cellulose-bd_IV.
DR   InterPro; IPR005084; CMB_fam6.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR006710; Glyco_hydro_43.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   PANTHER; PTHR43772:SF6; -; 1.
DR   PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR   Pfam; PF03422; CBM_6; 1.
DR   Pfam; PF04616; Glyco_hydro_43; 1.
DR   SMART; SM00606; CBD_IV; 1.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 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, ECO:0000256|RuleBase:RU361187};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361187};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..475
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002929182"
FT   DOMAIN          317..442
FT                   /note="CBM6"
FT                   /evidence="ECO:0000259|PROSITE:PS51175"
FT   ACT_SITE        34
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT   ACT_SITE        197
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
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   475 AA;  54222 MW;  1643A24C11E7A877 CRC64;
     MKNLNFWGVS LLLVMMAVSG TAQNPIIQTK YTADPAPMVY NDTVFLYTTH DEDDAEGFKM
     LDWLLYTSID MVNWTDHGAV ASLKSFDWVK RDNGAWAEQV IERNGKFYMY CPIHGNGIGV
     LVSDSPYGPF KDPLNKPLVW QKEHWYDIDP TVFIDDDGQA YMYWGNPNVY YVKLNEDMIS
     YSGEIVQVEN KPEHYQEGPW VYKRNGHYYM AFASTCCPEG IGYAMSDKAT GPWSTKGYIM
     RPTERSRGNH PGIIDYKGSS YVFGLNYDLL HLETLDHKER RSVSVAKMHY NPDGTIKEVP
     YWQETKLEQI ENFNPYRRVE AETMAWGYGL KAENHKNGGL YITDIDDNEY LCVRGADFGK
     KGAKKFSVSA ACVEKGGMIE IRLDSTEGPV IGSVSISPTG GLDIYKQMSC RIKNAKGVHD
     LYFCFKGEKG NKLFNLDYWE WFFVKFGGTS SIVNKESWLS VVYFLPYCTS AFLPL
//
DBGET integrated database retrieval system