ID A0A402D4X6_9BACT Unreviewed; 471 AA.
AC A0A402D4X6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=Ricin B lectin domain-containing protein {ECO:0000259|Pfam:PF14200};
GN ORFNames=CCAX7_39750 {ECO:0000313|EMBL:BDI31924.1}, CCAX7_57940
GN {ECO:0000313|EMBL:GCE57280.1};
OS Capsulimonas corticalis.
OC Bacteria; Armatimonadota; Armatimonadia; Capsulimonadales;
OC Capsulimonadaceae; Capsulimonas.
OX NCBI_TaxID=2219043 {ECO:0000313|EMBL:GCE57280.1};
RN [1] {ECO:0000313|EMBL:GCE57280.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX-7 {ECO:0000313|EMBL:GCE57280.1};
RA Li J., Tonouchi A.;
RT "Draft Genome Sequence of Capsulimonas corticalis strain AX-7.";
RL Int. J. Syst. Evol. Microbiol. 0:0-0(2018).
RN [2] {ECO:0000313|EMBL:BDI31924.1, ECO:0000313|Proteomes:UP000287394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX-7 {ECO:0000313|EMBL:BDI31924.1,
RC ECO:0000313|Proteomes:UP000287394};
RA Li J., Kudo C., Tonouchi A.;
RT "Capsulimonas corticalis gen. nov., sp. nov., an aerobic capsulated
RT bacterium, of a novel bacterial order, Capsulimonadales ord. nov., of the
RT class Armatimonadia of the phylum Armatimonadetes.";
RL Int. J. Syst. Evol. Microbiol. 69:220-226(2019).
RN [3] {ECO:0000313|EMBL:BDI31924.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AX-7 {ECO:0000313|EMBL:BDI31924.1};
RA Li J., Tonouchi A.;
RL Submitted (MAY-2022) 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; AP025739; BDI31924.1; -; Genomic_DNA.
DR EMBL; BHFQ01000023; GCE57280.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A402D4X6; -.
DR KEGG; ccot:CCAX7_39750; -.
DR InParanoid; A0A402D4X6; -.
DR Proteomes; UP000287394; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 CDD; cd00161; RICIN; 1.
DR Gene3D; 2.80.10.50; -; 2.
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; 2.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|RuleBase:RU361187};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000287394};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 327..405
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|Pfam:PF14200"
FT DOMAIN 411..468
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|Pfam:PF14200"
FT ACT_SITE 55
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT ACT_SITE 220
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR606710-1"
FT SITE 171
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; 50399 MW; 6988E49781CF924B CRC64;
MNAISGYVNE AIEGISRHCC GKSIRRAATV LVLLMTAAFA CGGAWAMEGD DGIFDPSTIV
KVGSTYHVFG DGQGITHKTS TDLVNWTTVS SIFGSGNGPS WIQSYVSGFS GYFWAPDLIY
MGGKYYLYYS CSTFGSKVSV IGVATSSDLS TWTDQGVVVS SNSSSAYNAI DPSMFKDASG
NYWITWGSWN NGIYDAQLNA STGKLLNSTK YNIVNISDAE ASYMVYHGGY YYVFYNRGSC
CNGTSSTYYV SVARSTSPSG GFTGNTVFIG SSSPCIGPGH FGYLNDGGAE YASYHYVDAN
SNGYPRLAVS HLTWSSGWPY MSPDWIANGT YKVTSQANGL AWDDWGCTGV SGQAVAQNTY
TGLNCQQWVF HQLGWGIYEI TCANGGLALD ALNCSNANGT ALDLYAYWAG TCQQYKIYRA
SDGSYVLATM NGSGNGTSVI DVPGSSSTKG LQLDLWAYNG GSNQKWYIAA P
//
