ID A0A1W6E8D9_9BACT Unreviewed; 483 AA.
AC A0A1W6E8D9;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Glycoside hydrolase {ECO:0000313|EMBL:ARK11709.1};
GN ORFNames=A6C57_15995 {ECO:0000313|EMBL:ARK11709.1};
OS Fibrella sp. ES10-3-2-2.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Fibrella.
OX NCBI_TaxID=1834519 {ECO:0000313|EMBL:ARK11709.1, ECO:0000313|Proteomes:UP000193660};
RN [1] {ECO:0000313|Proteomes:UP000193660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ES10-3-2-2 {ECO:0000313|Proteomes:UP000193660};
RA Kim M.K., Srinivasan S., Kim E.B., Kim K.S.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC {ECO:0000256|ARBA:ARBA00004834}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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DR EMBL; CP015317; ARK11709.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W6E8D9; -.
DR STRING; 1834519.A6C57_15995; -.
DR KEGG; fib:A6C57_15995; -.
DR OrthoDB; 9801455at2; -.
DR Proteomes; UP000193660; Chromosome.
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; cd08998; GH43_Arb43a-like; 1.
DR Gene3D; 2.80.10.50; -; 1.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR PANTHER; PTHR43301; ARABINAN ENDO-1,5-ALPHA-L-ARABINOSIDASE; 1.
DR PANTHER; PTHR43301:SF3; ARABINOSIDASE-RELATED; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR Pfam; PF14200; RicinB_lectin_2; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|RuleBase:RU361187, ECO:0000313|EMBL:ARK11709.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000193660};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..483
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010879725"
FT DOMAIN 377..445
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|Pfam:PF14200"
FT REGION 334..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 33
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 188
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 139
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 483 AA; 52191 MW; 20A71EA57E6FCD40 CRC64;
MKVRSTLLGA IALLSVWLTG TVHAQIGKPF IHDPSTIQEC EGKYYTFGTG RGGLISEDGW
TWNGGAERPG GGAAPDVLKI GDRYLVVYGA TGGGLGGGHN GRILTMWNKT LDPKSPDFKY
SEAIVVASSD GVEDNDAIDP GLLLDPTDGR LWVSYGTYFG FIRLVELDPK TGKRVEGNNA
INIAIDCEAT DLMYKDGWYY LLGTHGTCCD GANSTYNIVV GRSRKVTGPY LDNVGRDMLK
GGGKMVLAAG GRVNGPGHFG RIVIGDGVEK MSCHYEADLD QSGRSVLGIR PLLWKNGWPV
AGDNFNEGTY EIESERRGYA LELAVDFTRM PVAPRGANRN NDEPVKPVPS QGLSDVIKTW
PTGTIGVRIG DYMFRPHQKW TITIVPGAGG YLGAPYYKIL IAGTERALAA TADAEVISVP
TFTGAPEQLW RIEQLVDGTY RIMPKVVPNS KEDLVLVSSG DSTPTLSTFD MTSDNSKWNF
KAH
//
