ID A0A0C1R755_9CYAN Unreviewed; 471 AA.
AC A0A0C1R755;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 28-JUN-2023, entry version 23.
DE RecName: Full=CBM6 domain-containing protein {ECO:0000259|PROSITE:PS51175};
GN ORFNames=DA73_0244140 {ECO:0000313|EMBL:KIE08185.1};
OS Tolypothrix bouteillei VB521301.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC Tolypothrix.
OX NCBI_TaxID=1479485 {ECO:0000313|EMBL:KIE08185.1};
RN [1] {ECO:0000313|EMBL:KIE08185.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VB521301 {ECO:0000313|EMBL:KIE08185.1};
RX PubMed=25700407;
RA Chandrababunaidu M.M., Singh D., Sen D., Bhan S., Das S., Gupta A.,
RA Adhikary S.P., Tripathy S.;
RT "Draft Genome Sequence of Tolypothrix boutellei Strain VB521301.";
RL Genome Announc. 3:e00001-15(2015).
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:KIE08185.1}.
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DR EMBL; JHEG02000059; KIE08185.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C1R755; -.
DR STRING; 1479485.DA73_0244140; -.
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:InterPro.
DR CDD; cd18820; GH43_LbAraf43-like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
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; PTHR43817; GLYCOSYL HYDROLASE; 1.
DR PANTHER; PTHR43817:SF1; HYDROLASE, FAMILY 43, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G01660)-RELATED; 1.
DR Pfam; PF16990; CBM_35; 1.
DR Pfam; PF04616; Glyco_hydro_43; 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 Glycosidase {ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|RuleBase:RU361187}.
FT DOMAIN 346..468
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
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; 52564 MW; 2B91FB85C034DC49 CRC64;
MFGVIGPGNL IFSANSSLAI KNSFARSPTF NFYNVLTSSG ADPWVYKHTD GYYYMTYLTN
QNITIFRSLT LSGIVGGERK TVWTPPKSGS NSQNIWAPEL HFLDGKWYIY YTADDGNTLN
HRMFVLENAS PDPFRGNFVD RGKIFDKKND KWAIDGTVLT VSGKRYFIWS GWEGDNNVQQ
NLYIAPMSNP TTLGSSRVKI SSPTYPWESF GSPPTVNEGP QVIIKDKTIN LIYSASVGWT
NNYALGLLTA KVGSNLLSPS AWRKYKEPVF QSGNGVVSPG HSSFVKSPNN KEDWIVYHAA
NFLSAGWNRH IRTQRFGWNR DGTPNFGSPA PVNAPISLPS GEPQHDRYQA EDALFTGAAK
IISNPNASNG AKVGYIDNPQ SNVEFRVRVN KRGTYNMSVR FGNGTEGGKE ASHKLYINGK
ELPALRYVWT GWDNWLNSVI RVQLNTGVNQ IRFSKGENFA EIDSIDIFPL R
//
