ID D9T1N3_MICAI Unreviewed; 513 AA.
AC D9T1N3;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=non-reducing end alpha-L-arabinofuranosidase {ECO:0000256|ARBA:ARBA00012670};
DE EC=3.2.1.55 {ECO:0000256|ARBA:ARBA00012670};
GN OrderedLocusNames=Micau_5990 {ECO:0000313|EMBL:ADL49492.1};
OS Micromonospora aurantiaca (strain ATCC 27029 / DSM 43813 / BCRC 12538 / CBS
OS 129.76 / JCM 10878 / NBRC 16125 / NRRL B-16091 / INA 9442).
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=644283 {ECO:0000313|EMBL:ADL49492.1, ECO:0000313|Proteomes:UP000001908};
RN [1] {ECO:0000313|EMBL:ADL49492.1, ECO:0000313|Proteomes:UP000001908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27029 / DSM 43813 / JCM 10878 / NBRC 16125 / INA 9442
RC {ECO:0000313|Proteomes:UP000001908};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA Hirsch A.M., Woyke T.;
RT "Complete sequence of Micromonospora aurantiaca ATCC 27029.";
RL Submitted (AUG-2010) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002162; ADL49492.1; -; Genomic_DNA.
DR RefSeq; WP_013289089.1; NC_014391.1.
DR AlphaFoldDB; D9T1N3; -.
DR STRING; 644283.Micau_5990; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GH62; Glycoside Hydrolase Family 62.
DR KEGG; mau:Micau_5990; -.
DR eggNOG; COG3693; Bacteria.
DR HOGENOM; CLU_041805_2_0_11; -.
DR OrthoDB; 4241492at2; -.
DR Proteomes; UP000001908; Chromosome.
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 InterPro; IPR006311; TAT_signal.
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.
DR PROSITE; PS51318; TAT; 1.
PE 4: Predicted;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00022651};
KW Glycosidase {ECO:0000313|EMBL:ADL49492.1};
KW Hydrolase {ECO:0000313|EMBL:ADL49492.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651};
KW Reference proteome {ECO:0000313|Proteomes:UP000001908};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT DOMAIN 54..190
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
SQ SEQUENCE 513 AA; 55264 MW; 57F1F2C49D875E3F CRC64;
MFAFGRSPST VSPPRRRGWL PRVVATGAAA VLVGAGAVAV VSAPAAAASV DTNAWYVLVN
RNSGKALDVY NLATNDGARI VQWSRNNGNQ QQWQFVDSGG GYYRLKSRLS GKVLDVYNWS
TANGGSIVQW SDLNGTNQQF RLADSDSGYV RLISRHSNKV VEVQGASTAD GGNIVQYDDW
NGANQQWQLV RVDGGGGNPT TPPPTTPPPG GTCNLPSSYR WSSTGALAQP RSGWVSLKDF
TVVPYNGQHL VYATTHDTGS SWGSMNFGLF SNWSQMASAS QNAMSSGTVA PTLFYFAPRN
IWVLAYQWGP TAFSYRTSND PTNPNGWSSA QPLFTGSISG SGTGPIDQTL IADDQNMYLF
FAGDNGKIYR SSMPLGNFPG SFGSTYTTIM SDSTNNLFEA VQVYKLQGQT RYLMIVEAIG
SQGRYFRSFT ATSLNGAWTP QAATESNPFA GKANSGATWT NDISHGELIR TTADQTFTVD
PCNLQLLYQG RSPNSGGDYG LLPYRPGLLT LQR
//
