ID A0A1G5UM51_9SPHN Unreviewed; 471 AA.
AC A0A1G5UM51;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Carbohydrate binding module (Family 6) {ECO:0000313|EMBL:SDA33905.1};
GN ORFNames=SAMN03159340_02989 {ECO:0000313|EMBL:SDA33905.1};
OS Sphingomonas sp. NFR15.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1566282 {ECO:0000313|EMBL:SDA33905.1, ECO:0000313|Proteomes:UP000199327};
RN [1] {ECO:0000313|Proteomes:UP000199327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NFR15 {ECO:0000313|Proteomes:UP000199327};
RA Varghese N., Submissions S.;
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; FMWX01000006; SDA33905.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5UM51; -.
DR STRING; 1566282.SAMN03159340_02989; -.
DR Proteomes; UP000199327; 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:UP000199327};
KW Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..471
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011591214"
FT DOMAIN 322..461
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT ACT_SITE 37
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 202
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 155
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 471 AA; 51292 MW; 60ADA327DCB45D21 CRC64;
MRIRSIITGL CALLATALFP APVNADNPII QTLFTADPAP LVHDGTVYLY TSHDEDDARN
FVMRDWRLYT STDMVNWTDH GAVASLKTFP WARQDNDAWA PQVIARGGKF YLYVPISVAG
SPKNVIAVAV ADTPYGPFKD ALGHPLIAPA SDNIDPTVAI DGDGQAWLYW GNPDLWRVKL
NPDMISTAGP IVKMPRLTDY QEGPWFYRRA GHYYMAYAST CCPEGIGYAM SDHAAGPWRY
QGSIMDHDKR SSGNHPGIID YKGHSYVFGF NYRLNDAQTG EHRERRSVTV TEFRYNKDGT
IPMQPWWDTV GAKQLGTIDP FRRVEAETIA WTSATDTSAS GAHAWAPGVR TASSGATGMY
VTHVLDGGYI VVRGVDFGTG AGKTFEATVA AARAGAGIDL RLDGLAGPRV ATLAVPATGG
PETWRTVSAP LARTRGVHDV FLVFHGTPGE SLFNFDAWRI GTGRGGHQAP R
//
