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Database: UniProt
Entry: E6K3N0_9BACT
LinkDB: E6K3N0_9BACT
Original site: E6K3N0_9BACT 
ID   E6K3N0_9BACT            Unreviewed;       346 AA.
AC   E6K3N0;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Glycosyl hydrolase, family 43 {ECO:0000313|EMBL:EFU31798.1};
DE            EC=3.2.1.99 {ECO:0000313|EMBL:EFU31798.1};
GN   ORFNames=HMPREF6485_0183 {ECO:0000313|EMBL:EFU31798.1};
OS   Segatella buccae ATCC 33574.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Segatella.
OX   NCBI_TaxID=873513 {ECO:0000313|EMBL:EFU31798.1, ECO:0000313|Proteomes:UP000003112};
RN   [1] {ECO:0000313|EMBL:EFU31798.1, ECO:0000313|Proteomes:UP000003112}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33574 {ECO:0000313|EMBL:EFU31798.1,
RC   ECO:0000313|Proteomes:UP000003112};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA   Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA   Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA   Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA   Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA   Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA   Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC       {ECO:0000256|ARBA:ARBA00004834, ECO:0000256|PIRNR:PIRNR026534}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC       {ECO:0000256|ARBA:ARBA00009865, ECO:0000256|PIRNR:PIRNR026534}.
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:EFU31798.1}.
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DR   EMBL; AEPD01000006; EFU31798.1; -; Genomic_DNA.
DR   RefSeq; WP_004344058.1; NZ_GL586311.1.
DR   AlphaFoldDB; E6K3N0; -.
DR   STRING; 873513.HMPREF6485_0183; -.
DR   eggNOG; COG3507; Bacteria.
DR   HOGENOM; CLU_009397_5_1_10; -.
DR   UniPathway; UPA00667; -.
DR   Proteomes; UP000003112; Unassembled WGS sequence.
DR   GO; GO:0046558; F:arabinan endo-1,5-alpha-L-arabinosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0031222; P:arabinan catabolic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR006710; Glyco_hydro_43.
DR   InterPro; IPR016840; Glyco_hydro_43_endo_a_Ara-ase.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
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   PIRSF; PIRSF026534; Endo_alpha-L-arabinosidase; 1.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PIRNR:PIRNR026534};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR026534};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003112};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..346
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003206844"
FT   ACT_SITE        41
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR026534-1"
FT   ACT_SITE        227
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR026534-1"
FT   BINDING         41
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR026534-2"
FT   BINDING         119
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR026534-2"
FT   BINDING         156..159
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR026534-2"
FT   BINDING         176..178
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR026534-2"
FT   SITE            159
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:PIRSR026534-3"
FT   SITE            298
FT                   /note="Important for substrate recognition"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR026534-3"
SQ   SEQUENCE   346 AA;  38954 MW;  074C9CCA9442EF8A CRC64;
     MKRPLFLMLF FAATAITLAQ PDGRSHGGFD TFVTDTPMVH DPVMAFENGR YYLFSTGHGI
     RQMVSSDRRS WTVSRHPALD SIPAWTRDSV PGFAIHVWAP DIIRWHGRWW MAYSCSTFGK
     NTSAIGLMSR SSLSDSVGWK DEGPLVCSRE GRDNWNAIDP NFIIDEHDRP WLVWGSFWDG
     IQLVRLDSTL HIASGEHPHT IARRYAPSST AQEKNPTSEY AGPNAIEAPF IFRHGGYYYL
     FVSWDYCCRG TQSSYRVAVG RSKTIEGPYI DESGRDMLQG GGTVLVEGDK KTFEALGHCA
     AYHFADGDLF ICHGYSVEKQ GTSVLVQRRM EWKILADGTD WPVLVP
//
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