ID D5BBA0_ZUNPS Unreviewed; 329 AA.
AC D5BBA0;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Alpha-N-arabinofuranosidase {ECO:0000313|EMBL:ADF54640.1};
GN OrderedLocusNames=ZPR_4338 {ECO:0000313|EMBL:ADF54640.1};
OS Zunongwangia profunda (strain DSM 18752 / CCTCC AB 206139 / SM-A87) (Wangia
OS profunda).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Zunongwangia.
OX NCBI_TaxID=655815 {ECO:0000313|EMBL:ADF54640.1, ECO:0000313|Proteomes:UP000001654};
RN [1] {ECO:0000313|EMBL:ADF54640.1, ECO:0000313|Proteomes:UP000001654}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18752 / CCTCC AB 206139 / SM-A87
RC {ECO:0000313|Proteomes:UP000001654};
RX PubMed=20398413; DOI=10.1186/1471-2164-11-247;
RA Qin Q.L., Zhang X.Y., Wang X.M., Liu G.M., Chen X.L., Xie B.B., Dang H.Y.,
RA Zhou B.C., Yu J., Zhang Y.Z.;
RT "The complete genome of Zunongwangia profunda SM-A87 reveals its adaptation
RT to the deep-sea environment and ecological role in sedimentary organic
RT nitrogen degradation.";
RL BMC Genomics 11:247-247(2010).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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DR EMBL; CP001650; ADF54640.1; -; Genomic_DNA.
DR AlphaFoldDB; D5BBA0; -.
DR STRING; 655815.ZPR_4338; -.
DR CAZy; GH43; Glycoside Hydrolase Family 43.
DR KEGG; zpr:ZPR_4338; -.
DR eggNOG; COG3940; Bacteria.
DR HOGENOM; CLU_009397_2_2_10; -.
DR Proteomes; UP000001654; Chromosome.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd18820; GH43_LbAraf43-like; 1.
DR InterPro; IPR016828; Alpha-L-arabinofuranosidase.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR43817; GLYCOSYL HYDROLASE; 1.
DR PANTHER; PTHR43817:SF1; HYDROLASE, FAMILY 43, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G01660)-RELATED; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR PIRSF; PIRSF025414; Alpha-L-arabinofuranosidase; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361187};
KW Hydrolase {ECO:0000256|RuleBase:RU361187}.
FT SITE 136
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 329 AA; 37563 MW; C9DDCB29DCF7C9F1 CRC64;
MVLVCGLSFA QQKTFTNPLL ASGADPYSTY HEGYYYYIHT QQNRLVLWKT KNLAHLKTAE
KTTIWTPPEN TMYSKELWAP EVHMIDGNWY VYFAADDGDN NNHRMYVLEN TSGNPMNNSW
KFKGKLATPS DKWAIDGNVF KHQGQLYMIW SGWEGDENGR QDLFIAKMKN PTTMEGKRQK
IATPTYDWET RWEGGPHVLV NEGPQYLSNG EEVFIVFSGS GCWTDYYTLG LLALKGEDLM
DPDNWEKHKK PIFAWSKENG VYAPGHNSFF KSPDGKEDWI LYHANDNSGD GCGGKRSPRM
QKISWNKDGT PNLGTPVSTN TILEIPSEE
//
