ID A0A0A0B4H2_9CELL Unreviewed; 454 AA.
AC A0A0A0B4H2;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=non-reducing end alpha-L-arabinofuranosidase {ECO:0000256|ARBA:ARBA00012670};
DE EC=3.2.1.55 {ECO:0000256|ARBA:ARBA00012670};
DE Flags: Fragment;
GN ORFNames=Q760_03900 {ECO:0000313|EMBL:KGM01073.1};
OS Cellulomonas cellasea DSM 20118.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=1408250 {ECO:0000313|EMBL:KGM01073.1, ECO:0000313|Proteomes:UP000029833};
RN [1] {ECO:0000313|EMBL:KGM01073.1, ECO:0000313|Proteomes:UP000029833}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20118 {ECO:0000313|EMBL:KGM01073.1,
RC ECO:0000313|Proteomes:UP000029833};
RA Wang G., Zhuang W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside
CC residues in alpha-L-arabinosides.; EC=3.2.1.55;
CC Evidence={ECO:0000256|ARBA:ARBA00001462};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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:KGM01073.1}.
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DR EMBL; AXNT01000136; KGM01073.1; -; Genomic_DNA.
DR RefSeq; WP_034633714.1; NZ_AXNT01000136.1.
DR AlphaFoldDB; A0A0A0B4H2; -.
DR STRING; 1408250.Q760_03900; -.
DR OrthoDB; 4241492at2; -.
DR Proteomes; UP000029833; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046373; P:L-arabinose metabolic process; IEA:InterPro.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR CDD; cd08987; GH62; 1.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.80.10.50; -; 3.
DR InterPro; IPR005193; GH62_arabinosidase.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR PANTHER; PTHR40631; ALPHA-L-ARABINOFURANOSIDASE AXHA-2-RELATED; 1.
DR PANTHER; PTHR40631:SF1; ALPHA-L-ARABINOFURANOSIDASE AXHA-2-RELATED; 1.
DR Pfam; PF03664; Glyco_hydro_62; 1.
DR Pfam; PF14200; RicinB_lectin_2; 2.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 4: Predicted;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00022651};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651};
KW Reference proteome {ECO:0000313|Proteomes:UP000029833};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT DOMAIN 1..129
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KGM01073.1"
SQ SEQUENCE 454 AA; 49060 MW; B33162FB63C8CEA3 CRC64;
GSGKALDVYN LSTADGARIT QWTRNDGAQQ QWQFVDAGDG YYRVKSRLSG KVLDVYNFST
ADGGAIVQYT DRNQTNQQFR LQDSAGGSVT LINRNSNKAV EVQGASTADG ANIVQYASWG
GANQQWLLVP VGGANPNPNP TPTTTTPAPN PGTCNLPSSY RWSSTGSLAT PRSGWASLKD
FTVAPYNGKQ LVYATTHDNG TSWGSMNFGL FTNYSEMASA SQNSMPFTAV APSLFYFAPK
NIWVMAYQWG GPAFSYRTST DPSNPNSWGP HQTLFSGSIT GSGTGPIDQT LIADDQNMYL
FFAGDNGKIY RSSMPLGNFP GSFGSSYQTI MTDTTNNLFE APQVYKLQGQ NRYLMIVEAI
GSQGRYFRSF TATSLGGTWT PQAATESNPF AGKANSGATW TNDISHGELL RVSADQTMTV
DPCNLRLLYQ GRSPSSGGDY GRLPYRPGLL TLQR
//
