ID A0A0V8J4I2_9BACI Unreviewed; 610 AA.
AC A0A0V8J4I2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=CBM6 domain-containing protein {ECO:0000259|PROSITE:PS51175};
GN ORFNames=AS030_17490 {ECO:0000313|EMBL:KSU82066.1};
OS Fictibacillus enclensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Fictibacillus.
OX NCBI_TaxID=1017270 {ECO:0000313|EMBL:KSU82066.1, ECO:0000313|Proteomes:UP000054099};
RN [1] {ECO:0000313|EMBL:KSU82066.1, ECO:0000313|Proteomes:UP000054099}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIO-1003 {ECO:0000313|EMBL:KSU82066.1,
RC ECO:0000313|Proteomes:UP000054099};
RX PubMed=24343101; DOI=10.1007/s10482-013-0097-9;
RA Dastager S.G., Mawlankar R., Srinivasan K., Tang S.K., Lee J.C.,
RA Ramana V.V., Shouche Y.S.;
RT "Fictibacillus enclensis sp. nov., isolated from marine sediment.";
RL Antonie Van Leeuwenhoek 105:461-469(2014).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865}.
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:KSU82066.1}.
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DR EMBL; LNQN01000005; KSU82066.1; -; Genomic_DNA.
DR RefSeq; WP_061973991.1; NZ_KQ758619.1.
DR AlphaFoldDB; A0A0V8J4I2; -.
DR OrthoDB; 177947at2; -.
DR Proteomes; UP000054099; 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:InterPro.
DR CDD; cd18820; GH43_LbAraf43-like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
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; PTHR43817; GLYCOSYL HYDROLASE; 1.
DR PANTHER; PTHR43817:SF1; HYDROLASE, FAMILY 43, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G01660)-RELATED; 1.
DR Pfam; PF16990; CBM_35; 2.
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; 2.
DR PROSITE; PS51175; CBM6; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000054099};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..610
FT /note="CBM6 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039668656"
FT DOMAIN 364..482
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT ACT_SITE 46
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 224
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 162
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 610 AA; 67615 MW; F8D837331E32DE57 CRC64;
MKIRKMYAFT LGLLIVAFLF PSPSSASAPS TEMKLFKNPV VGDGADPWVV KHTDGYYYYM
QTTGNNLTIR KSKTLTGLDD AEKKVVWTPD SGAENSGNIW APELHFLDGR WYIYFAAGDG
NMGKQRMYVL ESEGSDPLGK YSYPKGTKLG KISDPSDKWA IDGTVFEYKN KRYFVWSGWE
GDENVSQQIY IAPMKNPWTI SGERVELSRP ELPWEKNGTP LINEGPEILK NKQGDVFIVY
SASGSWTDDY CLGMLKLTGK DPLKAGDWAK NPEPVFKSSP ADNVYGPGHN SIVKSPDGKE
DWIVYHAAKF KGAGWNRNVR IQEFTWKADG TPNFGTPLPA DTMLRAPSGE DGGKLVPALP
GKVYSYEAEN GVVNHATIVN NTSASGGSKV GMIDYNDSFV EFKVDAAPGD YTLKVRYSNG
MGETSTHVLA LNGKSLGEAA YPSYGWDTWR DAEQEVHLNA GENKIKLSKG TLFAEIDRID
LVPKKTKVFQ YEAELGYLKN AKVVNEYDAA NHQAVGLMSA HNSSVRFPIS VEKSGTYEMN
IRYKQPKGIN AVQVLHVNGK KSLILYKGEG SDKWKETAVK VKLKKGKNDI SFSKSRGAVD
LDYFTLNQTK
//
