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Database: UniProt
Entry: A0A1V2QSP8_9PSEU
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ID   A0A1V2QSP8_9PSEU        Unreviewed;       446 AA.
AC   A0A1V2QSP8;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=acetylxylan esterase {ECO:0000256|ARBA:ARBA00013092};
DE            EC=3.1.1.72 {ECO:0000256|ARBA:ARBA00013092};
GN   ORFNames=ALI22I_09470 {ECO:0000313|EMBL:ONI91287.1};
OS   Saccharothrix sp. ALI-22-I.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharothrix.
OX   NCBI_TaxID=1933778 {ECO:0000313|EMBL:ONI91287.1, ECO:0000313|Proteomes:UP000188617};
RN   [1] {ECO:0000313|EMBL:ONI91287.1, ECO:0000313|Proteomes:UP000188617}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ALI-22-I {ECO:0000313|EMBL:ONI91287.1,
RC   ECO:0000313|Proteomes:UP000188617};
RX   PubMed=28087533;
RA   Yeager C.M., Gallegos-Graves V., Dunbar J., Hesse C.N., Daligault H.,
RA   Kuske C.R.;
RT   "Polysaccharide degradation capability of Actinomycetales soil isolates
RT   from a semi-arid grassland of the Colorado Plateau.";
RL   Appl. Environ. Microbiol. 0:0-0(2017).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Deacetylation of xylans and xylo-oligosaccharides.;
CC         EC=3.1.1.72; Evidence={ECO:0000256|ARBA:ARBA00001691};
CC   -!- PATHWAY: Glycan degradation; xylan degradation.
CC       {ECO:0000256|ARBA:ARBA00004851}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SIMILARITY: Belongs to the carbohydrate esterase 1 (CE1) family. AxeA
CC       subfamily. {ECO:0000256|ARBA:ARBA00007052}.
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:ONI91287.1}.
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DR   EMBL; MTQP01000048; ONI91287.1; -; Genomic_DNA.
DR   RefSeq; WP_077005091.1; NZ_MTQP01000048.1.
DR   AlphaFoldDB; A0A1V2QSP8; -.
DR   STRING; 1933778.ALI22I_09470; -.
DR   OrthoDB; 9767239at2; -.
DR   Proteomes; UP000188617; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd00161; RICIN; 1.
DR   Gene3D; 2.80.10.50; -; 3.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR010126; Esterase_phb.
DR   InterPro; IPR035992; Ricin_B-like_lectins.
DR   InterPro; IPR000772; Ricin_B_lectin.
DR   NCBIfam; TIGR01840; esterase_phb; 1.
DR   PANTHER; PTHR43037:SF6; CARBOXYLIC ESTER HYDROLASE; 1.
DR   PANTHER; PTHR43037; UNNAMED PRODUCT-RELATED; 1.
DR   Pfam; PF10503; Esterase_PHB; 1.
DR   Pfam; PF00652; Ricin_B_lectin; 1.
DR   SMART; SM00458; RICIN; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 2.
DR   SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR   PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023001};
KW   Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023001};
KW   Reference proteome {ECO:0000313|Proteomes:UP000188617};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           32..446
FT                   /note="acetylxylan esterase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013183244"
FT   DOMAIN          317..446
FT                   /note="Ricin B lectin"
FT                   /evidence="ECO:0000259|SMART:SM00458"
SQ   SEQUENCE   446 AA;  47323 MW;  EB52F0E707E8BC29 CRC64;
     MRRMLTTLLT MASLLSLVLG AALMSAGPAA AATLTRVTDF GANPTNLGMY VYVPDNVAPR
     PALLVLVHYC GGSADAIFNG NGRDFATAAD RYGYVVVVPE ATREGHCFDV STRAGLIRNG
     GSDSTGIMSM VGWTRQRYDV DPARIVVSGF SSGAMMTNVL AAQYPDVFAA ASAFSGVPAG
     CFATTNGSLW NSQCSSGNIV KTPQEWGNLA RSMYPGYTGS YPRMQLWHGD QDTTLAYRNF
     GEEIKQWTNL RGLSQTPSFT DRPQSSWTRT RYGDTGTRAT VEGISITGTG HTLPQAGMLA
     YAIAFLGLDG GGGGGATGPL RSVGAGKCLD VPNQSTTAGT RLQMWDCWNG PNQQWTSTTT
     QELAVYSTDS RRCLDAENAG TTAGTLVIIW TCHGGTNQKW RLNTDGSITG VQSGLCLEVT
     GGSTANGASA RLWTCNGQNN QKWNRV
//
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