ID A0A2L0F4P2_SORCE Unreviewed; 561 AA.
AC A0A2L0F4P2;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Carbohydrate-binding protein {ECO:0000313|EMBL:AUX46540.1};
GN ORFNames=SOCE26_080460 {ECO:0000313|EMBL:AUX46540.1};
OS Sorangium cellulosum (Polyangium cellulosum).
OC Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae; Sorangium.
OX NCBI_TaxID=56 {ECO:0000313|EMBL:AUX46540.1, ECO:0000313|Proteomes:UP000238348};
RN [1] {ECO:0000313|EMBL:AUX46540.1, ECO:0000313|Proteomes:UP000238348}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=So ce26 {ECO:0000313|EMBL:AUX46540.1,
RC ECO:0000313|Proteomes:UP000238348};
RA Zaburannyi N., Bunk B., Overmann J., Mueller R.;
RT "Sorangium comparison.";
RL Submitted (SEP-2015) 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; CP012673; AUX46540.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2L0F4P2; -.
DR OrthoDB; 5488121at2; -.
DR Proteomes; UP000238348; Chromosome.
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..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..561
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014778756"
FT DOMAIN 336..459
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT REGION 462..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 43
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 214
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 160
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 561 AA; 58949 MW; F22DCBE649CD7A4D CRC64;
MATITTSPQH KLLIAAMLLC STTAFPSESM ADNPIIQTIY TADPAPMVHD GTLYLYTTHD
EDSASTFFGM NEWRVYSSTD MANWTDRGSP LKYKDFSWSK ADAWAGQVTH RNGKFYFYIP
TTSRTLNRMT IGVAVSDSPV GPFEDALGRP LITANCGDID PTVFIDDDGQ AYLYWGNPNL
CYVKLNEDMT SYQGDVVRVP MTAESFGERT GSAERPTLYE EGPWLYKRDG MYYLAYPAGG
IPEYIAYSTS SSPTGPWTYR GVIMPTEGGS FTNHPGIIDY KDNSYFFYHN AALPGGDGYH
RSVAVERFTY NADGTIPTIT MTEAGPPAAG TLDPYVMTEA ETIAWESGVE TEACSEGGMN
VTSIEDGDYI KVKGVDFGAG AGSFDARVAS ATSGGSIELR LDSTTGTLVG TCMVQGTGGP
QTWVTESCAV DGATGIHDLY LKFTGGNGPL FNFNWWKFTP RDATDPTGSG GGQSTGEGGA
TGSGGSGEGG SASSAATTGS GTGGAGAAPP DGASEDEGGC GCRVISGPSS PAGVLAALTA
LGAIAARRRA RRAGRSGADA S
//