ID   A0A1H8WAS9_9SPHI        Unreviewed;       482 AA.
AC   A0A1H8WAS9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Arabinan endo-1,5-alpha-L-arabinosidase {ECO:0000313|EMBL:SEP24719.1};
GN   ORFNames=SAMN05428947_10971 {ECO:0000313|EMBL:SEP24719.1};
OS   Mucilaginibacter sp. OK283.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Mucilaginibacter.
OX   NCBI_TaxID=1881049 {ECO:0000313|EMBL:SEP24719.1, ECO:0000313|Proteomes:UP000199509};
RN   [1] {ECO:0000313|EMBL:SEP24719.1, ECO:0000313|Proteomes:UP000199509}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OK283 {ECO:0000313|EMBL:SEP24719.1,
RC   ECO:0000313|Proteomes:UP000199509};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC       {ECO:0000256|ARBA:ARBA00004834}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC       {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|RuleBase:RU361187}.
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DR   EMBL; FODR01000009; SEP24719.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H8WAS9; -.
DR   STRING; 1881049.SAMN05428947_10971; -.
DR   OrthoDB; 9801455at2; -.
DR   Proteomes; UP000199509; 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:InterPro.
DR   CDD; cd08998; GH43_Arb43a-like; 1.
DR   Gene3D; 2.80.10.50; -; 1.
DR   InterPro; IPR006710; Glyco_hydro_43.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   InterPro; IPR035992; Ricin_B-like_lectins.
DR   InterPro; IPR000772; Ricin_B_lectin.
DR   PANTHER; PTHR43301; ARABINAN ENDO-1,5-ALPHA-L-ARABINOSIDASE; 1.
DR   PANTHER; PTHR43301:SF3; ARABINOSIDASE-RELATED; 1.
DR   Pfam; PF04616; Glyco_hydro_43; 1.
DR   Pfam; PF14200; RicinB_lectin_2; 1.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR   SUPFAM; SSF50370; Ricin B-like lectins; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|RuleBase:RU361187};
KW   Hydrolase {ECO:0000256|RuleBase:RU361187};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..482
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011715049"
FT   DOMAIN          376..444
FT                   /note="Ricin B lectin"
FT                   /evidence="ECO:0000259|Pfam:PF14200"
FT   SITE            139
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   482 AA;  52043 MW;  C686B2E73F3B5E62 CRC64;
     MKLIVKVLST ISLFSLLLAP QANAQVGKPF IHDPSTIAEC DGKYYTFGTF GGGLISEDGW
     TWNGGGVRPG GGAAPDVLKI GDRYLIVYGA TGGGLAGGHN GTILTMWNKS LDPKSPDFKY
     SEPVKVASSD GIEDCDAIDP GLLLDPTDGR LWLSYGTYFG YIRLVELDPK TGKRVEGNKA
     LNIAIDCEAT DLLYRDGWYY LLGTHGTCCD GPNSTYNIVV GRSRKVTGPY LDNIGRDMLK
     GGGKMVVAAG DRLVGPGHFG RIIVGDGVEK MSCHYEADLD QSGRSVLGIR PLLWKNGWPV
     AGDNCKEGTY EIESERRGYA LELGVDFTRM PGGMRFNRNN DEPVKPVPSQ ELADVVSGWP
     AGNIGVRISD YMFRPHQKWA ISSVPGAGGY LGGPYYKIVI AGTDRALAAT AEAELVTVPT
     FTGAPEQLWR IDQLTDGTYR IMPKVVPNSG EQLALVSSGD STPTLARFDM NSDNSKWNLR
     TH
//