ID A0A1I7KQY5_9BACT Unreviewed; 453 AA.
AC A0A1I7KQY5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Carbohydrate binding module (Family 6) {ECO:0000313|EMBL:SFU99872.1};
GN ORFNames=SAMN04487941_4015 {ECO:0000313|EMBL:SFU99872.1};
OS Pontibacter akesuensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Pontibacter.
OX NCBI_TaxID=388950 {ECO:0000313|EMBL:SFU99872.1, ECO:0000313|Proteomes:UP000182491};
RN [1] {ECO:0000313|Proteomes:UP000182491}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18820 {ECO:0000313|Proteomes:UP000182491};
RA Varghese N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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DR EMBL; FPCA01000007; SFU99872.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I7KQY5; -.
DR STRING; 388950.GCA_001611675_04079; -.
DR OrthoDB; 3308423at2; -.
DR Proteomes; UP000182491; 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 Reference proteome {ECO:0000313|Proteomes:UP000182491};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..453
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010257054"
FT DOMAIN 326..452
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT ACT_SITE 35
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 211
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 150
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 453 AA; 50432 MW; E201434CFEF7016B CRC64;
MNNLFTATCL MYAFCLVSFL AQAQNPIIQT AYTADPAPMV HNNKLYLYTS HDEDGSTWFT
MNDWKLYTTE DMVNWTDHGA ILAYSDFSWA RINAWAPQCI ERGGKFYMYV PLTTHDNQMA
IGVAVANSPY GPFRDPLGKP LIQSGGGDID PSIFLDDDGQ AYLYWGNPKS FYVKLNEDMI
SYQGEIVQVP NTVASFGRRE GSPERPTTYE EGPWLYKRKG LYYLLFAAGP LPEHIGYSTS
ANPTGPWKYQ GVLMSTEGSS FTNHPGIIDF KGKTYFFYHN GALPGGGGFT RSVSVEEVTF
KKDGTIQPMK MTKGITRGLA PLNPFVKNEA ETIAWSEGVK SMQNEKVGVF VTALRNGAYT
KVKDVDFRKT GASKFTARLG TTHNTEVNLE VRLGSVEGEL IGTVKAPLTG GNDRWALVAS
SVKKVTGIHD VYFVFKGKEA SNILFFDYWM FSE
//
