ID A0A098U7B6_9BURK Unreviewed; 460 AA.
AC A0A098U7B6;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Carbohydrate-binding protein {ECO:0000313|EMBL:KGF80207.1};
GN ORFNames=IA69_19610 {ECO:0000313|EMBL:KGF80207.1};
OS Massilia sp. JS1662.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1519190 {ECO:0000313|EMBL:KGF80207.1, ECO:0000313|Proteomes:UP000029701};
RN [1] {ECO:0000313|EMBL:KGF80207.1, ECO:0000313|Proteomes:UP000029701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS1662 {ECO:0000313|EMBL:KGF80207.1,
RC ECO:0000313|Proteomes:UP000029701};
RA Fida T.T., Spain J.C.;
RT "Identification of Arachidin-3 degrading bacteria in the peanut
RT rhizosphere.";
RL Submitted (JUL-2014) 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:KGF80207.1}.
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DR EMBL; JPQD01000022; KGF80207.1; -; Genomic_DNA.
DR RefSeq; WP_036236561.1; NZ_JPQD01000022.1.
DR AlphaFoldDB; A0A098U7B6; -.
DR OrthoDB; 9758923at2; -.
DR Proteomes; UP000029701; 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:0000272; P:polysaccharide catabolic 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; ENDO-1,4-BETA-XYLANASE; 1.
DR PANTHER; PTHR43772:SF2; PUTATIVE (AFU_ORTHOLOGUE AFUA_2G04480)-RELATED; 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:ARBA00023277};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361187};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..460
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001949965"
FT DOMAIN 320..459
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 200
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 152
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 460 AA; 50822 MW; BC6FBEFD51299370 CRC64;
MNLRCITVAV AVCWGAGLPA FAENPIIQTS FTADPAPLVH GDTVYLYTSH DEDDAQGFKM
RDWKLYTSKD MVNWTDRGTV ADLSIFAWAN QDNDAWAPQV VERNGKFYLY APVTVGGSPR
NVIGVAVADS PLGPFKDPLG RPLIDRGEGY FDPTVLIDDD GQAYLYWGNP HLWYVKLDKD
MTSYSGKIER IDAKPGNYQE GPWVYKRNGK YYLAYASTCC SEGIGYAMSD TPTGPWEYKG
QIMEPTTEST GNHPGIVDFR GKSYVFGFSY RLNFADTPLH RERRSVSVTD FSYRPDGTIP
TQPFWNQAGV QQVQPLSPYQ RVEAETIAWE SRVKRDWDRP FDWVAGVRTA RDPRTGMYVY
PVGARAYVKV AGVDFGARGP RTFKASVASA GAGGHLDVRV GSPQGALVAS VDVPATGGPG
AWKEMAVPAS AVAGVQDVYV VFNAGGRHVS FNVDYWQFEQ
//