ID A0A0A6UK68_ACTUT Unreviewed; 495 AA.
AC A0A0A6UK68;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=non-reducing end alpha-L-arabinofuranosidase {ECO:0000256|ARBA:ARBA00012670};
DE EC=3.2.1.55 {ECO:0000256|ARBA:ARBA00012670};
GN ORFNames=MB27_20415 {ECO:0000313|EMBL:KHD75811.1};
OS Actinoplanes utahensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=1869 {ECO:0000313|EMBL:KHD75811.1, ECO:0000313|Proteomes:UP000054537};
RN [1] {ECO:0000313|EMBL:KHD75811.1, ECO:0000313|Proteomes:UP000054537}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 12052 {ECO:0000313|EMBL:KHD75811.1,
RC ECO:0000313|Proteomes:UP000054537};
RA Velasco-Bucheli B., del Cerro C., Hormigo D., Garcia J.L., Acebal C.,
RA Arroyo M., de la Mata I.;
RT "Draft genome sequence of Actinoplanes utahensis NRRL 12052.";
RL Submitted (OCT-2014) 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:KHD75811.1}.
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DR EMBL; JRTT01000023; KHD75811.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A6UK68; -.
DR STRING; 1869.MB27_20415; -.
DR eggNOG; COG3693; Bacteria.
DR Proteomes; UP000054537; 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:UP000054537};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..495
FT /note="non-reducing end alpha-L-arabinofuranosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039506929"
FT DOMAIN 43..178
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
SQ SEQUENCE 495 AA; 53253 MW; 2CE388303160B58A CRC64;
MTPTRTRRRT WRTALAAMVL LTGGAAVAVT ATAASAATID TNASYVLVNR TSGKALDVYN
LSTSDGARIT QWTRNDQAQQ QWQFVDSGGG FYRLKSKHSG KVLDVYNLST ADGGAIVQWT
DNNTTNQQFS VQDVDGYIQL INRNSGKAVE VQGASTADGA NIVQYSDWNG ANQQWQLVKV
GGSTPTTSPT SGGSCTLPSS YRWSSTGVLA NPKAGWVALK DFTHAPYNGK QLVYATTHDN
GTSWGSMNFG TFTNWSEMGS ASQNGMNFSA VAPSLFYFAP KNIWVLAYQW GGPAFSYRTS
SDPTNPNGWS APQTLFTGSI TGSGTGPIDQ TLIADSQNMY LFFAGDNGKI YRASMPIGNF
PGNFGSSYTT IMSDTTNNLF EAPQVYKVKG QNQYLMIVEA IGANGRYFRS FTATSLNGSW
TPQAATEGNP FAGKANSGAT WTNDISHGEL IRSSADQTMT IDPCNLQLLY QGRSPNSGGD
YGLLPYRPGV LTLQR
//
