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Database: UniProt
Entry: A0A261QAH7_9BACT
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Original site: A0A261QAH7_9BACT 
ID   A0A261QAH7_9BACT        Unreviewed;       350 AA.
AC   A0A261QAH7;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 11.
DE   SubName: Full=Alpha-N-arabinofuranosidase {ECO:0000313|EMBL:OZI09427.1};
GN   ORFNames=BWI93_03985 {ECO:0000313|EMBL:OZI09427.1};
OS   Siphonobacter sp. BAB-5385.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae;
OC   Siphonobacter.
OX   NCBI_TaxID=1864822 {ECO:0000313|EMBL:OZI09427.1, ECO:0000313|Proteomes:UP000215802};
RN   [1] {ECO:0000313|EMBL:OZI09427.1, ECO:0000313|Proteomes:UP000215802}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BAB-5385 {ECO:0000313|EMBL:OZI09427.1,
RC   ECO:0000313|Proteomes:UP000215802};
RA   Dhebar S., Dhebar S., Bhargava P., Bagatharia S.B., Soni S., Joshi M.N.;
RT   "Draft genome of Siphonobacter sp. BAB-5385.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC       {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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:OZI09427.1}.
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DR   EMBL; NMPS01000042; OZI09427.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A261QAH7; -.
DR   OrthoDB; 3308423at2; -.
DR   Proteomes; UP000215802; Unassembled WGS sequence.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd18619; GH43_CoXyl43_like; 1.
DR   InterPro; IPR006710; Glyco_hydro_43.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   PANTHER; PTHR43772:SF2; BETA-1,4-XYLOSIDASE (EUROFUNG); 1.
DR   PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR   Pfam; PF04616; Glyco_hydro_43; 1.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361187};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361187};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651};
KW   Reference proteome {ECO:0000313|Proteomes:UP000215802};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..350
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012175834"
FT   SITE            164
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   350 AA;  39790 MW;  601BF34930035F2B CRC64;
     MQRVFKPLAL AAWMAASLTS FAQTNGGKNP ISQPLVSHIY TADPSAHVFN GKIYIYPSHD
     IDAENVKRDD DGGHFAMRDY HVLSMDKIGG PVKDHGVALD LKDVPWAGRQ LWAPDVAYKN
     GTYYLYFPAK DKQDIFRIGV ATSKSPTGPF KAEPEPIKGT YSIDPTVFQD TDGQAYLYFG
     GIWGGQLQRW DTNEYHPDGA LKKSEEVAYL PRVVRLNQDM KTLAEPVREI QLLDKNGKPF
     LEKDSDKRFF EGAWLHRYQG KYYFSYSTGD THNLCYAISD SPYGPFTYQG ILLKPVLGWT
     THHSIVEVNK KWYLFYHDVQ LSGKTHLRNV KVTELKYNPD GTIQTIDAYK
//
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